IGSF1_HUMAN
ID IGSF1_HUMAN Reviewed; 1336 AA.
AC Q8N6C5; B5MEG2; H9KV64; O15070; Q9NTC8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Immunoglobulin superfamily member 1;
DE Short=IgSF1;
DE AltName: Full=Immunoglobulin-like domain-containing protein 1;
DE AltName: Full=Inhibin-binding protein;
DE Short=InhBP;
DE AltName: Full=Pituitary gland-specific factor 2;
DE AltName: Full=p120;
DE Flags: Precursor;
GN Name=IGSF1; Synonyms=IGDC1, KIAA0364, PGSF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9729118; DOI=10.1016/s0378-1119(98)00253-4;
RA Frattini A., Faranda S., Redolfi E., Allavena P., Vezzoni P.;
RT "Identification and genomic organization of a gene coding for a new member
RT of the cell adhesion molecule family mapping to Xq25.";
RL Gene 214:1-6(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=9521868; DOI=10.1006/geno.1997.5156;
RA Mazzarella R., Pengue G., Jones J., Jones C., Schlessinger D.;
RT "Cloning and expression of an immunoglobulin superfamily gene (IGSF1) in
RT Xq25.";
RL Genomics 48:157-162(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC TISSUE=Pituitary;
RX PubMed=11854097; DOI=10.1677/jme.0.0280033;
RA Tanaka S., Tatsumi K., Okubo K., Itoh K., Kawamoto S., Matsubara K.,
RA Amino N.;
RT "Expression profile of active genes in the human pituitary gland.";
RL J. Mol. Endocrinol. 28:33-44(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Liver;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1153-1336.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH ACVR1B; ACVR2A; ACVR2B; ACVRL1 AND BMPR1B.
RX PubMed=11266516; DOI=10.1210/mend.15.4.0616;
RA Chapman S.C., Woodruff T.K.;
RT "Modulation of activin signal transduction by inhibin B and inhibin-binding
RT protein (INhBP).";
RL Mol. Endocrinol. 15:668-679(2001).
RN [9]
RP INTERACTION WITH HECTD1.
RX PubMed=12421765; DOI=10.1101/gr.406902;
RA Nakayama M., Kikuno R., Ohara O.;
RT "Protein-protein interactions between large proteins: two-hybrid screening
RT using a functionally classified library composed of long cDNAs.";
RL Genome Res. 12:1773-1784(2002).
RN [10]
RP NEGATIVE INTERACTION WITH INHA.
RX PubMed=12385827; DOI=10.1016/s0303-7207(02)00227-7;
RA Chapman S.C., Bernard D.J., Jelen J., Woodruff T.K.;
RT "Properties of inhibin binding to betaglycan, InhBP/p120 and the activin
RT type II receptors.";
RL Mol. Cell. Endocrinol. 196:79-93(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, VARIANTS CHTE 708-ALA--LYS-716
RP DEL; ASN-765; PHE-858 AND ARG-942, AND CHARACTERIZATION OF 708-ALA--LYS-716
RP DEL; ASN-765; PHE-858 AND ARG-942.
RX PubMed=23143598; DOI=10.1038/ng.2453;
RA Sun Y., Bak B., Schoenmakers N., van Trotsenburg A.S., Oostdijk W.,
RA Voshol P., Cambridge E., White J.K., le Tissier P., Gharavy S.N.,
RA Martinez-Barbera J.P., Stokvis-Brantsma W.H., Vulsma T., Kempers M.J.,
RA Persani L., Campi I., Bonomi M., Beck-Peccoz P., Zhu H., Davis T.M.,
RA Hokken-Koelega A.C., Del Blanco D.G., Rangasami J.J., Ruivenkamp C.A.,
RA Laros J.F., Kriek M., Kant S.G., Bosch C.A., Biermasz N.R.,
RA Appelman-Dijkstra N.M., Corssmit E.P., Hovens G.C., Pereira A.M.,
RA den Dunnen J.T., Wade M.G., Breuning M.H., Hennekam R.C., Chatterjee K.,
RA Dattani M.T., Wit J.M., Bernard D.J.;
RT "Loss-of-function mutations in IGSF1 cause an X-linked syndrome of central
RT hypothyroidism and testicular enlargement.";
RL Nat. Genet. 44:1375-1381(2012).
RN [13]
RP VARIANT GLY-774.
RX PubMed=23092983; DOI=10.1038/tp.2012.102;
RA Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D.,
RA Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A.,
RA Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G.,
RA Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T.,
RA Brice A., Depienne C.;
RT "Analysis of the chromosome X exome in patients with autism spectrum
RT disorders identified novel candidate genes, including TMLHE.";
RL Transl. Psychiatry 2:E179-E179(2012).
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 (By similarity). Necessary to
CC mediate a specific antagonistic effect of inhibin B on activin-
CC stimulated transcription. {ECO:0000250, ECO:0000269|PubMed:11266516}.
CC -!- SUBUNIT: Interacts with INHA (By similarity). In PubMed:12385827 does
CC not interact with INHA; standard receptor binding assay. Interacts with
CC ACVR1B; the interaction appears to be ligand-dependent as it is
CC diminished by inhibin B and activin A. Interacts with ACVR2A, ACVR2B,
CC ACVRL1 and BMPR1B. Interacts with HECTD1. {ECO:0000250,
CC ECO:0000269|PubMed:11266516, ECO:0000269|PubMed:12421765}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=InhBP-L, long;
CC IsoId=Q8N6C5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N6C5-2; Sequence=VSP_031195;
CC Name=3; Synonyms=InhBP-S, short;
CC IsoId=Q8N6C5-3; Sequence=VSP_031196, VSP_031197;
CC Name=4;
CC IsoId=Q8N6C5-4; Sequence=VSP_044554;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas, testis and fetal
CC liver. Moderately expressed in heart, prostate and small intestine.
CC Expressed at very low levels in brain, thymus, ovary, colon, fetal lung
CC and fetal kidney. Expressed in muscle. Isoform 3 is expressed in
CC pituitary gland. {ECO:0000269|PubMed:11854097,
CC ECO:0000269|PubMed:23143598, ECO:0000269|PubMed:9521868}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo Carnegie stage 18 in Rathke's
CC pouch progenitors. {ECO:0000269|PubMed:23143598}.
CC -!- DISEASE: Hypothyroidism, central, and testicular enlargement (CHTE)
CC [MIM:300888]: A disorder characterized by insufficient thyroid gland
CC stimulation by thyroid stimulating hormone (TSH), resulting from
CC hypothalamic and/or pituitary dysfunction. CHTE patients have delayed
CC testosterone increase at puberty with normal testosterone levels in
CC adulthood, normal testicular volume in childhood and enlarged testicles
CC in adulthood. {ECO:0000269|PubMed:23143598}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
CC {ECO:0000305}.
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DR EMBL; Y10523; CAA71535.1; -; mRNA.
DR EMBL; AF034198; AAC52057.1; -; mRNA.
DR EMBL; AB058894; BAB40235.1; -; mRNA.
DR EMBL; AB002362; BAA20819.2; -; mRNA.
DR EMBL; AK226008; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL135784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137369; CAB70713.1; -; mRNA.
DR CCDS; CCDS14629.1; -. [Q8N6C5-1]
DR CCDS; CCDS14630.1; -. [Q8N6C5-3]
DR CCDS; CCDS55490.1; -. [Q8N6C5-2]
DR CCDS; CCDS55491.1; -. [Q8N6C5-4]
DR RefSeq; NP_001164432.1; NM_001170961.1. [Q8N6C5-4]
DR RefSeq; NP_001164433.1; NM_001170962.1. [Q8N6C5-2]
DR RefSeq; NP_001164434.1; NM_001170963.1. [Q8N6C5-3]
DR RefSeq; NP_001546.2; NM_001555.4. [Q8N6C5-1]
DR RefSeq; NP_991402.1; NM_205833.3. [Q8N6C5-3]
DR RefSeq; XP_011529632.1; XM_011531330.1. [Q8N6C5-4]
DR AlphaFoldDB; Q8N6C5; -.
DR SMR; Q8N6C5; -.
DR BioGRID; 109763; 15.
DR IntAct; Q8N6C5; 7.
DR MINT; Q8N6C5; -.
DR STRING; 9606.ENSP00000359940; -.
DR GlyGen; Q8N6C5; 14 sites.
DR iPTMnet; Q8N6C5; -.
DR PhosphoSitePlus; Q8N6C5; -.
DR BioMuta; IGSF1; -.
DR DMDM; 226694182; -.
DR EPD; Q8N6C5; -.
DR jPOST; Q8N6C5; -.
DR MassIVE; Q8N6C5; -.
DR MaxQB; Q8N6C5; -.
DR PaxDb; Q8N6C5; -.
DR PeptideAtlas; Q8N6C5; -.
DR PRIDE; Q8N6C5; -.
DR ProteomicsDB; 46220; -.
DR ProteomicsDB; 72153; -. [Q8N6C5-1]
DR ProteomicsDB; 72154; -. [Q8N6C5-2]
DR Antibodypedia; 16308; 191 antibodies from 20 providers.
DR DNASU; 3547; -.
DR Ensembl; ENST00000361420.8; ENSP00000355010.3; ENSG00000147255.19. [Q8N6C5-1]
DR Ensembl; ENST00000370900.5; ENSP00000359937.1; ENSG00000147255.19. [Q8N6C5-3]
DR Ensembl; ENST00000370901.4; ENSP00000359938.4; ENSG00000147255.19. [Q8N6C5-3]
DR Ensembl; ENST00000370903.8; ENSP00000359940.3; ENSG00000147255.19. [Q8N6C5-4]
DR Ensembl; ENST00000370904.6; ENSP00000359941.1; ENSG00000147255.19. [Q8N6C5-2]
DR Ensembl; ENST00000370910.5; ENSP00000359947.1; ENSG00000147255.19. [Q8N6C5-2]
DR Ensembl; ENST00000651556.1; ENSP00000498789.1; ENSG00000147255.19. [Q8N6C5-1]
DR GeneID; 3547; -.
DR KEGG; hsa:3547; -.
DR MANE-Select; ENST00000361420.8; ENSP00000355010.3; NM_001555.5; NP_001546.2.
DR UCSC; uc004ewd.5; human. [Q8N6C5-1]
DR CTD; 3547; -.
DR DisGeNET; 3547; -.
DR GeneCards; IGSF1; -.
DR HGNC; HGNC:5948; IGSF1.
DR HPA; ENSG00000147255; Group enriched (brain, pituitary gland).
DR MalaCards; IGSF1; -.
DR MIM; 300137; gene.
DR MIM; 300888; phenotype.
DR neXtProt; NX_Q8N6C5; -.
DR OpenTargets; ENSG00000147255; -.
DR Orphanet; 329235; X-linked central congenital hypothyroidism with late-onset testicular enlargement.
DR PharmGKB; PA29761; -.
DR VEuPathDB; HostDB:ENSG00000147255; -.
DR eggNOG; ENOG502RYEX; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_006143_0_0_1; -.
DR InParanoid; Q8N6C5; -.
DR OMA; GCGHGCW; -.
DR OrthoDB; 1327293at2759; -.
DR PhylomeDB; Q8N6C5; -.
DR TreeFam; TF336644; -.
DR PathwayCommons; Q8N6C5; -.
DR SignaLink; Q8N6C5; -.
DR BioGRID-ORCS; 3547; 9 hits in 705 CRISPR screens.
DR ChiTaRS; IGSF1; human.
DR GeneWiki; IGSF1; -.
DR GenomeRNAi; 3547; -.
DR Pharos; Q8N6C5; Tbio.
DR PRO; PR:Q8N6C5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8N6C5; protein.
DR Bgee; ENSG00000147255; Expressed in pituitary gland and 132 other tissues.
DR ExpressionAtlas; Q8N6C5; baseline and differential.
DR Genevisible; Q8N6C5; HS.
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; IDA:UniProtKB.
DR GO; GO:0038102; F:activin receptor antagonist activity; IDA:UniProtKB.
DR GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
DR GO; GO:0034711; F:inhibin binding; IDA:UniProtKB.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
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 InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 6.
DR SMART; SM00409; IG; 11.
DR SMART; SM00408; IGc2; 9.
DR SUPFAM; SSF48726; SSF48726; 12.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Congenital hypothyroidism; Disease variant;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1336
FT /note="Immunoglobulin superfamily member 1"
FT /id="PRO_0000318512"
FT TOPO_DOM 29..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..559
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..1336
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 38..122
FT /note="Ig-like C2-type 1"
FT DOMAIN 137..222
FT /note="Ig-like C2-type 2"
FT DOMAIN 226..312
FT /note="Ig-like C2-type 3"
FT DOMAIN 321..408
FT /note="Ig-like C2-type 4"
FT DOMAIN 419..500
FT /note="Ig-like C2-type 5"
FT DOMAIN 589..677
FT /note="Ig-like C2-type 6"
FT DOMAIN 686..760
FT /note="Ig-like C2-type 7"
FT DOMAIN 777..869
FT /note="Ig-like C2-type 8"
FT DOMAIN 873..958
FT /note="Ig-like C2-type 9"
FT DOMAIN 965..1060
FT /note="Ig-like C2-type 10"
FT DOMAIN 1065..1150
FT /note="Ig-like C2-type 11"
FT DOMAIN 1161..1242
FT /note="Ig-like C2-type 12"
FT REGION 1308..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1027
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1082
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 343..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 441..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 703..750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 799..849
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 895..942
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1087..1134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1183..1226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 24..33
FT /note="RMSLGMTSIV -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9205841,
FT ECO:0000303|PubMed:9521868"
FT /id="VSP_031195"
FT VAR_SEQ 224..242
FT /note="LYPKPTLTAHPGPIMAPGE -> GCGYGCWHLAIVVPGIMAG (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11854097"
FT /id="VSP_031196"
FT VAR_SEQ 243..1336
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11854097"
FT /id="VSP_031197"
FT VAR_SEQ 572
FT /note="C -> CAISFA (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_044554"
FT VARIANT 381
FT /note="N -> H (in dbSNP:rs6637826)"
FT /id="VAR_054960"
FT VARIANT 708..716
FT /note="Missing (in CHTE; impairs IGSF1 trafficking to the
FT plasma membrane)"
FT /evidence="ECO:0000269|PubMed:23143598"
FT /id="VAR_069268"
FT VARIANT 765
FT /note="S -> N (in CHTE; impairs IGSF1 trafficking to the
FT plasma membrane)"
FT /evidence="ECO:0000269|PubMed:23143598"
FT /id="VAR_069269"
FT VARIANT 774
FT /note="E -> G"
FT /evidence="ECO:0000269|PubMed:23092983"
FT /id="VAR_076256"
FT VARIANT 858
FT /note="S -> F (in CHTE; impairs IGSF1 trafficking to the
FT plasma membrane; dbSNP:rs397514622)"
FT /evidence="ECO:0000269|PubMed:23143598"
FT /id="VAR_069270"
FT VARIANT 942
FT /note="C -> R (in CHTE; impairs IGSF1 trafficking to the
FT plasma membrane)"
FT /evidence="ECO:0000269|PubMed:23143598"
FT /id="VAR_069271"
FT CONFLICT 397
FT /note="T -> A (in Ref. 5; AK226008)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="K -> R (in Ref. 1; CAA71535)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="I -> M (in Ref. 1; CAA71535)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="R -> L (in Ref. 1; CAA71535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1336 AA; 148936 MW; 7D0D2C36FD1CE8B8 CRC64;
MTLDRPGEGA TMLKTFTVLL FCIRMSLGMT SIVMDPQPEL WIESNYPQAP WENITLWCRS
PSRISSKFLL LKDKTQMTWI RPSHKTFQVS FLIGALTESN AGLYRCCYWK ETGWSKPSKV
LELEAPGQLP KPIFWIQAET PALPGCNVNI LCHGWLQDLV FMLFKEGYAE PVDYQVPTGT
MAIFSIDNLT PEDEGVYICR THIQMLPTLW SEPSNPLKLV VAGLYPKPTL TAHPGPIMAP
GESLNLRCQG PIYGMTFALM RVEDLEKSFY HKKTIKNEAN FFFQSLKIQD TGHYLCFYYD
ASYRGSLLSD VLKIWVTDTF PKTWLLARPS AVVQMGQNVS LRCRGPVDGV GLALYKKGED
KPLQFLDATS IDDNTSFFLN NVTYSDTGIY SCHYLLTWKT SIRMPSHNTV ELMVVDKPPK
PSLSAWPSTV FKLGKAITLQ CRVSHPVLEF SLEWEERETF QKFSVNGDFI ISNVDGKGTG
TYSCSYRVET HPNIWSHRSE PLKLMGPAGY LTWNYVLNEA IRLSLIMQLV ALLLVVLWIR
WKCRRLRIRE AWLLGTAQGV TMLFIVTALL CCGLCNGVLI EETEIVMPTP KPELWAETNF
PLAPWKNLTL WCRSPSGSTK EFVLLKDGTG WIATRPASEQ VRAAFPLGAL TQSHTGSYHC
HSWEEMAVSE PSEALELVGT DILPKPVISA SPTIRGQELQ LRCKGWLAGM GFALYKEGEQ
EPVQQLGAVG REAFFTIQRM EDKDEGNYSC RTHTEKRPFK WSEPSEPLEL VIKEMYPKPF
FKTWASPVVT PGARVTFNCS TPHQHMSFIL YKDGSEIASS DRSWASPGAS AAHFLIISVG
IGDGGNYSCR YYDFSIWSEP SDPVELVVTE FYPKPTLLAQ PGPVVFPGKS VILRCQGTFQ
GMRFALLQEG AHVPLQFRSV SGNSADFLLH TVGAEDSGNY SCIYYETTMS NRGSYLSMPL
MIWVTDTFPK PWLFAEPSSV VPMGQNVTLW CRGPVHGVGY ILHKEGEATS MQLWGSTSND
GAFPITNISG TSMGRYSCCY HPDWTSSIKI QPSNTLELLV TGLLPKPSLL AQPGPMVAPG
ENMTLQCQGE LPDSTFVLLK EGAQEPLEQQ RPSGYRADFW MPAVRGEDSG IYSCVYYLDS
TPFAASNHSD SLEIWVTDKP PKPSLSAWPS TMFKLGKDIT LQCRGPLPGV EFVLEHDGEE
APQQFSEDGD FVINNVEGKG IGNYSCSYRL QAYPDIWSEP SDPLELVGAA GPVAQECTVG
NIVRSSLIVV VVVALGVVLA IEWKKWPRLR TRGSETDGRD QTIALEECNQ EGEPGTPANS
PSSTSQRISV ELPVPI
