IGS11_HUMAN
ID IGS11_HUMAN Reviewed; 431 AA.
AC Q5DX21; C9JZN0; Q8N4F1; Q8N7T8; Q8NDD2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Immunoglobulin superfamily member 11;
DE Short=IgSF11;
DE AltName: Full=Brain and testis-specific immunoglobulin superfamily protein;
DE Short=Bt-IGSF;
DE AltName: Full=V-set and immunoglobulin domain-containing protein 3;
DE Flags: Precursor;
GN Name=IGSF11; Synonyms=BTIGSF, CXADRL1, VSIG3;
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), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT ASP-333.
RC TISSUE=Kidney;
RX PubMed=16108831; DOI=10.1111/j.1349-7006.2005.00073.x;
RA Watanabe T., Suda T., Tsunoda T., Uchida N., Ura K., Kato T., Hasegawa S.,
RA Satoh S., Ohgi S., Tahara H., Furukawa Y., Nakamura Y.;
RT "Identification of immunoglobulin superfamily 11 (IGSF11) as a novel target
RT for cancer immunotherapy of gastrointestinal and hepatocellular
RT carcinomas.";
RL Cancer Sci. 96:498-506(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS THR-39 AND
RP ASP-333.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-39.
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-431 (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP IDENTIFICATION, AND ALTERNATIVE SPLICING.
RX PubMed=12851705;
RA Katoh M., Katoh M.;
RT "IGSF11 gene, frequently up-regulated in intestinal-type gastric cancer,
RT encodes adhesion molecule homologous to CXADR, FLJ22415 and ESAM.";
RL Int. J. Oncol. 23:525-531(2003).
RN [7]
RP FUNCTION.
RX PubMed=15795899; DOI=10.1002/jcp.20361;
RA Harada H., Suzu S., Hayashi Y., Okada S.;
RT "BT-IgSF, a novel immunoglobulin superfamily protein, functions as a cell
RT adhesion molecule.";
RL J. Cell. Physiol. 204:919-926(2005).
CC -!- FUNCTION: Functions as a cell adhesion molecule through homophilic
CC interaction. Stimulates cell growth. {ECO:0000269|PubMed:15795899,
CC ECO:0000269|PubMed:16108831}.
CC -!- INTERACTION:
CC Q5DX21-2; Q9BS40: LXN; NbExp=3; IntAct=EBI-12178037, EBI-1044504;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5DX21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DX21-2; Sequence=VSP_030936;
CC Name=3;
CC IsoId=Q5DX21-3; Sequence=VSP_030936, VSP_030937;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in testis and ovary and to a
CC lower extent in brain, kidney and skeletal muscle.
CC {ECO:0000269|PubMed:16108831}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: The last 20 cytoplasmic amino acids are not required for
CC the cell adhesion function.
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DR EMBL; AB071618; BAD90695.1; -; mRNA.
DR EMBL; AK097667; BAC05139.1; -; mRNA.
DR EMBL; AC007023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034411; AAH34411.1; -; mRNA.
DR EMBL; AL834256; CAD38931.1; -; mRNA.
DR CCDS; CCDS2983.1; -. [Q5DX21-2]
DR CCDS; CCDS46891.1; -. [Q5DX21-1]
DR CCDS; CCDS87125.1; -. [Q5DX21-3]
DR RefSeq; NP_001015887.1; NM_001015887.1. [Q5DX21-1]
DR RefSeq; NP_689751.2; NM_152538.2. [Q5DX21-2]
DR RefSeq; XP_011510771.1; XM_011512469.1. [Q5DX21-2]
DR RefSeq; XP_011510772.1; XM_011512470.1.
DR RefSeq; XP_011510774.1; XM_011512472.1.
DR AlphaFoldDB; Q5DX21; -.
DR SMR; Q5DX21; -.
DR BioGRID; 127445; 2.
DR IntAct; Q5DX21; 1.
DR STRING; 9606.ENSP00000377370; -.
DR GlyGen; Q5DX21; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q5DX21; -.
DR PhosphoSitePlus; Q5DX21; -.
DR BioMuta; IGSF11; -.
DR DMDM; 311033430; -.
DR jPOST; Q5DX21; -.
DR MassIVE; Q5DX21; -.
DR PaxDb; Q5DX21; -.
DR PeptideAtlas; Q5DX21; -.
DR PRIDE; Q5DX21; -.
DR ProteomicsDB; 62754; -. [Q5DX21-1]
DR ProteomicsDB; 62755; -. [Q5DX21-2]
DR ProteomicsDB; 62756; -. [Q5DX21-3]
DR TopDownProteomics; Q5DX21-1; -. [Q5DX21-1]
DR Antibodypedia; 46572; 220 antibodies from 26 providers.
DR DNASU; 152404; -.
DR Ensembl; ENST00000354673.6; ENSP00000346700.2; ENSG00000144847.13. [Q5DX21-2]
DR Ensembl; ENST00000393775.7; ENSP00000377370.2; ENSG00000144847.13. [Q5DX21-1]
DR Ensembl; ENST00000425327.6; ENSP00000406092.2; ENSG00000144847.13. [Q5DX21-2]
DR Ensembl; ENST00000441144.6; ENSP00000401240.2; ENSG00000144847.13. [Q5DX21-3]
DR GeneID; 152404; -.
DR KEGG; hsa:152404; -.
DR MANE-Select; ENST00000393775.7; ENSP00000377370.2; NM_001015887.3; NP_001015887.1.
DR UCSC; uc003ebw.5; human. [Q5DX21-1]
DR CTD; 152404; -.
DR DisGeNET; 152404; -.
DR GeneCards; IGSF11; -.
DR HGNC; HGNC:16669; IGSF11.
DR HPA; ENSG00000144847; Group enriched (brain, ovary, retina, testis).
DR MIM; 608351; gene.
DR neXtProt; NX_Q5DX21; -.
DR OpenTargets; ENSG00000144847; -.
DR PharmGKB; PA134939253; -.
DR VEuPathDB; HostDB:ENSG00000144847; -.
DR eggNOG; ENOG502QV48; Eukaryota.
DR GeneTree; ENSGT00940000156392; -.
DR InParanoid; Q5DX21; -.
DR OMA; WHNPKPS; -.
DR OrthoDB; 841952at2759; -.
DR PhylomeDB; Q5DX21; -.
DR TreeFam; TF330875; -.
DR PathwayCommons; Q5DX21; -.
DR SignaLink; Q5DX21; -.
DR BioGRID-ORCS; 152404; 11 hits in 1065 CRISPR screens.
DR ChiTaRS; IGSF11; human.
DR GenomeRNAi; 152404; -.
DR Pharos; Q5DX21; Tbio.
DR PRO; PR:Q5DX21; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q5DX21; protein.
DR Bgee; ENSG00000144847; Expressed in secondary oocyte and 127 other tissues.
DR ExpressionAtlas; Q5DX21; baseline and differential.
DR Genevisible; Q5DX21; HS.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IMP:UniProtKB.
DR GO; GO:0045185; P:maintenance of protein location; IEA:Ensembl.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0061885; P:positive regulation of mini excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR013106; Ig_V-set.
DR InterPro; IPR042758; IGSF11.
DR PANTHER; PTHR44699; PTHR44699; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Growth regulation; Immunoglobulin domain; Membrane;
KW Methylation; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..431
FT /note="Immunoglobulin superfamily member 11"
FT /id="PRO_0000317370"
FT TOPO_DOM 23..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..136
FT /note="Ig-like V-type"
FT DOMAIN 144..234
FT /note="Ig-like C2-type"
FT REGION 379..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 378
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P0C673"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 165..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..17
FT /note="MTSQRSPLAPLLLLSLH -> MSLVELLLWWNCFSRT (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030936"
FT VAR_SEQ 211..235
FT /note="GLYQCVASNAIGTSTCLLDLQVISP -> A (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030937"
FT VARIANT 39
FT /note="P -> T (in dbSNP:rs2903250)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_038516"
FT VARIANT 333
FT /note="E -> D (in dbSNP:rs36052974)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16108831"
FT /id="VAR_038517"
FT VARIANT 388
FT /note="S -> N (in dbSNP:rs34908332)"
FT /id="VAR_056048"
FT CONFLICT 267
FT /note="Y -> H (in Ref. 2; BAC05139)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="V -> A (in Ref. 2; BAC05139)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="K -> E (in Ref. 1; BAD90695)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 46120 MW; 724985A1F8DEA8FC CRC64;
MTSQRSPLAP LLLLSLHGVA ASLEVSESPG SIQVARGQPA VLPCTFTTSA ALINLNVIWM
VTPLSNANQP EQVILYQGGQ MFDGAPRFHG RVGFTGTMPA TNVSIFINNT QLSDTGTYQC
LVNNLPDIGG RNIGVTGLTV LVPPSAPHCQ IQGSQDIGSD VILLCSSEEG IPRPTYLWEK
LDNTLKLPPT ATQDQVQGTV TIRNISALSS GLYQCVASNA IGTSTCLLDL QVISPQPRNI
GLIAGAIGTG AVIIIFCIAL ILGAFFYWRS KNKEEEEEEI PNEIREDDLP PKCSSAKAFH
TEISSSDNNT LTSSNAYNSR YWSNNPKVHR NTESVSHFSD LGQSFSFHSG NANIPSIYAN
GTHLVPGQHK TLVVTANRGS SPQVMSRSNG SVSRKPRPPH THSYTISHAT LERIGAVPVM
VPAQSRAGSL V