Q7TQA1 · IGSF1_MOUSE
- ProteinImmunoglobulin superfamily member 1
- GeneIgsf1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1317 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Seems to be a coreceptor in inhibin signaling, but seems not to be a high-affinity inhibin receptor. Antagonizes activin A signaling in the presence or absence of inhibin B. Necessary to mediate a specific antagonistic effect of inhibin B on activin-stimulated transcription (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Molecular Function | activin receptor antagonist activity | |
Molecular Function | coreceptor activity | |
Molecular Function | inhibin binding | |
Biological Process | immune response-regulating signaling pathway | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameImmunoglobulin superfamily member 1
- Short namesIgSF1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ7TQA1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-499 | Extracellular | ||||
Sequence: SLAVESQPELWIESNYPQAPWENITLWCKSPSRVSSKFLLLKDNSQMTWIRPPYKTFQVSFFIGALTESNTGLYRCCYWKEKGWSKPSKILELEAPGQLPKPIFWIQAETPPLPGCNVNIFCHGWLQDLVFMLFKEGYTEPVDYQVPTGTMAIFSIDNLAPENEGVYICRTHIQMLPTLWSEPSNPLKLVVAGLYPKPTLTAHPGPILAPGESLSLRCQGPIYGMTFALMRLEDLKKSFYHKKPIKNEAYFYFQDLKIQDTGHYLCFYYDGSYRGSLLSDILKIWVTDTFPKTWLLVQPSPVIQMGQNVSLRCGGLMDGVGLALYKKGEEKPLQFLDASSNTGNNSFFLKNVTYRDAGIYSCHYYLTWKTSIKMATYNTVELMVVAWPSSVFKVGKTITLQCRVSHPVLEFSLEWEERTTFQKFSVDGDFLITDIEGQGTGTYSCSYRIEAHPNTWSHRSKPLKLVGPAGFLTWNSILN | ||||||
Transmembrane | 500-520 | Helical | ||||
Sequence: EAVRVSLTMQLASLLLLVVWI | ||||||
Topological domain | 521-531 | Cytoplasmic | ||||
Sequence: RWKCRRLRLRE | ||||||
Transmembrane | 532-552 | Helical | ||||
Sequence: AWLLGTAQGVAMLFILMALLC | ||||||
Topological domain | 553-1317 | Extracellular | ||||
Sequence: CGLCNGALTEEIEIVMPTPKPELWAETNFPLAPWKNLTLWCRSPSGSTKEFVLLKDGTGWIATRPASEQVRAAFPLGALTHSHTGSYHCHSWEEMAVSEPSEALELVGTDILPKPVISASLPIRGQELQIRCKGWLEGLGFALYKKGEQEPVQQLGAVGREAFFTIQRMEDKDEGNYSCRTHTEMQPFKWSEPSEPLELVIKEMYPKPFFKTWASPVVTPGSRVTFNCSTSHEHMSFILYKDGNEIASSDLAWGNPGGSTAHFLIISVGIGDGGNYSCRYYDFSIWSEPSNPVELVVTEFYPKPTLLAQPGPVVLPGKNVTLRCQGIFQGMRFALLQEGTHTPLQFQSTSGTSADFLLHTVGAQDFGNYSCVYYETTMSNRGSSLSTPLMIWVTDTFPRPWLSAEPSSVVTMGQNVTLWCQGPVRGVGYILHKEGEATSMQLWGSTSNEGAFPIINISGASIGRYSCCYHPDWMSPIKIQPSNTLELIVTGLLPKPSLLVQPGPMVAPGENVTLQCQGELPDSTFVLLKEGTRQPLEQQRPSGYRADFWMPVVRDQDSGVYSCVYYLDSAPLVASNHSNSLEIWVTDKPPKPSLSAWPSTIFKLGKDITLQCRGPLPGVEFVLEHDGEEAPQQFSEDGDFVIDNLEGKGIGNYSCSYRLQAYPDIWSEPSDTLELVGAAGPVAQECTVGNIVRSTLIVVVVVALGIVLAVEWKKWPRLRTRGSETDGRDQTVVLEECNQEGEPGTTTNSPSSASQEVSVELTVPI |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice are viable and fertile and show no alterations in FSH synthesis or secretion or in ovarian and testicular function. According to PubMed:23143598 male mice show diminished pituitary and serum thyroid-stimulating hormone (TSH) concentrations, reduced pituitary thyrotropin-releasing hormone (TRH) receptor expression, decreased triiodothyronine concentrations and increased body mass.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 126 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MMLRTFTLLLLCIWLNPGMT | ||||||
Chain | PRO_0000318513 | 21-1317 | Immunoglobulin superfamily member 1 | |||
Sequence: SLAVESQPELWIESNYPQAPWENITLWCKSPSRVSSKFLLLKDNSQMTWIRPPYKTFQVSFFIGALTESNTGLYRCCYWKEKGWSKPSKILELEAPGQLPKPIFWIQAETPPLPGCNVNIFCHGWLQDLVFMLFKEGYTEPVDYQVPTGTMAIFSIDNLAPENEGVYICRTHIQMLPTLWSEPSNPLKLVVAGLYPKPTLTAHPGPILAPGESLSLRCQGPIYGMTFALMRLEDLKKSFYHKKPIKNEAYFYFQDLKIQDTGHYLCFYYDGSYRGSLLSDILKIWVTDTFPKTWLLVQPSPVIQMGQNVSLRCGGLMDGVGLALYKKGEEKPLQFLDASSNTGNNSFFLKNVTYRDAGIYSCHYYLTWKTSIKMATYNTVELMVVAWPSSVFKVGKTITLQCRVSHPVLEFSLEWEERTTFQKFSVDGDFLITDIEGQGTGTYSCSYRIEAHPNTWSHRSKPLKLVGPAGFLTWNSILNEAVRVSLTMQLASLLLLVVWIRWKCRRLRLREAWLLGTAQGVAMLFILMALLCCGLCNGALTEEIEIVMPTPKPELWAETNFPLAPWKNLTLWCRSPSGSTKEFVLLKDGTGWIATRPASEQVRAAFPLGALTHSHTGSYHCHSWEEMAVSEPSEALELVGTDILPKPVISASLPIRGQELQIRCKGWLEGLGFALYKKGEQEPVQQLGAVGREAFFTIQRMEDKDEGNYSCRTHTEMQPFKWSEPSEPLELVIKEMYPKPFFKTWASPVVTPGSRVTFNCSTSHEHMSFILYKDGNEIASSDLAWGNPGGSTAHFLIISVGIGDGGNYSCRYYDFSIWSEPSNPVELVVTEFYPKPTLLAQPGPVVLPGKNVTLRCQGIFQGMRFALLQEGTHTPLQFQSTSGTSADFLLHTVGAQDFGNYSCVYYETTMSNRGSSLSTPLMIWVTDTFPRPWLSAEPSSVVTMGQNVTLWCQGPVRGVGYILHKEGEATSMQLWGSTSNEGAFPIINISGASIGRYSCCYHPDWMSPIKIQPSNTLELIVTGLLPKPSLLVQPGPMVAPGENVTLQCQGELPDSTFVLLKEGTRQPLEQQRPSGYRADFWMPVVRDQDSGVYSCVYYLDSAPLVASNHSNSLEIWVTDKPPKPSLSAWPSTIFKLGKDITLQCRGPLPGVEFVLEHDGEEAPQQFSEDGDFVIDNLEGKGIGNYSCSYRLQAYPDIWSEPSDTLELVGAAGPVAQECTVGNIVRSTLIVVVVVALGIVLAVEWKKWPRLRTRGSETDGRDQTVVLEECNQEGEPGTTTNSPSSASQEVSVELTVPI | ||||||
Glycosylation | 43 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 48↔96 | |||||
Sequence: CKSPSRVSSKFLLLKDNSQMTWIRPPYKTFQVSFFIGALTESNTGLYRC | ||||||
Disulfide bond | 238↔286 | |||||
Sequence: CQGPIYGMTFALMRLEDLKKSFYHKKPIKNEAYFYFQDLKIQDTGHYLC | ||||||
Glycosylation | 328 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 333↔382 | |||||
Sequence: CGGLMDGVGLALYKKGEEKPLQFLDASSNTGNNSFFLKNVTYRDAGIYSC | ||||||
Glycosylation | 371 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 422↔465 | |||||
Sequence: CRVSHPVLEFSLEWEERTTFQKFSVDGDFLITDIEGQGTGTYSC | ||||||
Disulfide bond | 780↔830 | |||||
Sequence: CSTSHEHMSFILYKDGNEIASSDLAWGNPGGSTAHFLIISVGIGDGGNYSC | ||||||
Glycosylation | 871 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 876↔923 | |||||
Sequence: CQGIFQGMRFALLQEGTHTPLQFQSTSGTSADFLLHTVGAQDFGNYSC | ||||||
Glycosylation | 967 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1063 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1068↔1115 | |||||
Sequence: CQGELPDSTFVLLKEGTRQPLEQQRPSGYRADFWMPVVRDQDSGVYSC | ||||||
Disulfide bond | 1164↔1207 | |||||
Sequence: CRGPLPGVEFVLEHDGEEAPQQFSEDGDFVIDNLEGKGIGNYSC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with INHA; the interaction is not confirmed by standard receptor binding assays (By similarity).
Interacts with ACVR1B; the interaction appears to be ligand-dependent as it is diminished by inhibin B and activin A. Interacts with ACVR2A, ACVR2B, ACVRL1 and BMPR1B (By similarity).
Interacts with HECTD1 (By similarity).
Interacts with ACVR1B; the interaction appears to be ligand-dependent as it is diminished by inhibin B and activin A. Interacts with ACVR2A, ACVR2B, ACVRL1 and BMPR1B (By similarity).
Interacts with HECTD1 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-112 | Ig-like C2-type 1 | ||||
Sequence: SLAVESQPELWIESNYPQAPWENITLWCKSPSRVSSKFLLLKDNSQMTWIRPPYKTFQVSFFIGALTESNTGLYRCCYWKEKGWSKPSKILE | ||||||
Domain | 114-211 | Ig-like C2-type 2 | ||||
Sequence: EAPGQLPKPIFWIQAETPPLPGCNVNIFCHGWLQDLVFMLFKEGYTEPVDYQVPTGTMAIFSIDNLAPENEGVYICRTHIQMLPTLWSEPSNPLKLVV | ||||||
Domain | 216-302 | Ig-like C2-type 3 | ||||
Sequence: PKPTLTAHPGPILAPGESLSLRCQGPIYGMTFALMRLEDLKKSFYHKKPIKNEAYFYFQDLKIQDTGHYLCFYYDGSYRGSLLSDIL | ||||||
Domain | 311-398 | Ig-like C2-type 4 | ||||
Sequence: PKTWLLVQPSPVIQMGQNVSLRCGGLMDGVGLALYKKGEEKPLQFLDASSNTGNNSFFLKNVTYRDAGIYSCHYYLTWKTSIKMATYN | ||||||
Domain | 400-481 | Ig-like C2-type 5 | ||||
Sequence: VELMVVAWPSSVFKVGKTITLQCRVSHPVLEFSLEWEERTTFQKFSVDGDFLITDIEGQGTGTYSCSYRIEAHPNTWSHRSK | ||||||
Domain | 570-658 | Ig-like C2-type 6 | ||||
Sequence: TPKPELWAETNFPLAPWKNLTLWCRSPSGSTKEFVLLKDGTGWIATRPASEQVRAAFPLGALTHSHTGSYHCHSWEEMAVSEPSEALEL | ||||||
Domain | 659-753 | Ig-like C2-type 7 | ||||
Sequence: VGTDILPKPVISASLPIRGQELQIRCKGWLEGLGFALYKKGEQEPVQQLGAVGREAFFTIQRMEDKDEGNYSCRTHTEMQPFKWSEPSEPLELVI | ||||||
Domain | 758-850 | Ig-like C2-type 8 | ||||
Sequence: PKPFFKTWASPVVTPGSRVTFNCSTSHEHMSFILYKDGNEIASSDLAWGNPGGSTAHFLIISVGIGDGGNYSCRYYDFSIWSEPSNPVELVVT | ||||||
Domain | 854-938 | Ig-like C2-type 9 | ||||
Sequence: PKPTLLAQPGPVVLPGKNVTLRCQGIFQGMRFALLQEGTHTPLQFQSTSGTSADFLLHTVGAQDFGNYSCVYYETTMSNRGSSLS | ||||||
Domain | 946-1041 | Ig-like C2-type 10 | ||||
Sequence: TDTFPRPWLSAEPSSVVTMGQNVTLWCQGPVRGVGYILHKEGEATSMQLWGSTSNEGAFPIINISGASIGRYSCCYHPDWMSPIKIQPSNTLELIV | ||||||
Domain | 1046-1131 | Ig-like C2-type 11 | ||||
Sequence: PKPSLLVQPGPMVAPGENVTLQCQGELPDSTFVLLKEGTRQPLEQQRPSGYRADFWMPVVRDQDSGVYSCVYYLDSAPLVASNHSN | ||||||
Domain | 1142-1223 | Ig-like C2-type 12 | ||||
Sequence: PKPSLSAWPSTIFKLGKDITLQCRGPLPGVEFVLEHDGEEAPQQFSEDGDFVIDNLEGKGIGNYSCSYRLQAYPDIWSEPSD | ||||||
Region | 1290-1310 | Disordered | ||||
Sequence: NQEGEPGTTTNSPSSASQEVS | ||||||
Compositional bias | 1292-1310 | Polar residues | ||||
Sequence: EGEPGTTTNSPSSASQEVS |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 5 isoforms produced by Alternative promoter usage & Alternative splicing.
Q7TQA1-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsInhBP-L, long
- NoteProduced by alternative promoter usage.
- Length1,317
- Mass (Da)147,010
- Last updated2003-10-01 v1
- Checksum09D1E7A89ADCB04D
Q7TQA1-2
Q7TQA1-3
- Name3
- SynonymsInhBP-3
- NoteProduced by alternative splicing of isoform 1.
Q7TQA1-4
- Name4
- SynonymsInhBP-S, short
- NoteProduced by alternative splicing of isoform 1.
Q7TQA1-5
- Name5
- SynonymsInhBP-4, variant 4
- NoteProduced by alternative promoter usage.
- Differences from canonical
- 1-542: Missing
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_031198 | 1-542 | in isoform 5 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_031199 | 214-232 | in isoform 4 | |||
Sequence: LYPKPTLTAHPGPILAPGE → GCGHGCWHLTIVIPGIMAG | ||||||
Alternative sequence | VSP_031200 | 233-1317 | in isoform 4 | |||
Sequence: Missing | ||||||
Sequence conflict | 277 | in Ref. 1; AAP57081 | ||||
Sequence: K → E | ||||||
Alternative sequence | VSP_031201 | 755-762 | in isoform 3 | |||
Sequence: EMYPKPFF → DGRTKAQN | ||||||
Alternative sequence | VSP_031202 | 763-1317 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_031203 | 865-1156 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 1292-1310 | Polar residues | ||||
Sequence: EGEPGTTTNSPSSASQEVS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY227771 EMBL· GenBank· DDBJ | AAP57079.1 EMBL· GenBank· DDBJ | mRNA | ||
AY227772 EMBL· GenBank· DDBJ | AAP57080.1 EMBL· GenBank· DDBJ | mRNA | ||
AY227773 EMBL· GenBank· DDBJ | AAP57081.1 EMBL· GenBank· DDBJ | mRNA | ||
AY227774 EMBL· GenBank· DDBJ | AAP57082.1 EMBL· GenBank· DDBJ | mRNA | ||
AK129126 EMBL· GenBank· DDBJ | BAC97936.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK030452 EMBL· GenBank· DDBJ | BAC26969.1 EMBL· GenBank· DDBJ | mRNA |