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IGSF1_RAT
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   03-AUG-2022, entry version 124.
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   GlyGen; Q925N6; 15 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q925N6; -.
DR   PhosphoSitePlus; Q925N6; -.
DR   PaxDb; Q925N6; -.
DR   PRIDE; Q925N6; -.
DR   GeneID; 302822; -.
DR   KEGG; rno:302822; -.
DR   UCSC; RGD:631402; rat. [Q925N6-1]
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   OMA; VGKYKPP; -.
DR   OrthoDB; 1327293at2759; -.
DR   PhylomeDB; Q925N6; -.
DR   TreeFam; TF336644; -.
DR   PRO; PR:Q925N6; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000007600; Expressed in testis and 10 other tissues.
DR   Genevisible; Q925N6; RN.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 transcription, DNA-templated; ISO:RGD.
DR   Gene3D; 2.60.40.10; -; 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   Pfam; PF13895; Ig_2; 4.
DR   SMART; SM00409; IG; 11.
DR   SMART; SM00408; IGc2; 6.
DR   SUPFAM; SSF48726; SSF48726; 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
 
 
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