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Conserved domains on  [gi|7305449|ref|NP_038676|]
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reticulon-2 isoform B [Mus musculus]

Protein Classification

reticulon family protein( domain architecture ID 10493657)

reticulon family protein associates with the endoplasmic reticulum (ER) through a C-terminal di-lysine ER retention motif; such as mammalian RTN4/Nogo, a developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching

Gene Ontology:  GO:0005789|GO:0005783
PubMed:  12832288|18177508|22425683|33924890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reticulon pfam02453
Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of ...
 272-436 1.50e-49

Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of unknown function which associates with the endoplasmic reticulum. This family represents the C-terminal domain of the three reticulon isoforms and their homologs.


:

Pssm-ID: 460562 [Multi-domain]  Cd Length: 157  Bit Score: 166.51  E-value: 1.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449    272 VADLLYWKDTRTSGAVFTGLMASLL--CLLHFSIVSVAAHLALLGLCATISLRVYRKVLQAVhrgdGTNPfqayldMDLT 349
Cdd:pfam02453   1 VADLLLWRNPKKSGGVFGGATALWLlfEVLGYSLLSLVSKLLLLLLLVLFLWAEYAGKLNRP----PPPI------PELE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449    350 LTREQTERLSQQIASHVVSTATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLVILGVVALFTVPLLYRQHQAQI 429
Cdd:pfam02453  71 LSEETVRELADSLRVLINFALSELRRIALGEDLKLFLKVAVVLWILSYVGSLFSFLTLLYIGVVLAFTVPLLYEKYEDEI 150


                  ....*..
gi 7305449    430 DQYVGLV 436
Cdd:pfam02453 151 DAYVEKA 157
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 58-226 5.36e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449     58 TPRELTFSYIAFDGVVGSGG--RRDSVVR--------RPRPQGRSVSEPRDPPQQSGLG---DSLESIPSlSQSPEPGRR 124
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSVAPGGdvRRRPPSRspaakpaaPARPPVRRLARPAVSRSTESFAlppDQPERPPQ-PQAPPPPQP 2919

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449    125 GDPDPVPPAERPLEELRLRLD-QLGWVVRSAGSGEDSATSSSTPLENEEPDGLEASEAgeetnlelrlaqslhlqlevLT 203
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQpPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF--------------------RV 2979

                         170       180
                  ....*....|....*....|...
gi 7305449    204 PQLSPSSGTPQAHTPSPQRSQDS 226
Cdd:PHA03247 2980 PQPAPSREAPASSTPPLTGHSLS 3002
 
Name Accession Description Interval E-value
Reticulon pfam02453
Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of ...
 272-436 1.50e-49

Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of unknown function which associates with the endoplasmic reticulum. This family represents the C-terminal domain of the three reticulon isoforms and their homologs.


Pssm-ID: 460562 [Multi-domain]  Cd Length: 157  Bit Score: 166.51  E-value: 1.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449    272 VADLLYWKDTRTSGAVFTGLMASLL--CLLHFSIVSVAAHLALLGLCATISLRVYRKVLQAVhrgdGTNPfqayldMDLT 349
Cdd:pfam02453   1 VADLLLWRNPKKSGGVFGGATALWLlfEVLGYSLLSLVSKLLLLLLLVLFLWAEYAGKLNRP----PPPI------PELE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449    350 LTREQTERLSQQIASHVVSTATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLVILGVVALFTVPLLYRQHQAQI 429
Cdd:pfam02453  71 LSEETVRELADSLRVLINFALSELRRIALGEDLKLFLKVAVVLWILSYVGSLFSFLTLLYIGVVLAFTVPLLYEKYEDEI 150


                  ....*..
gi 7305449    430 DQYVGLV 436
Cdd:pfam02453 151 DAYVEKA 157
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 270-448 4.13e-04

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 42.04  E-value: 4.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449  270 LLVADLLywkDTRTSGAVFTGLMASLLCLLHFSIVSVAAHLALLGLCA-----TISLRVYRKVLQAvhrgdgtnPfQAYL 344
Cdd:cd18551  20 LLVKNLI---DALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGervvlDLRRRLWRRLLRL--------P-VSFF 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449  345 DmdltltreqtERLSQQIASHVVSTATQLRHFfLVEDLVDslklaLLFYILTFVGAIF------NGLTLVILGVVALFTV 418
Cdd:cd18551  88 D----------RRRSGDLVSRVTNDTTLLREL-ITSGLPQ-----LVTGVLTVVGAVVlmflldWVLTLVTLAVVPLAFL 151

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 7305449  419 ------PLLYR-QHQAQidQYVGLVTNQLSHIKAKIR 448
Cdd:cd18551 152 iilplgRRIRKaSKRAQ--DALGELSAALERALSAIR 186
PHA03247 PHA03247
large tegument protein UL36; Provisional
 58-226 5.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449     58 TPRELTFSYIAFDGVVGSGG--RRDSVVR--------RPRPQGRSVSEPRDPPQQSGLG---DSLESIPSlSQSPEPGRR 124
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSVAPGGdvRRRPPSRspaakpaaPARPPVRRLARPAVSRSTESFAlppDQPERPPQ-PQAPPPPQP 2919

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449    125 GDPDPVPPAERPLEELRLRLD-QLGWVVRSAGSGEDSATSSSTPLENEEPDGLEASEAgeetnlelrlaqslhlqlevLT 203
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQpPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF--------------------RV 2979

                         170       180
                  ....*....|....*....|...
gi 7305449    204 PQLSPSSGTPQAHTPSPQRSQDS 226
Cdd:PHA03247 2980 PQPAPSREAPASSTPPLTGHSLS 3002
 
Name Accession Description Interval E-value
Reticulon pfam02453
Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of ...
 272-436 1.50e-49

Reticulon; Reticulon, also know as neuroendocrine-specific protein (NSP), is a protein of unknown function which associates with the endoplasmic reticulum. This family represents the C-terminal domain of the three reticulon isoforms and their homologs.


Pssm-ID: 460562 [Multi-domain]  Cd Length: 157  Bit Score: 166.51  E-value: 1.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449    272 VADLLYWKDTRTSGAVFTGLMASLL--CLLHFSIVSVAAHLALLGLCATISLRVYRKVLQAVhrgdGTNPfqayldMDLT 349
Cdd:pfam02453   1 VADLLLWRNPKKSGGVFGGATALWLlfEVLGYSLLSLVSKLLLLLLLVLFLWAEYAGKLNRP----PPPI------PELE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449    350 LTREQTERLSQQIASHVVSTATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLVILGVVALFTVPLLYRQHQAQI 429
Cdd:pfam02453  71 LSEETVRELADSLRVLINFALSELRRIALGEDLKLFLKVAVVLWILSYVGSLFSFLTLLYIGVVLAFTVPLLYEKYEDEI 150


                  ....*..
gi 7305449    430 DQYVGLV 436
Cdd:pfam02453 151 DAYVEKA 157
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 270-448 4.13e-04

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 42.04  E-value: 4.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449  270 LLVADLLywkDTRTSGAVFTGLMASLLCLLHFSIVSVAAHLALLGLCA-----TISLRVYRKVLQAvhrgdgtnPfQAYL 344
Cdd:cd18551  20 LLVKNLI---DALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGervvlDLRRRLWRRLLRL--------P-VSFF 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449  345 DmdltltreqtERLSQQIASHVVSTATQLRHFfLVEDLVDslklaLLFYILTFVGAIF------NGLTLVILGVVALFTV 418
Cdd:cd18551  88 D----------RRRSGDLVSRVTNDTTLLREL-ITSGLPQ-----LVTGVLTVVGAVVlmflldWVLTLVTLAVVPLAFL 151

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 7305449  419 ------PLLYR-QHQAQidQYVGLVTNQLSHIKAKIR 448
Cdd:cd18551 152 iilplgRRIRKaSKRAQ--DALGELSAALERALSAIR 186
PHA03247 PHA03247
large tegument protein UL36; Provisional
 58-226 5.36e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449     58 TPRELTFSYIAFDGVVGSGG--RRDSVVR--------RPRPQGRSVSEPRDPPQQSGLG---DSLESIPSlSQSPEPGRR 124
Cdd:PHA03247 2841 PPPGPPPPSLPLGGSVAPGGdvRRRPPSRspaakpaaPARPPVRRLARPAVSRSTESFAlppDQPERPPQ-PQAPPPPQP 2919

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305449    125 GDPDPVPPAERPLEELRLRLD-QLGWVVRSAGSGEDSATSSSTPLENEEPDGLEASEAgeetnlelrlaqslhlqlevLT 203
Cdd:PHA03247 2920 QPQPPPPPQPQPPPPPPPRPQpPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRF--------------------RV 2979

                         170       180
                  ....*....|....*....|...
gi 7305449    204 PQLSPSSGTPQAHTPSPQRSQDS 226
Cdd:PHA03247 2980 PQPAPSREAPASSTPPLTGHSLS 3002
 
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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