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Conserved domains on  [gi|2217312806|ref|XP_047292349|]
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testis-expressed protein 2 isoform X1 [Homo sapiens]

Protein Classification

SMP domain-containing protein( domain architecture ID 17749740)

SMP (synaptotagmin-like mitochondrial-lipid-binding) domain-containing protein contains a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers

Gene Ontology:  GO:0006869|GO:0008289|GO:0016020
PubMed:  24847877|31002947|26686281

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 830-1107 1.94e-84

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed protein 2 (TEX2) and similar proteins; testis-expressed protein 2 (TEX2), also called transmembrane protein 96 (TMEM96), is a transmembrane protein with uncharacterized biological function. Diseases associated with TEX2 include Wernicke-Korsakoff Syndrome. This model corresponds to the SMP domain of TEX2, which may be implicated in lipid transport.


:

Pssm-ID: 439231  Cd Length: 186  Bit Score: 271.67  E-value: 1.94e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  830 WVNALLGRIFWDFLGEKYWSDLVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQAFKPYVD-HQGLWIDLEMSYN 908
Cdd:cd21675      1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDpDGGLWVDLDVSYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  909 GSFLMTLETKMNLTKLGKeplvealkvgeigkegcrprafcladsdeesssagsseeddapepsggdkqllpgaegyvgg 988
Cdd:cd21675     81 GGFSLTLETKLNLSKLKK-------------------------------------------------------------- 98

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  989 hrtskimrfvdkitkskyfqkatetefikkkiEEVSNTPLLLTVEVQECRGTLAVNIPPPPTDRVWYGFRKPPHVELKAR 1068
Cdd:cd21675     99 --------------------------------EKVSNVPLVLAVEVKSLSGTLRLNIKPPPSNRLWYGFREMPKLELEIE 146

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2217312806 1069 PKLGEREVTLVHVTDWIEKKLEQEFQKVFVMPNMDDVYI 1107
Cdd:cd21675    147 PVVGERQVTLPHVTNWIEKKLKEEIKESLVLPNMDDFPF 185
 
Name Accession Description Interval E-value
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 830-1107 1.94e-84

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed protein 2 (TEX2) and similar proteins; testis-expressed protein 2 (TEX2), also called transmembrane protein 96 (TMEM96), is a transmembrane protein with uncharacterized biological function. Diseases associated with TEX2 include Wernicke-Korsakoff Syndrome. This model corresponds to the SMP domain of TEX2, which may be implicated in lipid transport.


Pssm-ID: 439231  Cd Length: 186  Bit Score: 271.67  E-value: 1.94e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  830 WVNALLGRIFWDFLGEKYWSDLVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQAFKPYVD-HQGLWIDLEMSYN 908
Cdd:cd21675      1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDpDGGLWVDLDVSYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  909 GSFLMTLETKMNLTKLGKeplvealkvgeigkegcrprafcladsdeesssagsseeddapepsggdkqllpgaegyvgg 988
Cdd:cd21675     81 GGFSLTLETKLNLSKLKK-------------------------------------------------------------- 98

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  989 hrtskimrfvdkitkskyfqkatetefikkkiEEVSNTPLLLTVEVQECRGTLAVNIPPPPTDRVWYGFRKPPHVELKAR 1068
Cdd:cd21675     99 --------------------------------EKVSNVPLVLAVEVKSLSGTLRLNIKPPPSNRLWYGFREMPKLELEIE 146

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2217312806 1069 PKLGEREVTLVHVTDWIEKKLEQEFQKVFVMPNMDDVYI 1107
Cdd:cd21675    147 PVVGERQVTLPHVTNWIEKKLKEEIKESLVLPNMDDFPF 185
 
Name Accession Description Interval E-value
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 830-1107 1.94e-84

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed protein 2 (TEX2) and similar proteins; testis-expressed protein 2 (TEX2), also called transmembrane protein 96 (TMEM96), is a transmembrane protein with uncharacterized biological function. Diseases associated with TEX2 include Wernicke-Korsakoff Syndrome. This model corresponds to the SMP domain of TEX2, which may be implicated in lipid transport.


Pssm-ID: 439231  Cd Length: 186  Bit Score: 271.67  E-value: 1.94e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  830 WVNALLGRIFWDFLGEKYWSDLVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQAFKPYVD-HQGLWIDLEMSYN 908
Cdd:cd21675      1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDpDGGLWVDLDVSYR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  909 GSFLMTLETKMNLTKLGKeplvealkvgeigkegcrprafcladsdeesssagsseeddapepsggdkqllpgaegyvgg 988
Cdd:cd21675     81 GGFSLTLETKLNLSKLKK-------------------------------------------------------------- 98

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  989 hrtskimrfvdkitkskyfqkatetefikkkiEEVSNTPLLLTVEVQECRGTLAVNIPPPPTDRVWYGFRKPPHVELKAR 1068
Cdd:cd21675     99 --------------------------------EKVSNVPLVLAVEVKSLSGTLRLNIKPPPSNRLWYGFREMPKLELEIE 146

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 2217312806 1069 PKLGEREVTLVHVTDWIEKKLEQEFQKVFVMPNMDDVYI 1107
Cdd:cd21675    147 PVVGERQVTLPHVTNWIEKKLKEEIKESLVLPNMDDFPF 185
SMP_SF cd21669
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP ...
 848-1105 1.15e-10

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP domain is a lipid transport domain found in phospholipid transfer proteins such as synaptotagmin family proteins, tricalbin (TCB) family proteins, maintenance of mitochondrial morphology protein 1 (MMM1), mitochondrial distribution and morphology protein 12 (MDM12), mitochondrial distribution and morphology protein 34 (MDM34), PDZ domain-containing protein 8 (PDZD8), testis-expressed protein 2 (TEX2), meiotically up-regulated gene 190 protein (Mug190), C2 domain-containing protein 2 (C2CD2) and C2 domain-containing protein 2-like (C2CD2L). The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP (tubular lipid-binding proteins). It adopts a TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure.


Pssm-ID: 439225  Cd Length: 165  Bit Score: 61.18  E-value: 1.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  848 WSDLVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKI--LQAFKPYVDHQGLWIDLEMSYNGSFLMTLETKMNLTKLG 925
Cdd:cd21669      1 LEQLIRESLQELLEEVKKPSFIESLELTEFTLGSNPPRIksVRVLDSPSSDLQLVLDLDLEYAGDFSVVLSAKLGGGGLG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  926 Keplvealkvgeigkegcrprafcladsdeesssagsseeddapepsggdkqllpgaegyvgghrtskimrfvdkitksk 1005
Cdd:cd21669     81 L------------------------------------------------------------------------------- 81

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806 1006 yfqkatetefikkkieevsntPLLLTVEVQECRGTLAVNI----PPPPTDRVWYGFRKPPHVELKARPKLGEREVTLVHV 1081
Cdd:cd21669     82 ---------------------PVPVSVSDLSLEGRLRVRLtllpEFPYVGALSISFVEPPDIDFSIRPLGGVDLMELPGL 140

                          250       260
                   ....*....|....*....|....
gi 2217312806 1082 TDWIEKKLEQEFQKVFVMPNMDDV 1105
Cdd:cd21669    141 SSWLEKLLTDALVELLVEPNRIVI 164
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 830-921 6.75e-04

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of mitochondrial morphology protein 1 (Mmm1) and similar proteins; Maintenance of mitochondrial morphology protein 1 (Mmm1), also called mitochondrial outer membrane protein Mmm1, or yeast mitochondrial escape protein 6 (YME6), is a mitochondrial outer membrane protein essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. It is a component of the ER-mitochondrion encounter structure/ mitochondrial distribution and morphology (ERMES/Mdm) complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The Mdm12-Mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The Mdm10-Mdm12-Mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the Mdm12-Mmm1 complex. This model corresponds to the SMP domain of Mmm1, which may be implicated in lipid transport.


Pssm-ID: 439227  Cd Length: 216  Bit Score: 42.51  E-value: 6.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  830 WVNALLGRIFwdflgEKYWSDLVSK-----KIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQA-FKPYVDHQGLWIDL 903
Cdd:cd21671     23 WLNVLLAQIL-----AQYRSDAEGDdnllrKLEEALNGERKPSFLDPIKVTDLDLGDDFPRFSNArIRPSDDSGGLRAEI 97

                           90
                   ....*....|....*...
gi 2217312806  904 EMSYNGSFLMTLETKMNL 921
Cdd:cd21671     98 DIDYSDTISLGIDTSLLL 115
SMP_ESyt cd21670
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended ...
 830-921 7.48e-04

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended synaptotagmin (E-Syt) family; The extended synaptotagmin (E-Syt) family includes a group of Ca2+-regulated intrinsic membrane proteins, such as E-Syt1, E-Syt2 and E-Syt3. They are composed of an N-terminal endoplasmic reticulum (ER)-membrane anchor, a central SMP-domain, and five (E-Syt1) or three C-terminal cytoplasmic C2-domains (E-Syt2 and E-Syt3). The ER-membrane anchor and C2 domains are required for tethering, while the SMP domain is a lipid-binding domain that links the ER with other lipid bilayer-membranes within the cell. This model corresponds to the SMP domain, which has a beta-barrel structure like protein modules in the tubular-lipid-binding (TULIP) superfamily. It dimerizes to form an approximately 90-Angstrom-long cylinder traversed by a channel lined entirely with hydrophobic residues. The following two C2 domains then form arched structures flexibly linked to the SMP domain.


Pssm-ID: 439226  Cd Length: 177  Bit Score: 41.77  E-value: 7.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217312806  830 WVNALLGRIfWDFLGEkYWSDLVSKKIQMKLSKIkLPYFMNELTLTELDMGVAVPKI--LQAFKPYVDHQGLWIDLEMSY 907
Cdd:cd21670      5 WLNKIIKQL-WPYINE-YVEKLLKEKIEPSIRAL-LPGPLKSFRFEKIDLGDKPPRIggVKVYTDNVDRDEIILDLDISY 81

                           90
                   ....*....|....*.
gi 2217312806  908 NG--SFLMTLETKMNL 921
Cdd:cd21670     82 DGdaDIEVSVGTGIKA 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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