CD276_HUMAN
ID CD276_HUMAN Reviewed; 534 AA.
AC Q5ZPR3; Q6P5Y4; Q6UXI2; Q8NBI8; Q8NC34; Q8NCB6; Q9BXR1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=CD276 antigen;
DE AltName: Full=4Ig-B7-H3;
DE AltName: Full=B7 homolog 3;
DE Short=B7-H3;
DE AltName: Full=Costimulatory molecule;
DE AltName: CD_antigen=CD276;
DE Flags: Precursor;
GN Name=CD276; Synonyms=B7H3; ORFNames=PSEC0249, UNQ309/PRO352;
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 2), TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=11224528; DOI=10.1038/85339;
RA Chapoval A.I., Ni J., Lau J.S., Wilcox R.A., Flies D.B., Liu D., Dong H.,
RA Sica G.L., Zhu G., Tamada K., Chen L.;
RT "B7-H3: a costimulatory molecule for T cell activation and IFN-gamma
RT production.";
RL Nat. Immunol. 2:269-274(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, AND
RP INDUCTION.
RX PubMed=14764704; DOI=10.4049/jimmunol.172.4.2352;
RA Steinberger P., Majdic O., Derdak S.V., Pfistershammer K., Kirchberger S.,
RA Klauser C., Zlabinger G., Pickl W.F., Stockl J., Knapp W.;
RT "Molecular characterization of human 4Ig-B7-H3, a member of the B7 family
RT with four Ig-like domains.";
RL J. Immunol. 172:2352-2359(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 91-534 (ISOFORM 1), AND VARIANT MET-160.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-160.
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Lung;
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 [7]
RP PROTEIN SEQUENCE OF 29-43.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP FUNCTION, AND GENOMIC DOMAIN DUPLICATION.
RX PubMed=12906861; DOI=10.1016/s0888-7543(03)00126-5;
RA Ling V., Wu P.W., Spaulding V., Kieleczawa J., Luxenberg D., Carreno B.M.,
RA Collins M.;
RT "Duplication of primate and rodent B7-H3 immunoglobulin V- and C-like
RT domains: divergent history of functional redundancy and exon loss.";
RL Genomics 82:365-377(2003).
RN [9]
RP FUNCTION.
RX PubMed=15314238; DOI=10.1073/pnas.0405025101;
RA Castriconi R., Dondero A., Augugliaro R., Cantoni C., Carnemolla B.,
RA Sementa A.R., Negri F., Conte R., Corrias M.V., Moretta L., Moretta A.,
RA Bottino C.;
RT "Identification of 4Ig-B7-H3 as a neuroblastoma-associated molecule that
RT exerts a protective role from an NK cell-mediated lysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12640-12645(2004).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=16049332; DOI=10.1016/s0002-9440(10)62990-2;
RA Petroff M.G., Kharatyan E., Torry D.S., Holets L.;
RT "The immunomodulatory proteins B7-DC, B7-H2, and B7-H3 are differentially
RT expressed across gestation in the human placenta.";
RL Am. J. Pathol. 167:465-473(2005).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15961727; DOI=10.1165/rcmb.2004-0129oc;
RA Kim J., Myers A.C., Chen L., Pardoll D.M., Truong-Tran Q.A., Lane A.P.,
RA McDyer J.F., Fortuno L., Schleimer R.P.;
RT "Constitutive and inducible expression of B7 family of ligands by human
RT airway epithelial cells.";
RL Am. J. Respir. Cell Mol. Biol. 33:280-289(2005).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=16274630;
RA Zhang G.B., Dong Q.M., Xu Y., Yu G.H., Zhang X.G.;
RT "B7-H3: another molecule marker for Mo-DCs?";
RL Cell. Mol. Immunol. 2:307-311(2005).
RN [13]
RP FUNCTION, AND INDUCTION.
RX PubMed=15682454; DOI=10.1002/eji.200425518;
RA Wang L., Fraser C.C., Kikly K., Wells A.D., Han R., Coyle A.J., Chen L.,
RA Hancock W.W.;
RT "B7-H3 promotes acute and chronic allograft rejection.";
RL Eur. J. Immunol. 35:428-438(2005).
RN [14]
RP INTERACTION WITH TREML2.
RX PubMed=18650384; DOI=10.1073/pnas.0802423105;
RA Hashiguchi M., Kobori H., Ritprajak P., Kamimura Y., Kozono H., Azuma M.;
RT "Triggering receptor expressed on myeloid cell-like transcript 2 (TLT-2) is
RT a counter-receptor for B7-H3 and enhances T cell responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10495-10500(2008).
RN [15]
RP ERRATUM OF PUBMED:18650384.
RA Hashiguchi M., Kobori H., Ritprajak P., Kamimura Y., Kozono H., Azuma M.;
RL Proc. Natl. Acad. Sci. U.S.A. 105:14744-14744(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-322 AND ASN-407.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May participate in the regulation of T-cell-mediated immune
CC response. May play a protective role in tumor cells by inhibiting
CC natural-killer mediated cell lysis as well as a role of marker for
CC detection of neuroblastoma cells. May be involved in the development of
CC acute and chronic transplant rejection and in the regulation of
CC lymphocytic activity at mucosal surfaces. Could also play a key role in
CC providing the placenta and fetus with a suitable immunological
CC environment throughout pregnancy. Both isoform 1 and isoform 2 appear
CC to be redundant in their ability to modulate CD4 T-cell responses.
CC Isoform 2 is shown to enhance the induction of cytotoxic T-cells and
CC selectively stimulates interferon gamma production in the presence of
CC T-cell receptor signaling. {ECO:0000269|PubMed:11224528,
CC ECO:0000269|PubMed:12906861, ECO:0000269|PubMed:14764704,
CC ECO:0000269|PubMed:15314238, ECO:0000269|PubMed:15682454,
CC ECO:0000269|PubMed:15961727}.
CC -!- SUBUNIT: Interacts with TREML2 and this interaction enhances T-cell
CC activation. {ECO:0000269|PubMed:18650384}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=4Ig-B7-H3;
CC IsoId=Q5ZPR3-1; Sequence=Displayed;
CC Name=2; Synonyms=B7-H3;
CC IsoId=Q5ZPR3-2; Sequence=VSP_017088;
CC Name=3;
CC IsoId=Q5ZPR3-3; Sequence=VSP_017089, VSP_017090;
CC Name=4;
CC IsoId=Q5ZPR3-4; Sequence=VSP_017091;
CC -!- TISSUE SPECIFICITY: Ubiquitous but not detectable in peripheral blood
CC lymphocytes or granulocytes. Weakly expressed in resting monocytes.
CC Expressed in dendritic cells derived from monocytes. Expressed in
CC epithelial cells of sinonasal tissue. Expressed in extravillous
CC trophoblast cells and Hofbauer cells of the first trimester placenta
CC and term placenta. {ECO:0000269|PubMed:11224528,
CC ECO:0000269|PubMed:14764704, ECO:0000269|PubMed:15961727,
CC ECO:0000269|PubMed:16049332, ECO:0000269|PubMed:16274630}.
CC -!- INDUCTION: By bacterial lipopolysaccharides (LPS) in monocytes and by
CC ionomycin in T and B-lymphocytes. Up-regulated in cells mediating
CC rejection of human transplants. {ECO:0000269|PubMed:14764704,
CC ECO:0000269|PubMed:15682454}.
CC -!- MISCELLANEOUS: B7-H3 locus underwent genomic duplication leading to
CC tandemly repeated immunoglobulin-like V and C domains (VC domains). The
CC dominantly expressed human B7-H3 isoform contains tandemly duplicated
CC VC domains. In contrast, mouse B7-H3 transcript contains only one
CC single VC domain form due to an exon structure corresponding to V
CC domain-(pseudoexon C)-(pseudoexon V)-C domain. This duplication
CC appearing in primates is suggested to be very recent supporting a model
CC of multiple independent emergence of tandem VC repeats within human and
CC monkey species.
CC -!- MISCELLANEOUS: [Isoform 1]: Contains tandemly repeated immunoglobulin-
CC like V and C domains.
CC -!- MISCELLANEOUS: [Isoform 2]: Minor transcript. Contains one single set
CC of immunoglobulin-like V and C domains. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Contains tandemly repeated immunoglobulin-
CC like V and C domains. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Contains tandemly repeated immunoglobulin-
CC like V and C domains. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11344.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF302102; AAK15438.1; -; mRNA.
DR EMBL; AJ583695; CAE47548.1; -; mRNA.
DR EMBL; AY358343; AAQ88709.1; -; mRNA.
DR EMBL; AK074849; BAC11243.1; -; mRNA.
DR EMBL; AK074997; BAC11344.1; ALT_INIT; mRNA.
DR EMBL; AK075549; BAC11692.1; -; mRNA.
DR EMBL; BC062581; AAH62581.1; -; mRNA.
DR CCDS; CCDS10251.1; -. [Q5ZPR3-2]
DR CCDS; CCDS32288.1; -. [Q5ZPR3-1]
DR RefSeq; NP_001019907.1; NM_001024736.1. [Q5ZPR3-1]
DR RefSeq; NP_001316557.1; NM_001329628.1. [Q5ZPR3-2]
DR RefSeq; NP_001316558.1; NM_001329629.1.
DR RefSeq; NP_079516.1; NM_025240.2. [Q5ZPR3-2]
DR RefSeq; XP_005254757.1; XM_005254700.4. [Q5ZPR3-1]
DR RefSeq; XP_011520397.1; XM_011522095.2. [Q5ZPR3-1]
DR RefSeq; XP_011520398.1; XM_011522096.2.
DR RefSeq; XP_016878127.1; XM_017022638.1. [Q5ZPR3-1]
DR AlphaFoldDB; Q5ZPR3; -.
DR BioGRID; 123260; 25.
DR IntAct; Q5ZPR3; 15.
DR MINT; Q5ZPR3; -.
DR STRING; 9606.ENSP00000320084; -.
DR ChEMBL; CHEMBL3712879; -.
DR DrugBank; DB15635; Omburtamab.
DR GuidetoPHARMACOLOGY; 2938; -.
DR GlyConnect; 1087; 38 N-Linked glycans (3 sites).
DR GlyGen; Q5ZPR3; 7 sites, 37 N-linked glycans (3 sites).
DR iPTMnet; Q5ZPR3; -.
DR PhosphoSitePlus; Q5ZPR3; -.
DR SwissPalm; Q5ZPR3; -.
DR BioMuta; CD276; -.
DR DMDM; 74757248; -.
DR EPD; Q5ZPR3; -.
DR jPOST; Q5ZPR3; -.
DR MassIVE; Q5ZPR3; -.
DR MaxQB; Q5ZPR3; -.
DR PaxDb; Q5ZPR3; -.
DR PeptideAtlas; Q5ZPR3; -.
DR PRIDE; Q5ZPR3; -.
DR ProteomicsDB; 65865; -. [Q5ZPR3-1]
DR ProteomicsDB; 65866; -. [Q5ZPR3-2]
DR ProteomicsDB; 65867; -. [Q5ZPR3-3]
DR ProteomicsDB; 65868; -. [Q5ZPR3-4]
DR ABCD; Q5ZPR3; 60 sequenced antibodies.
DR Antibodypedia; 2288; 903 antibodies from 45 providers.
DR CPTC; Q5ZPR3; 1 antibody.
DR DNASU; 80381; -.
DR Ensembl; ENST00000318424.9; ENSP00000320058.5; ENSG00000103855.18. [Q5ZPR3-2]
DR Ensembl; ENST00000318443.10; ENSP00000320084.5; ENSG00000103855.18. [Q5ZPR3-1]
DR Ensembl; ENST00000561213.5; ENSP00000452736.1; ENSG00000103855.18. [Q5ZPR3-4]
DR Ensembl; ENST00000564751.5; ENSP00000454940.1; ENSG00000103855.18. [Q5ZPR3-2]
DR GeneID; 80381; -.
DR KEGG; hsa:80381; -.
DR MANE-Select; ENST00000318443.10; ENSP00000320084.5; NM_001024736.2; NP_001019907.1.
DR UCSC; uc002avu.2; human. [Q5ZPR3-1]
DR CTD; 80381; -.
DR DisGeNET; 80381; -.
DR GeneCards; CD276; -.
DR HGNC; HGNC:19137; CD276.
DR HPA; ENSG00000103855; Low tissue specificity.
DR MIM; 605715; gene.
DR neXtProt; NX_Q5ZPR3; -.
DR OpenTargets; ENSG00000103855; -.
DR PharmGKB; PA142672148; -.
DR VEuPathDB; HostDB:ENSG00000103855; -.
DR eggNOG; ENOG502QU94; Eukaryota.
DR GeneTree; ENSGT00940000154641; -.
DR HOGENOM; CLU_510842_0_0_1; -.
DR InParanoid; Q5ZPR3; -.
DR OMA; TCKSHGW; -.
DR OrthoDB; 1254753at2759; -.
DR PhylomeDB; Q5ZPR3; -.
DR TreeFam; TF331083; -.
DR PathwayCommons; Q5ZPR3; -.
DR SignaLink; Q5ZPR3; -.
DR BioGRID-ORCS; 80381; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; CD276; human.
DR GeneWiki; CD276; -.
DR GenomeRNAi; 80381; -.
DR Pharos; Q5ZPR3; Tbio.
DR PRO; PR:Q5ZPR3; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q5ZPR3; protein.
DR Bgee; ENSG00000103855; Expressed in stromal cell of endometrium and 165 other tissues.
DR ExpressionAtlas; Q5ZPR3; baseline and differential.
DR Genevisible; Q5ZPR3; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:HGNC-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:HGNC-UCL.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:HGNC-UCL.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; NAS:HGNC-UCL.
DR GO; GO:0042110; P:T cell activation; IDA:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00407; IGc1; 2.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00406; IGv; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 29..534
FT /note="CD276 antigen"
FT /id="PRO_0000045801"
FT TOPO_DOM 29..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..139
FT /note="Ig-like V-type 1"
FT DOMAIN 145..238
FT /note="Ig-like C2-type 1"
FT DOMAIN 243..357
FT /note="Ig-like V-type 2"
FT DOMAIN 363..456
FT /note="Ig-like C2-type 2"
FT REGION 498..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 165..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 268..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 383..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 159..376
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11224528,
FT ECO:0000303|PubMed:12975309"
FT /id="VSP_017088"
FT VAR_SEQ 465..493
FT /note="EALWVTVGLSVCLIALLVALAFVCWRKIK -> GPASSAVPLSPAHPPHGSM
FT CWSHWFSRGL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017089"
FT VAR_SEQ 494..534
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017090"
FT VAR_SEQ 528..534
FT /note="DDGQEIA -> GKDTWA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017091"
FT VARIANT 97
FT /note="P -> L (in dbSNP:rs7173448)"
FT /id="VAR_049857"
FT VARIANT 111
FT /note="R -> S (in dbSNP:rs7173476)"
FT /id="VAR_049858"
FT VARIANT 137
FT /note="Q -> L (in dbSNP:rs11574477)"
FT /id="VAR_049859"
FT VARIANT 160
FT /note="T -> M (in dbSNP:rs11574479)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16303743"
FT /id="VAR_049860"
FT VARIANT 267
FT /note="R -> H (in dbSNP:rs11574483)"
FT /id="VAR_049861"
FT VARIANT 279
FT /note="A -> T (in dbSNP:rs10083681)"
FT /id="VAR_049862"
FT VARIANT 315
FT /note="P -> L (in dbSNP:rs148625372)"
FT /id="VAR_049863"
FT VARIANT 329
FT /note="R -> S (in dbSNP:rs7173476)"
FT /id="VAR_049864"
FT VARIANT 378
FT /note="T -> M (in dbSNP:rs145827704)"
FT /id="VAR_049865"
FT CONFLICT 387
FT /note="R -> Q (in Ref. 3; AAQ88709)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="L -> P (in Ref. 4; BAC11243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 57235 MW; 2181A064404C7939 CRC64;
MLRRRGSPGM GVHVGAALGA LWFCLTGALE VQVPEDPVVA LVGTDATLCC SFSPEPGFSL
AQLNLIWQLT DTKQLVHSFA EGQDQGSAYA NRTALFPDLL AQGNASLRLQ RVRVADEGSF
TCFVSIRDFG SAAVSLQVAA PYSKPSMTLE PNKDLRPGDT VTITCSSYQG YPEAEVFWQD
GQGVPLTGNV TTSQMANEQG LFDVHSILRV VLGANGTYSC LVRNPVLQQD AHSSVTITPQ
RSPTGAVEVQ VPEDPVVALV GTDATLRCSF SPEPGFSLAQ LNLIWQLTDT KQLVHSFTEG
RDQGSAYANR TALFPDLLAQ GNASLRLQRV RVADEGSFTC FVSIRDFGSA AVSLQVAAPY
SKPSMTLEPN KDLRPGDTVT ITCSSYRGYP EAEVFWQDGQ GVPLTGNVTT SQMANEQGLF
DVHSVLRVVL GANGTYSCLV RNPVLQQDAH GSVTITGQPM TFPPEALWVT VGLSVCLIAL
LVALAFVCWR KIKQSCEEEN AGAEDQDGEG EGSKTALQPL KHSDSKEDDG QEIA
