ID IGSF1_RAT Reviewed; 1320 AA.
AC Q925N6; A0JPK8; Q925N5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=Immunoglobulin superfamily member 1;
DE Short=IgSF1;
DE AltName: Full=Inhibin-binding protein;
DE Short=InhBP;
DE Flags: Precursor;
GN Name=Igsf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=11266515; DOI=10.1210/mend.15.4.0630;
RA Bernard D.J., Woodruff T.K.;
RT "Inhibin binding protein in rats: alternative transcripts and regulation in
RT the pituitary across the estrous cycle.";
RL Mol. Endocrinol. 15:654-667(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=10875264; DOI=10.1210/endo.141.7.7540;
RA Chong H., Pangas S.A., Bernard D.J., Wang E., Gitch J., Chen W.,
RA Draper L.B., Cox E.T., Woodruff T.K.;
RT "Structure and expression of a membrane component of the inhibin receptor
RT system.";
RL Endocrinology 141:2600-2607(2000).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-782, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Seems to be a coreceptor in inhibin signaling, but seems not
CC to be a high-affinity inhibin receptor. Antagonizes activin A signaling
CC in the presence or absence of inhibin B. Necessary to mediate a
CC specific antagonistic effect of inhibin B on activin-stimulated
CC transcription (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with INHA; the interaction is not confirmed by
CC standard receptor binding assays. Interacts with ACVR1B; the
CC interaction appears to be ligand-dependent as it is diminished by
CC inhibin B and activin A. Interacts with ACVR2A, ACVR2B, ACVRL1 and
CC BMPR1B (By similarity). Interacts with HECTD1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=InhBP-L, long;
CC IsoId=Q925N6-1; Sequence=Displayed;
CC Name=2; Synonyms=InhBP-S, short;
CC IsoId=Q925N6-2; Sequence=VSP_031205, VSP_031206;
CC Name=3;
CC IsoId=Q925N6-3; Sequence=VSP_031204, VSP_031205, VSP_031206;
CC -!- TISSUE SPECIFICITY: Expressed in pituitary gland, testis and liver.
CC Isoform 2 is expressed pituitary gland and testis.
CC {ECO:0000269|PubMed:10875264, ECO:0000269|PubMed:11266515}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF322216; AAK40083.1; -; mRNA.
DR EMBL; AF322217; AAK40084.1; -; mRNA.
DR EMBL; BC060309; AAH60309.1; -; mRNA.
DR EMBL; BC127478; AAI27479.1; -; mRNA.
DR RefSeq; NP_786939.1; NM_175763.2. [Q925N6-1]
DR AlphaFoldDB; Q925N6; -.
DR SMR; Q925N6; -.
DR STRING; 10116.ENSRNOP00000010325; -.
DR GlyCosmos; Q925N6; 15 sites, 2 glycans.
DR GlyGen; Q925N6; 15 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q925N6; -.
DR PhosphoSitePlus; Q925N6; -.
DR PaxDb; 10116-ENSRNOP00000010325; -.
DR Ensembl; ENSRNOT00055048548; ENSRNOP00055039909; ENSRNOG00055028046. [Q925N6-1]
DR Ensembl; ENSRNOT00060035075; ENSRNOP00060028825; ENSRNOG00060020228. [Q925N6-1]
DR GeneID; 302822; -.
DR KEGG; rno:302822; -.
DR UCSC; RGD:631402; rat. [Q925N6-1]
DR AGR; RGD:631402; -.
DR CTD; 3547; -.
DR RGD; 631402; Igsf1.
DR VEuPathDB; HostDB:ENSRNOG00000007600; -.
DR eggNOG; ENOG502RYEX; Eukaryota.
DR HOGENOM; CLU_006143_0_0_1; -.
DR InParanoid; Q925N6; -.
DR OrthoDB; 5355093at2759; -.
DR PhylomeDB; Q925N6; -.
DR TreeFam; TF336644; -.
DR PRO; PR:Q925N6; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000007600; Expressed in testis and 10 other cell types or tissues.
DR Genevisible; Q925N6; RN.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0038102; F:activin receptor antagonist activity; ISO:RGD.
DR GO; GO:0015026; F:coreceptor activity; IDA:RGD.
DR GO; GO:0034711; F:inhibin binding; ISO:RGD.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:RGD.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD.
DR Gene3D; 2.60.40.10; Immunoglobulins; 12.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR11738; MHC CLASS I NK CELL RECEPTOR; 1.
DR PANTHER; PTHR11738:SF159; PLATELET GLYCOPROTEIN VI; 1.
DR Pfam; PF13895; Ig_2; 4.
DR Pfam; PF13927; Ig_3; 1.
DR SMART; SM00409; IG; 11.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; Immunoglobulin; 12.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1320
FT /note="Immunoglobulin superfamily member 1"
FT /id="PRO_0000318514"
FT TOPO_DOM 19..504
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..1320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 29..113
FT /note="Ig-like C2-type 1"
FT DOMAIN 115..212
FT /note="Ig-like C2-type 2"
FT DOMAIN 224..308
FT /note="Ig-like C2-type 3"
FT DOMAIN 312..399
FT /note="Ig-like C2-type 4"
FT DOMAIN 401..482
FT /note="Ig-like C2-type 5"
FT DOMAIN 572..665
FT /note="Ig-like C2-type 6"
FT DOMAIN 662..756
FT /note="Ig-like C2-type 7"
FT DOMAIN 761..853
FT /note="Ig-like C2-type 8"
FT DOMAIN 857..942
FT /note="Ig-like C2-type 9"
FT DOMAIN 949..1044
FT /note="Ig-like C2-type 10"
FT DOMAIN 1049..1134
FT /note="Ig-like C2-type 11"
FT DOMAIN 1145..1226
FT /note="Ig-like C2-type 12"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 970
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 334..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 423..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 783..833
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 879..926
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1071..1118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1167..1210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 24
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031204"
FT VAR_SEQ 215..233
FT /note="LYPKPTLTAHPGPILAPGE -> GCAHGCWHLTIVIPGIMAG (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11266515,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031205"
FT VAR_SEQ 234..1320
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11266515,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031206"
SQ SEQUENCE 1320 AA; 147293 MW; F5F5B2AA77BA3C2A CRC64;
MMLRTFTLLL LCIWLNRGMT SMAAVESQPE LWIESNYPQA PWENITLWCK SPSRVSSKFL
LLKDNTQMTW IHPPYKTFQV SFFIGALTES NTGLYRCCYW NEKGWSKPSK ILELEAPGQL
PKPIFWIQAE TPPFPGCNVN ILCHGWLQDL VFMLFKEGYT EPIDYQVPTG TMAIFSIDNL
APENEGIYIC RTHIQMLPTL WSEPSNPLKL VVAGLYPKPT LTAHPGPILA PGESLSLRCQ
GPIYGMTFAL MRLEDLKKPY YYKKPIKNEA YFYFQALKTQ DTGHYLCFYY DGSYRGSLLS
DILKIWVTDT FPKTWLLVQP SPVIQMGQNV SLRCGGLMDG VGLALHKKGE EKPLQFLDAT
SNTGNNSFFL KNVTYRDAGI YSCHYYLTWK TSIKMATYNT VELIVVAWPS SVFKVGKTIT
LQCRVSHPVL EFSLEWEETT TFQKFSVDGD FIITNIEGQG TGTYSCSYRI ESHANIWSHR
SEPLKLVGPA VTGFLPWNSI LNEAIRVSLT VQFLSLLLLV LWLQWKCRRL RLREAWLLGT
AQGVAMLVIL IALLCCGLCN GALTEEIEII MPTPKPELWA ETNFPQAPWK NVTLWCRSPS
GSTKEFVLLK DGTGWIATRP ASEQVRAAFP LGALTQSHTG SYHCHSWEEM AVSEPSEALE
LVGTDILPKP VISASLPIRG QELQIRCKGW LEGLGFALYK MGEQEPVQQL GAVGREAFFT
IQRMEDKEEG NYSCRTHTEK QPFKWSEPSA PLELVIKELY PKPFFKTWAS PVVTPGSRVT
FNCSTSREHM SFILYKDGNE IASSDPVWGN PGTSTAHFLI ISVGIGDGGN YSCRYYDFSI
WSEPSDPVEL IVTEFYPKPT LLAQPGPVVL PGKNVTLRCQ GIFQGMRFAL LQEGAHAPLQ
FQSASGTSVD FLLHTVGAED FGNYSCVYYE TTMSNRGSYL STPLMIWVTD TFPRPWLSAE
PSSVVTMGQN VTLWCQGPVH GVGYILHKEG EATSMQLWDS TSNEGAFPII NISGASIGRY
SCCYHPDWMS PIKIQPSNTL ELIVTGLLPK PSLLVQPGPM VVPGENMTFQ CQGELPDSTF
VLLKEGTQQP IEQQRPSGYR ADFWMPVVRD QDSGVYSCVY YLDSAPLVAS NHSNSLEIWV
TDKPPKPSLS AWPSTVFKLG KDITLQCRGP LPGVEFVLEH DGEEAPQQFS EDGDFVIGNM
EGKGIGNYSC SYRLQAYPDI WSEPSDSLEL VGAAGPVAQE CTVGNIVRST LIVVVVVALG
IVLAIEWKKW PRLRTRGSET DGRDQTIVLE ECNQDGEPGT ATNSPSSALQ GVSVEQTVPI
//
