CD276_MOUSE
ID CD276_MOUSE Reviewed; 316 AA.
AC Q8VE98;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=CD276 antigen;
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12055244; DOI=10.4049/jimmunol.168.12.6294;
RA Sun M., Richards S., Prasad D.V., Mai X.M., Rudensky A., Dong C.;
RT "Characterization of mouse and human B7-H3 genes.";
RL J. Immunol. 168:6294-6297(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=C57BL/6J;
RX PubMed=12925852; DOI=10.1038/ni967;
RA Suh W.-K., Gajewska B.U., Okada H., Gronski M.A., Bertram E.M., Dawicki W.,
RA Duncan G.S., Bukczynski J., Plyte S., Elia A., Wakeham A., Itie A.,
RA Chung S., Da Costa J., Arya S., Horan T., Campbell P., Gaida K.,
RA Ohashi P.S., Watts T.H., Yoshinaga S.K., Bray M.R., Jordana M., Mak T.W.;
RT "The B7 family member B7-H3 preferentially down-regulates T helper type 1-
RT mediated immune responses.";
RL Nat. Immunol. 4:899-906(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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 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 [6]
RP FUNCTION, AND GENE TRANSFER.
RX PubMed=12939639; DOI=10.1038/sj.gt.3302070;
RA Sun X., Vale M., Leung E., Kanwar J.R., Gupta R., Krissansen G.W.;
RT "Mouse B7-H3 induces antitumor immunity.";
RL Gene Ther. 10:1728-1734(2003).
RN [7]
RP FUNCTION.
RX PubMed=15294965; DOI=10.4049/jimmunol.173.4.2500;
RA Prasad D.V., Nguyen T., Li Z., Yang Y., Duong J., Wang Y., Dong C.;
RT "Murine B7-H3 is a negative regulator of T cells.";
RL J. Immunol. 173:2500-2506(2004).
RN [8]
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-189.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104; ASN-189 AND ASN-215.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: Modulates T-cell-mediated immune responses and the
CC development of acute and chronic transplant rejection. Plays a positive
CC regulatory role in bone formation and has a dual role in the bone-
CC immune interface. Induces antitumor immunity as it activates both
CC acquired and innate immunity leading to natural killer cell and CD8 T-
CC cell dependent killing of tumor cells. {ECO:0000269|PubMed:12055244,
CC ECO:0000269|PubMed:12925852, ECO:0000269|PubMed:12939639,
CC ECO:0000269|PubMed:15294965, ECO:0000269|PubMed:15682454}.
CC -!- SUBUNIT: Interacts with TREML2 and this interaction enhances T-cell
CC activation. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8VE98; Q8VE98: Cd276; NbExp=2; IntAct=EBI-16044767, EBI-16044767;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12055244}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in developing bones during
CC embryogenesis and expression increases as osteoblast precursor cells
CC differentiate into mature osteoblasts. {ECO:0000269|PubMed:12925852}.
CC -!- INDUCTION: Up-regulated in cells mediating rejection of mouse
CC transplant. {ECO:0000269|PubMed:15682454}.
CC -!- DISRUPTION PHENOTYPE: Mice display a lower bone mineral density in
CC cortical bones with femurs more susceptible to bone fracture, but do
CC not exhibit any important skeletal abnormalities. Calvarial cells
CC reveal normal number of osteoblast precursor cells with adequate
CC proliferative capacity, but have impaired osteogenic differentiation.
CC Furthermore, following cardiac transplantation, they display permanent
CC survival under rapamycin regimen and cardiac transplants also show
CC markedly decreased production of key cytokine and chemokine. The
CC incidence of chronic transplant rejection is also inhibited. Mice also
CC develop more severe airway inflammation and experimental autoimmune
CC encephalomyelitis earlier than wild-type littermates as well as
CC accumulate higher concentrations of autoantibodies to DNA.
CC {ECO:0000269|PubMed:12925852}.
CC -!- MISCELLANEOUS: Gene transfer of B7-H3 leads to complete regression of
CC 50 per cent tumors, or significantly slows tumor growth.
CC -!- MISCELLANEOUS: In primates, B7-H3 locus underwent genomic duplication
CC leading to tandemly repeated immunoglobulin-like V and C domains (VC
CC domains). The dominantly expressed human B7-H3 isoform contains
CC tandemly duplicated VC domains. In contrast, mouse B7-H3 transcript
CC contains only one single VC domain form due to an exon structure
CC corresponding to V domain-(pseudoexon C)-(pseudoexon V)-C domain. This
CC duplication appearing in primates is suggested to be very recent
CC supporting a model of multiple independent emergence of tandem VC
CC repeats within human and monkey species.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
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DR EMBL; AY190318; AAP04007.1; -; mRNA.
DR EMBL; AK155114; BAE33058.1; -; mRNA.
DR EMBL; BC019436; AAH19436.1; -; mRNA.
DR EMBL; BC056608; AAH56608.1; -; mRNA.
DR CCDS; CCDS23244.1; -.
DR RefSeq; NP_598744.1; NM_133983.4.
DR PDB; 4I0K; X-ray; 2.97 A; A=34-247.
DR PDBsum; 4I0K; -.
DR AlphaFoldDB; Q8VE98; -.
DR SMR; Q8VE98; -.
DR DIP; DIP-60156N; -.
DR STRING; 10090.ENSMUSP00000129418; -.
DR GlyGen; Q8VE98; 3 sites.
DR iPTMnet; Q8VE98; -.
DR PhosphoSitePlus; Q8VE98; -.
DR MaxQB; Q8VE98; -.
DR PaxDb; Q8VE98; -.
DR PeptideAtlas; Q8VE98; -.
DR PRIDE; Q8VE98; -.
DR ProteomicsDB; 265622; -.
DR Antibodypedia; 2288; 903 antibodies from 45 providers.
DR Ensembl; ENSMUST00000039788; ENSMUSP00000042681; ENSMUSG00000035914.
DR Ensembl; ENSMUST00000165365; ENSMUSP00000129418; ENSMUSG00000035914.
DR GeneID; 102657; -.
DR KEGG; mmu:102657; -.
DR UCSC; uc009pxb.1; mouse.
DR CTD; 80381; -.
DR MGI; MGI:2183926; Cd276.
DR VEuPathDB; HostDB:ENSMUSG00000035914; -.
DR eggNOG; ENOG502QU94; Eukaryota.
DR GeneTree; ENSGT00940000154641; -.
DR HOGENOM; CLU_013137_8_1_1; -.
DR InParanoid; Q8VE98; -.
DR OMA; AQLSLIW; -.
DR OrthoDB; 1254753at2759; -.
DR PhylomeDB; Q8VE98; -.
DR TreeFam; TF331083; -.
DR BioGRID-ORCS; 102657; 7 hits in 77 CRISPR screens.
DR ChiTaRS; Cd276; mouse.
DR PRO; PR:Q8VE98; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VE98; protein.
DR Bgee; ENSMUSG00000035914; Expressed in embryonic post-anal tail and 191 other tissues.
DR ExpressionAtlas; Q8VE98; baseline and differential.
DR Genevisible; Q8VE98; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IMP:MGI.
DR GO; GO:0042110; P:T cell activation; ISO:MGI.
DR GO; GO:0042098; P:T cell proliferation; IDA:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
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 Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..316
FT /note="CD276 antigen"
FT /id="PRO_0000045802"
FT TOPO_DOM 29..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..139
FT /note="Ig-like V-type"
FT DOMAIN 145..238
FT /note="Ig-like C2-type"
FT REGION 280..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 165..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4I0K"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:4I0K"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:4I0K"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4I0K"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4I0K"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 159..172
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:4I0K"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:4I0K"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:4I0K"
SQ SEQUENCE 316 AA; 34001 MW; 7BA30B1E67F55827 CRC64;
MLRGWGGPSV GVCVRTALGV LCLCLTGAVE VQVSEDPVVA LVDTDATLRC SFSPEPGFSL
AQLNLIWQLT DTKQLVHSFT EGRDQGSAYS NRTALFPDLL VQGNASLRLQ RVRVTDEGSY
TCFVSIQDFD SAAVSLQVAA PYSKPSMTLE PNKDLRPGNM VTITCSSYQG YPEAEVFWKD
GQGVPLTGNV TTSQMANERG LFDVHSVLRV VLGANGTYSC LVRNPVLQQD AHGSVTITGQ
PLTFPPEALW VTVGLSVCLV VLLVALAFVC WRKIKQSCEE ENAGAEDQDG DGEGSKTALR
PLKPSENKED DGQEIA
