Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414 259 FTDPFFLVETLCIVWFTFELLVRFSACPSKPAFFRNIMNIIDLVAIFPYFITLGtelvqqqeqqpasggggqnGQQAMSL 338
Cdd:pfam00520  31 LTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRYFRSPWNILDFVVVLPSLISLV-------------------LSSVGSL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414 339 AILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVY---------FAEADDDDSLFPSI 409
Cdd:pfam00520  92 SGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYqlfggklktWENPDNGRTNFDNF 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579414 410 PDAFWWAVVTMTTVGYGDMYPMTVGGK-------IVGSLCAIAGVLTIALPVPVIVSNFNYFYHRE 468
Cdd:pfam00520 172 PNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414 259 FTDPFFLVETLCIVWFTFELLVRFSACPSKPAFFRNIMNIIDLVAIFPYFITLGtelvqqqeqqpasggggqnGQQAMSL 338
Cdd:pfam00520  31 LTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRYFRSPWNILDFVVVLPSLISLV-------------------LSSVGSL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414 339 AILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVY---------FAEADDDDSLFPSI 409
Cdd:pfam00520  92 SGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYqlfggklktWENPDNGRTNFDNF 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579414 410 PDAFWWAVVTMTTVGYGDMYPMTVGGK-------IVGSLCAIAGVLTIALPVPVIVSNFNYFYHRE 468
Cdd:pfam00520 172 PNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414   43 LVINISGLRFETQLRTLSLFPDTLLGDPGRRvRFFDPLRNEYFFDRNRPSFDAILYYYQSgGRLRRPVNvPLDIFLEEIR 122
Cdd:smart00225   2 VTLVVGGKKFHAHKAVLAAHSPYFKALFSSD-FKESDKSEIYLDDVSPEDFRALLNFLYT-GKLDLPEE-NVEELLELAD 78

                   ....
gi 1034579414  123 FYQL 126
Cdd:smart00225  79 YLQI 82

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A members 2 (KCNA2) and 3 (KCNA3); KCNA2 is also called NGK1, voltage-gated K(+) channel HuKIV, voltage-gated potassium channel HBK5, or voltage-gated potassium channel subunit Kv1.2. KCNA3 is also called HGK5, HLK3, HPCN3, voltage-gated K(+) channel HuKIII, or voltage-gated potassium channel subunit Kv1.3. KCNA2 and KCNA3 mediate transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNA2 primarily functions in the brain and the central nervous system, but also in the cardiovascular system. It prevents aberrant action potential firing and regulates neuronal output. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA2 and KCNA3 are alpha subunits that form functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  41 ERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEE 120
Cdd:cd18403     1 ERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSEE 80

                          90
                  ....*....|....*....
gi 1034579414 121 IRFYQLGDEALAAFREDEG 139
Cdd:cd18403    81 IRFYELGEEAMEMFREDEG 99

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNA/Kv1 subfamily of Shaker-type voltage-dependent potassium channels; Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv1, also known as subfamily A, contains eight alpha subunit members, Kv1.1 (KCNA1), Kv1.2 (KCNA2), Kv1.3 (KCNA3), Kv1.4 (KCNA4), Kv1.5 (KCNA5), Kv1.6 (KCNA6), Kv1.7 (KCNA7), and Kv1.8 (KCNA10), which are orthologs of the Shaker gene in Drosophila. They are delayed rectifiers except for Kv1.4 (KCNA4), which is an A-type potassium channel. Delayed rectifiers are slow opening and closing voltage-gated potassium channels. Because of their delayed activation kinetics, they play an important role in controlling action potential duration. A-type channels are fast/rapidly inactivating potassium channels. Kv1/KCNA subfamily alpha subunits form functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  41 ERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEE 120
Cdd:cd18377     1 ERVVINVSGLRFETQLKTLAQFPNTLLGDPNKRMRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEE 80

                  ....*
gi 1034579414 121 IRFYQ 125
Cdd:cd18377    81 IRFYE 85

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A member 5 (KCNA5); KCNA5, also called HPCN1, voltage-gated potassium channel HK2, or voltage-gated potassium channel subunit Kv1.5, mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNA5 may play a role in regulating the secretion of insulin in normal pancreatic islets. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA5 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  41 ERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEE 120
Cdd:cd18406     1 ERVIINIAGLRFETQLGTLNQFPDTLLGDPDKRMRYFDPLRNEYFFDRNRPSFDGILYFYQSGGKIRRPVNVSIDVFADE 80

                          90
                  ....*....|....*..
gi 1034579414 121 IRFYQLGDEALAAFRED 137
Cdd:cd18406    81 IRFYQLGEEAMERFRED 97

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily A member 1 (KCNA1); KCNA1 is also called voltage-gated K(+) channel HuKI, voltage-gated potassium channel HBK1, or voltage-gated potassium channel subunit Kv1.1. It mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the kidney. It is involved in the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNA1 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv1/KCNA alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  41 ERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEE 120
Cdd:cd18402     9 ERVVINIAGLRFETQLKTLAQFPNTLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEE 88

                          90
                  ....*....|
gi 1034579414 121 IRFYQLGDEA 130
Cdd:cd18402    89 IKFYELGEEA 98

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414 259 FTDPFFLVETLCIVWFTFELLVRFSACPSKPAFFRNIMNIIDLVAIFPYFITLGtelvqqqeqqpasggggqnGQQAMSL 338
Cdd:pfam00520  31 LTTVLEILDYVFTGIFTLEMLLKIIAAGFKKRYFRSPWNILDFVVVLPSLISLV-------------------LSSVGSL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414 339 AILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVY---------FAEADDDDSLFPSI 409
Cdd:pfam00520  92 SGLRVLRLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYqlfggklktWENPDNGRTNFDNF 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579414 410 PDAFWWAVVTMTTVGYGDMYPMTVGGK-------IVGSLCAIAGVLTIALPVPVIVSNFNYFYHRE 468
Cdd:pfam00520 172 PNAFLWLFQTMTTEGWGDIMYDTIDGKgefwayiYFVSFIILGGFLLLNLFIAVIIDNFQELTERT 237

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins; This family includes two protein groups: voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins. Kv channels are membrane proteins with fundamental physiological roles. They are responsible for a variety of electrical phenomena, such as the repolarization of the action potential, spike frequency adaptation, synaptic repolarization, and smooth muscle contraction. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels, and others. All family members contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  43 LVINISGLRFETQLRTLSLFPDTLLGDP--GRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLrRPVNVPLDIFLEE 120
Cdd:cd18187     1 VVLNVSGTRFVTNRQTLTRHPDTLLGRMfkPGREFTFPNETGEYFIDRDPTVFRTILNYYRTGKLN-CPDGISIPDLREE 79

                  ....
gi 1034579414 121 IRFY 124
Cdd:cd18187    80 CDFY 83

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCND/Kv4 subfamily of Shal-type voltage-dependent potassium channels; Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv4, also known as subfamily D, contains three alpha subunit members, Kv4.1 (KCND1), Kv4.2 (KCND2), and Kv4.3 (KCND3), which are orthologs of the Shal gene in Drosophila. They are A-type potassium channels that mediate the native, fast inactivating (A-type) K+ current (IA) described both in the nervous system (A currents) and the heart (transient outward current). Kv4/KCND subfamily alpha subunits form functional homo- or hetero-tetrameric channels through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. They are modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  42 RLVINISGLRFETQLRTLSLFPDTLLGDpGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSgGRLRRPVNVPLDIFLEEI 121
Cdd:cd18380     1 RIVINVSGRRFETWKNTLEKYPDTLLGS-TEKEFFYDDDTKEYFFDRDPEIFRHILNFYRT-GKLHYPRHECISAYDDEL 78

                          90
                  ....*....|.
gi 1034579414 122 RFYQLGDEALA 132
Cdd:cd18380    79 AFFGILPEIIG 89

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily D member 1 (KCND1); KCND1, also called voltage-gated potassium channel subunit Kv4.1, is a pore-forming subunit of voltage-gated rapidly inactivating A-type potassium channels. It may contribute to I (To) current in heart and I (Sa) current in neurons. Its properties are modulated by interactions with other alpha subunits and with regulatory subunits. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCND1 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv4/KCND alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. It is modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  41 ERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVrFFDPLRNEYFFDRNRPSFDAILYYYQSgGRLRRPVNVPLDIFLEE 120
Cdd:cd18417    35 EILVVNVSGRRFQTWKNTLDRYPDTLLGSSEKEF-FYNEDTQEYFFDRDPEMFRHILNFYRT-GRLHYPRHECIQAFDEE 112

                          90       100
                  ....*....|....*....|.
gi 1034579414 121 IRFYQL-----GDEALAAFRE 136
Cdd:cd18417   113 LSFYGIipeiiGDCCLEEYRD 133

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster potassium voltage-gated channel protein Shal and similar proteins; Drosophila melanogaster Shal, also called Shaker cognate l or Shal2, is a transient potassium current (I(A)) channel, which is required for maintaining excitability during repetitive firing and normal locomotion in Drosophila. It may play a role in the nervous system and in the regulation of beating frequency in pacemaker cells. Shal mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. Shal is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  41 ERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVrFFDPLRNEYFFDRNRPSFDAILYYYQSgGRLRRPVNVPLDIFLEE 120
Cdd:cd18420    36 EKLIINVSGRRFETWRNTLEKYPDTLLGSNEREF-FYDEETKEYFFDRDPDIFRHILNYYRT-GKLHYPKHECLTAYDEE 113

                  ....
gi 1034579414 121 IRFY 124
Cdd:cd18420   114 LAFF 117

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily D member 2 (KCND2); KCND2, also called voltage-gated potassium channel subunit Kv4.2, is a major pore-forming subunit in somatodendritic subthreshold A-type potassium current I(SA) channels. It mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCND2 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other Kv4/KCND alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. It is modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  43 LVINISGLRFETQLRTLSLFPDTLLGDPGRRVrFFDPLRNEYFFDRNRPSFDAILYYYQSgGRLRRPVNVPLDIFLEEIR 122
Cdd:cd18418     2 IVLNVSGTRFQTWRNTLERYPDTLLGSSERDF-FYHEETQEYFFDRDPDIFRHILNFYRT-GKLHYPRHECISAYDEELA 79

                  ....
gi 1034579414 123 FYQL 126
Cdd:cd18418    80 FFGI 83

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily C members KCNC1 and KCNC3; KCNC1 (also called NGK2, voltage-gated potassium channel subunit Kv3.1, or voltage-gated potassium channel subunit Kv4) and KCNC3 (also called KSHIIID or voltage-gated potassium channel subunit Kv3.3) play important roles in the rapid repolarization of fast-firing brain neurons. Assuming opened or closed conformations in response to the voltage difference across the membrane, the proteins form tetrameric potassium-selective channels through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNC1 and KCNC3 are alpha subunit that form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  41 ERLVINISGLRFETQLRTLSLFPDTLLG---DPGRRVRF-FDPLRNEYFFDRNRPSFDAILYYYQSgGRLRRPVNVPLDI 116
Cdd:cd18414     3 DRIVINVGGTRHETYRSTLRTLPGTRLAwlaEPDAHSNFdYDPRADEFFFDRHPGVFAHILNYYRT-GKLHCPADVCGPL 81

                          90
                  ....*....|...
gi 1034579414 117 FLEEIRFYQLgDE 129
Cdd:cd18414    82 YEEELAFWGI-DE 93

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414   43 LVINISGLRFETQLRTLSLFPDTLLGDPGRRvRFFDPLRNEYFFDRNRPSFDAILYYYQSgGRLRRPVNvPLDIFLEEIR 122
Cdd:smart00225   2 VTLVVGGKKFHAHKAVLAAHSPYFKALFSSD-FKESDKSEIYLDDVSPEDFRALLNFLYT-GKLDLPEE-NVEELLELAD 78

                   ....
gi 1034579414  123 FYQL 126
Cdd:smart00225  79 YLQI 82

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily; Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  44 VINISGLRFETQLRTLSLFPDTLLGDPgrRVRFFDPLRNEYFFDR-NRPSFDAILYYYQSGGRLRRPVNVplDIFLEEIR 122
Cdd:cd01165     2 VLVVEGEKFHVNKELLAQSSEYFRALF--RGGFRESGQAEINLRDiSPEDFRALLEFLYGGKRDLDASNL--LELLEAAN 77

                  ..
gi 1034579414 123 FY 124
Cdd:cd01165    78 FL 79

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster potassium voltage-gated channel protein Shab and similar proteins; Shab is a slow delayed rectifier voltage-gated potassium channel in Drosophila. It mediates transmembrane potassium transport in excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. Shab is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034579414  42 RLVINISGLRFETQLRTLSLFPDTLLGdpgrRVRF-------------FDPLRNEYFFDRNRPSFDAILYYYQSG 103
Cdd:cd18413     3 RVVINVGGVKHEVLWRTLDRMPHTRLG----KLRDsntheaivelcddYSLADNEYFFDRHPRSFASILNFYRTG 73

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily V member 2 (KCNV2); KCNV2, also called voltage-gated potassium channel subunit Kv8.2, is a modulatory voltage-gated potassium channel alpha subunit that modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. KCNV2 is essential for visual function and cone survival. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNV2 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  43 LVINISGLRFETQLRTLSLFPDTLLG------DPGRRVRFFD---PLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVP 113
Cdd:cd18425     1 LNINVGGTSYQISYRVAASYPKTRIGrlatytDRSRKLDLCDdynVQNDEYFFDRDPAVFHHIYNFYRTGVLWVKDELCP 80

                          90
                  ....*....|.
gi 1034579414 114 LDiFLEEIRFY 124
Cdd:cd18425    81 RN-FLEEINYW 90

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins, KCTD1 and KCTD15; This subfamily of KCTD proteins includes KCTD1 and KCTD15. KCTD1 is a nuclear BTB/POZ domain-containing protein that acts as a transcriptional repressor and mediates protein-protein interactions through a BTB domain. It represses the transcriptional activity of AP-2 family members, including TFAP2A, TFAP2B and TFAP2C. It also functions as a novel inhibitor of the Wnt signaling pathway. Mutations in KCTD1 cause scalp-ear-nipple (SEN) syndrome. KCTD15 is a BTB/POZ domain-containing protein that plays a role in the regulation of neural crest (NC) formation and other steps in embryonic development. It inhibits AP2 transcriptional activity by interaction with its activation domain. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. The KCTD1 BTB domains form pentamers.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  45 INISGLRFETQLRTLSLFPDTLLGdpgrrvRFF--------DPLRNEYFFDRNRPSFDAILYYYQSgGRLRRPVNVP-LD 115
Cdd:cd18361     3 IDVGGHIYTSSLETLTKYPESRLG------KLFngsipivlDSLKQHYFIDRDGKMFRHILNFLRT-SKLLLPDDFTeFD 75

                          90
                  ....*....|.
gi 1034579414 116 IFLEEIRFYQL 126
Cdd:cd18361    76 LLYEEARYYEL 86

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily B member 1 (KCNB1); KCNB1, also called delayed rectifier potassium channel 1 (DRK1) or voltage-gated potassium channel subunit Kv2.1, mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNB1 is involved in the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNB1 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034579414  42 RLVINISGLRFETQLRTLSLFPDTLLGDPgRRVRFFDPL----------RNEYFFDRNRPSFDAILYYYQSG 103
Cdd:cd18411    11 RVKLNVGGLAHEVLWRTLDRLPRTRLGKL-RDCNTHESLmeicddynleENEYFFDRHPGAFTSILNFYRTG 81

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily B member 2 (KCNB2); KCNB2, also called voltage-gated potassium channel subunit Kv2.2, mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a tetrameric potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. KCNB2 contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNB2 is an alpha subunit that forms functional homo- or hetero-tetrameric channels (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034579414  42 RLVINISGLRFETQLRTLSLFPDTLLGDPgRRVRFFDPL----------RNEYFFDRNRPSFDAILYYYQSG 103
Cdd:cd18412    18 RVKINVGGLNHEVLWRTLDRLPRTRLGKL-RDCNTHESLlevcddynlnENEYFFDRHPGAFTSILNFYRTG 88

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily G members, KCNG1 and KCNG2; KCNG1, also called voltage-gated potassium channel subunit Kv6.1 or kH2, functions as a regulatory alpha-subunit of voltage-gated potassium channel that can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. KCNG2, also called cardiac potassium channel subunit or voltage-gated potassium channel subunit Kv6.2, is a new gamma-subunit of voltage-gated potassium channels that can form functional heterodimeric channels with KCNB1, and further modulates channel activity by shifting the threshold and the half-maximal activation to more negative values. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNG1 and KCNG2 are regulatory alpha subunits and do not form homomultimers. They form heteromultimers (with other alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  42 RLVINISGLRFETQLRTLSLFPDTLLGdpgrRVRF-------------FDPLRNEYFFDRNRPSFDAILYYYQSgGRLRR 108
Cdd:cd18421     5 HVIINVGGIKYRIPWTTLEEFPLTRLG----QLKScnnfdeimdicddYDVTCNEFFFDRNPCAFRTILTFLRA-GKLRL 79

                          90       100
                  ....*....|....*....|...
gi 1034579414 109 PVNVPLDIFLEEIRFYQLGDEAL 131
Cdd:cd18421    80 LREMCALSFQEELLYWGIEEENL 102

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNS/Kv9 subfamily of potassium voltage-gated channels; Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv9, also known as subfamily S, includes KCNS1 (Kv9.1), KCNS2 (Kv9.2) and KCNS3 (Kv9.3). They are regulatory alpha subunits that cannot form functional homo-tetrameric channels. Both KCNS1 and KCNS2 are delayed-rectifier K(+) channel alpha subunits that can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1) and KCNB2 (also known as Kv2.2), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2. KCNS3 is a delayed-rectifier K(+) channel alpha subunit linked to tissue oxygenation responses. It can form functional heterotetrameric channels with KCNB1, and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  45 INISGLRFETQLRTLSLFPDTLLG-----DPGRRVRF----FDPLRNEYFFDRNRPSFDAILYYYQSgGRLRRPVNVPLD 115
Cdd:cd18384     3 INVGGFRRRLSASALLRFPGTRLGrllacHSEEAILElcddYDVAAREFYFDRNPGFFLYVLHFYRT-GKLHVMDELCVF 81

                          90
                  ....*....|....*...
gi 1034579414 116 IFLEEIRFYQLGDEALAA 133
Cdd:cd18384    82 SFSQEIEYWGINEFFLDS 99

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily S member 2 (KCNS2); KCNS2, also called delayed-rectifier K(+) channel alpha subunit 2 or voltage-gated potassium channel subunit Kv9.2, is a modulatory alpha subunit of voltage-gated potassium channel that can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1) and KCNB2 (also known as Kv2.2), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNS2 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  45 INISGLRFETQLRTLSLFPDTLLGdpgrrvRF---------------FDPLRNEYFFDRNRPSFDAILYYYQSgGRLRRP 109
Cdd:cd18427     4 INVGGFKKRLRSHTLLRFPETRLG------RLlscrskesilelcddYDDTKNEFYFDRNPELFPYVLHFYNT-GKLHVM 76

                          90
                  ....*....|....*....
gi 1034579414 110 VNVPLDIFLEEIRFYQLGD 128
Cdd:cd18427    77 GELCVFSFSQEIEYWGINE 95

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium voltage-gated channel subfamily G member 4 (KCNG4); KCNG4, also called voltage-gated potassium channel subunit Kv6.4, is a silent voltage-gated potassium (KvS) channel subunit that can form functional heterotetrameric channels with KCNB1 (also known as Kv2.1), and further modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. KCNG4 is a regulatory alpha subunit that cannot form a functional homo-tetrameric channel. It forms hetero-tetrameric channels (with other functional alpha subunits) through its BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  43 LVINISGLRFETQLRTLSLFPDTLLGdpgrRVRF-------------FDPLRNEYFFDRNRPSFDAILYYYqSGGRLRRP 109
Cdd:cd18423     4 IIINVGGIKYLMPWSTLDEFPLTRLG----KLKFcssyeeivqicddYDEDTNEFFFDRNPCAFRMIVSFL-AAGKLRLL 78

                          90       100
                  ....*....|....*....|..
gi 1034579414 110 VNVPLDIFLEEIRFYQLGDEAL 131
Cdd:cd18423    79 REMCALSFQEELTYWGIEEANL 100

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Arabidopsis thaliana FH protein interacting protein FIP2 and similar proteins; FIP2 may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. It contains a BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579414  43 LVINISGLRFETQLRTLSLFPDTLLGD--PGRrvrfFDPLRNE---YFFDRNRPSFDAILYYYQSGGRLRRPVNVP-LDI 116
Cdd:cd18376     1 VKLNVGGQKFTTTLDTLTKDPDSMLAAmfSGR----HSLKKDEdgsYFIDRDGTHFRHILNYLRDGEVKIPTEDRSvLKE 76

                          90
                  ....*....|
gi 1034579414 117 FLEEIRFYQL 126
Cdd:cd18376    77 LLEEAEYYQL 86