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Q8VE98 (CD276_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CD276 antigen
Alternative name(s):
B7 homolog 3
Short name=B7-H3
Costimulatory molecule
CD_antigen=CD276
Gene names
Name:Cd276
Synonyms:B7h3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modulates T-cell-mediated immune responses and the development of acute and chronic transplant rejection. Plays a positive regulatory role in bone formation and has a dual role in the bone-immune interface. Induces antitumor immunity as it activates both acquired and innate immunity leading to natural killer cell and CD8 T-cell dependent killing of tumor cells. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8

Subunit structure

Interacts with TREML2 and this interaction enhances T-cell activation By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein Probable.

Tissue specificity

Ubiquitous. Ref.1

Developmental stage

Highly expressed in developing bones during embryogenesis and expression increases as osteoblast precursor cells differentiate into mature osteoblasts. Ref.2

Induction

Up-regulated in cells mediating rejection of mouse transplant. Ref.8

Disruption phenotype

Mice display a lower bone mineral density in cortical bones with femurs more susceptible to bone fracture, but do not exhibit any important skeletal abnormalities. Calvarial cells reveal normal number of osteoblast precursor cells with adequate proliferative capacity, but have impaired osteogenic differentiation. Furthermore, following cardiac transplantation, they display permanent survival under rapamycin regimen and cardiac transplants also show markedly decreased production of key cytokine and chemokine. The incidence of chronic transplant rejection is also inhibited. Mice also develop more severe airway inflammation and experimental autoimmune encephalomyelitis earlier than wild-type littermates as well as accumulate higher concentrations of autoantibodies to DNA. Ref.2

Miscellaneous

Gene transfer of B7-H3 leads to complete regression of 50 per cent tumors, or significantly slows tumor growth.

In primates, B7-H3 locus underwent genomic duplication leading to tandemly repeated immunoglobulin-like V and C domains (VC domains). The dominantly expressed human B7-H3 isoform containstandemly duplicated VC domains. In contrast, mouse B7-H3 transcript contains only one single VC domain form due to an exon structure corresponding to V domain-(pseudoexon C)-(pseudoexon V)-C domain. This duplication appearing in primates is suggested to be very recent supporting a model of multiple independent emergence of tandem VC repeats within human and monkey species.

Sequence similarities

Belongs to the immunoglobulin superfamily. BTN/MOG family.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainImmunoglobulin domain
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell activation

Inferred from electronic annotation. Source: Ensembl

negative regulation of T cell proliferation

Inferred from direct assay Ref.2. Source: MGI

negative regulation of inflammatory response

Inferred from mutant phenotype Ref.2. Source: MGI

negative regulation of interferon-gamma biosynthetic process

Inferred from direct assay Ref.2. Source: MGI

negative regulation of interleukin-2 biosynthetic process

Inferred from direct assay Ref.2. Source: MGI

positive regulation of T cell proliferation

Inferred from mutant phenotype PubMed 16751379. Source: MGI

positive regulation of bone mineralization

Inferred from mutant phenotype PubMed 15317945. Source: MGI

positive regulation of interferon-gamma biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-2 secretion

Inferred from mutant phenotype PubMed 16751379. Source: MGI

positive regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 15317945. Source: MGI

regulation of immune response

Inferred from mutant phenotype Ref.2. Source: MGI

   Cellular_componentexternal side of plasma membrane

Inferred from direct assay Ref.2PubMed 15317945. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionreceptor binding

Inferred from direct assay Ref.1PubMed 16751379. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 316288CD276 antigen
PRO_0000045802

Regions

Topological domain29 – 248220Extracellular Potential
Transmembrane249 – 26921Helical; Potential
Topological domain270 – 31647Cytoplasmic Potential
Domain29 – 139111Ig-like V-type
Domain145 – 23894Ig-like C2-type

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Ref.9 Ref.10
Glycosylation1891N-linked (GlcNAc...) Ref.9 Ref.10
Glycosylation1971N-linked (GlcNAc...); atypical Ref.9
Glycosylation2151N-linked (GlcNAc...) Ref.10
Disulfide bond165 ↔ 220 By similarity

Secondary structure

.................................. 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8VE98 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 7BA30B1E67F55827

FASTA31634,001
        10         20         30         40         50         60 
MLRGWGGPSV GVCVRTALGV LCLCLTGAVE VQVSEDPVVA LVDTDATLRC SFSPEPGFSL 

        70         80         90        100        110        120 
AQLNLIWQLT DTKQLVHSFT EGRDQGSAYS NRTALFPDLL VQGNASLRLQ RVRVTDEGSY 

       130        140        150        160        170        180 
TCFVSIQDFD SAAVSLQVAA PYSKPSMTLE PNKDLRPGNM VTITCSSYQG YPEAEVFWKD 

       190        200        210        220        230        240 
GQGVPLTGNV TTSQMANERG LFDVHSVLRV VLGANGTYSC LVRNPVLQQD AHGSVTITGQ 

       250        260        270        280        290        300 
PLTFPPEALW VTVGLSVCLV VLLVALAFVC WRKIKQSCEE ENAGAEDQDG DGEGSKTALR 

       310 
PLKPSENKED DGQEIA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of mouse and human B7-H3 genes."
Sun M., Richards S., Prasad D.V., Mai X.M., Rudensky A., Dong C.
J. Immunol. 168:6294-6297(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"The B7 family member B7-H3 preferentially down-regulates T helper type 1-mediated immune responses."
Suh W.-K., Gajewska B.U., Okada H., Gronski M.A., Bertram E.M., Dawicki W., Duncan G.S., Bukczynski J., Plyte S., Elia A., Wakeham A., Itie A., Chung S., Da Costa J., Arya S., Horan T., Campbell P., Gaida K. expand/collapse author list , Ohashi P.S., Watts T.H., Yoshinaga S.K., Bray M.R., Jordana M., Mak T.W.
Nat. Immunol. 4:899-906(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
Strain: C57BL/6.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon and Mammary tumor.
[5]"Duplication of primate and rodent B7-H3 immunoglobulin V- and C-like domains: divergent history of functional redundancy and exon loss."
Ling V., Wu P.W., Spaulding V., Kieleczawa J., Luxenberg D., Carreno B.M., Collins M.
Genomics 82:365-377(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOMIC DOMAIN DUPLICATION.
[6]"Mouse B7-H3 induces antitumor immunity."
Sun X., Vale M., Leung E., Kanwar J.R., Gupta R., Krissansen G.W.
Gene Ther. 10:1728-1734(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, GENE TRANSFER.
[7]"Murine B7-H3 is a negative regulator of T cells."
Prasad D.V., Nguyen T., Li Z., Yang Y., Duong J., Wang Y., Dong C.
J. Immunol. 173:2500-2506(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"B7-H3 promotes acute and chronic allograft rejection."
Wang L., Fraser C.C., Kikly K., Wells A.D., Han R., Coyle A.J., Chen L., Hancock W.W.
Eur. J. Immunol. 35:428-438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[9]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104; ASN-189 AND ASN-197.
Tissue: Myoblast.
[10]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104; ASN-189 AND ASN-215.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY190318 mRNA. Translation: AAP04007.1.
AK155114 mRNA. Translation: BAE33058.1.
BC019436 mRNA. Translation: AAH19436.1.
BC056608 mRNA. Translation: AAH56608.1.
RefSeqNP_598744.1. NM_133983.4.
UniGeneMm.5356.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4I0KX-ray2.97A34-247[»]
ProteinModelPortalQ8VE98.
SMRQ8VE98. Positions 35-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-60156N.

PTM databases

PhosphoSiteQ8VE98.

Proteomic databases

PRIDEQ8VE98.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000039788; ENSMUSP00000042681; ENSMUSG00000035914.
ENSMUST00000165365; ENSMUSP00000129418; ENSMUSG00000035914.
GeneID102657.
KEGGmmu:102657.
UCSCuc009pxb.1. mouse.

Organism-specific databases

CTD80381.
MGIMGI:2183926. Cd276.

Phylogenomic databases

eggNOGNOG85729.
GeneTreeENSGT00700000104325.
HOGENOMHOG000293131.
HOVERGENHBG079786.
InParanoidQ8VE98.
KOK06746.
OMAFPPVALW.
OrthoDBEOG7FBRH9.
PhylomeDBQ8VE98.
TreeFamTF331083.

Gene expression databases

ArrayExpressQ8VE98.
BgeeQ8VE98.
CleanExMM_CD276.
GenevestigatorQ8VE98.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio355600.
PROQ8VE98.
SOURCESearch...

Entry information

Entry nameCD276_MOUSE
AccessionPrimary (citable) accession number: Q8VE98
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot