Search
immunoglobulin superfamily member 1 (inhibin-binding protein, inhBP, immunoglobulin-like domain-containing protein 1, Pituitary gland specific factor 2, p120, IGSF1, IGDC1, KIAA0364, PGSF2)
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 (putative)
- necessary to mediate a specific antagonistic effect of inhibin B on activin-stimulated transcription
- interacts with INHA (putative)
- interacts with ACVR1B, interaction appears to be ligand- dependent as it is diminished by inhibin B & activin A
- interacts with ACVR2A, ACVR2B, ACVRL1 & BMPR1B
Structure:
- contains 12 Ig-like C2-type domain (immunoglobulin-like)
Compartment:
- isoforms 1 & 2: membrane
- isoform 3: secreted (putative)
Alternative splicing:
- named isoforms=3
- additional isoforms seem to exist
Expression:
- highly expressed in pancreas, testis & fetal liver
- moderately expressed in heart, prostate & small intestine
- expressed at very low levels in brain, thymus, ovary, colon, fetal lung & fetal kidney
- expressed in muscle
- isoform 3 is expressed in pituitary gland
General
glycoprotein
immunoglobulin superfamily protein
membrane protein
Properties
SIZE: entity length = 1325 aa
MW = 148 kD
COMPARTMENT: cellular membrane
MOTIF: exoplasmic domain {1-507}
MOTIF: signal sequence {1-17}
immunoglobulin superfamily domain {27-111}
N-glycosylation site {N42}
cysteine residue {C47}
MODIFICATION: cysteine residue {C95}
cysteine residue {C95}
MODIFICATION: cysteine residue {C47}
immunoglobulin superfamily domain {126-211}
immunoglobulin superfamily domain {215-301}
cysteine residue {C237}
MODIFICATION: cysteine residue {C285}
cysteine residue {C285}
MODIFICATION: cysteine residue {C237}
immunoglobulin superfamily domain {310-397}
N-glycosylation site {N327}
cysteine residue {C332}
MODIFICATION: cysteine residue {C381}
N-glycosylation site {N363}
N-glycosylation site {N370}
cysteine residue {C381}
MODIFICATION: cysteine residue {C332}
immunoglobulin superfamily domain {408-489}
cysteine residue {C430}
MODIFICATION: cysteine residue {C473}
cysteine residue {C473}
MODIFICATION: cysteine residue {C430}
transmembrane domain {508-528}
cytoplasmic loop {529-548}
transmembrane domain {549-569}
exoplasmic domain {570-1325}
MOTIF: immunoglobulin superfamily domain {578-666}
N-glycosylation site {N596}
immunoglobulin superfamily domain {675-749}
cysteine residue {C692}
MODIFICATION: cysteine residue {C739}
N-glycosylation site {N736}
cysteine residue {C739}
MODIFICATION: cysteine residue {C692}
immunoglobulin superfamily domain {766-858}
N-glycosylation site {N787}
cysteine residue {C788}
MODIFICATION: cysteine residue {C838}
N-glycosylation site {N835}
cysteine residue {C838}
MODIFICATION: cysteine residue {C788}
immunoglobulin superfamily domain {862-947}
cysteine residue {C884}
MODIFICATION: cysteine residue {C931}
N-glycosylation site {N928}
cysteine residue {C931}
MODIFICATION: cysteine residue {C884}
immunoglobulin superfamily domain {954-1049}
N-glycosylation site {N975}
N-glycosylation site {N1016}
immunoglobulin superfamily domain {1054-1139}
N-glycosylation site {N1071}
cysteine residue {C1076}
MODIFICATION: cysteine residue {C1123}
cysteine residue {C1123}
MODIFICATION: cysteine residue {C1076}
N-glycosylation site {N1136}
immunoglobulin superfamily domain {1150-1231}
cysteine residue {C1172}
MODIFICATION: cysteine residue {C1215}
N-glycosylation site {N1212}
cysteine residue {C1215}
MODIFICATION: cysteine residue {C1172}
Database Correlations
OMIM 300137
UniProt Q8N6C5
References
UniProt :accession Q8N6C5