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 27-MAR-2024, entry version 166. 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; 29. DR IntAct; Q5ZPR3; 18. 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 GlyCosmos; Q5ZPR3; 7 sites, 37 glycans. DR GlyGen; Q5ZPR3; 9 sites, 37 N-linked glycans (3 sites), 1 O-linked glycan (2 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; 9606-ENSP00000320084; -. DR PeptideAtlas; Q5ZPR3; -. DR ProteomicsDB; 65865; -. [Q5ZPR3-1] DR ProteomicsDB; 65866; -. [Q5ZPR3-2] DR ProteomicsDB; 65867; -. [Q5ZPR3-3] DR ProteomicsDB; 65868; -. [Q5ZPR3-4] DR Pumba; Q5ZPR3; -. DR ABCD; Q5ZPR3; 60 sequenced antibodies. DR Antibodypedia; 2288; 1092 antibodies from 46 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 AGR; HGNC:19137; -. 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; DIEWERT; -. DR OrthoDB; 5354085at2759; -. DR PhylomeDB; Q5ZPR3; -. DR TreeFam; TF331083; -. DR PathwayCommons; Q5ZPR3; -. DR SignaLink; Q5ZPR3; -. DR BioGRID-ORCS; 80381; 20 hits in 1170 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 167 other cell types or tissues. DR ExpressionAtlas; Q5ZPR3; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; NAS:HGNC-UCL. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:HGNC-UCL. DR GO; GO:0032729; P:positive regulation of type II interferon production; 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 CDD; cd00096; Ig; 1. DR CDD; cd20934; IgV_B7-H3; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 4. DR InterPro; IPR047318; CD276_IgV. 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 PANTHER; PTHR24100; BUTYROPHILIN; 1. DR PANTHER; PTHR24100:SF147; CD276 ANTIGEN; 1. DR Pfam; PF13927; Ig_3; 2. 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; Immunoglobulin; 4. DR PROSITE; PS50835; IG_LIKE; 4. DR Genevisible; Q5ZPR3; HS. 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 //