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Protein
Submitted name:

Cd86 antigen, isoform CRA_c

Gene

Cd86

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • receptor binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • B cell activation Source: Ensembl
  • cellular response to cytokine stimulus Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to metal ion Source: RGD
  • defense response to virus Source: RGD
  • myeloid dendritic cell differentiation Source: RGD
  • negative regulation of T cell anergy Source: RGD
  • positive regulation of activated T cell proliferation Source: RGD
  • positive regulation of T cell proliferation Source: RGD
  • response to drug Source: RGD
  • response to interferon-gamma Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to yeast Source: RGD
  • T cell proliferation involved in immune response Source: RGD
  • toll-like receptor 3 signaling pathway Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-389356. CD28 co-stimulation.
R-RNO-389357. CD28 dependent PI3K/Akt signaling.
R-RNO-389359. CD28 dependent Vav1 pathway.
R-RNO-389513. CTLA4 inhibitory signaling.
R-RNO-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Names & Taxonomyi

Protein namesi
Submitted name:
Cd86 antigen, isoform CRA_cImported
Submitted name:
Membrane glycoproteinImported
Submitted name:
Protein Cd86Imported
Gene namesi
Name:Cd86Imported
ORF Names:rCG_52586Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi628714. Cd86.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei249 – 26820HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Interactioni

GO - Molecular functioni

  • receptor binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003129.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 12790Ig-like (immunoglobulin-like)InterPro annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysis

Phylogenomic databases

eggNOGiENOG410IYP1. Eukaryota.
ENOG410ZD66. LUCA.
GeneTreeiENSGT00720000108819.
HOGENOMiHOG000276893.
HOVERGENiHBG004093.
KOiK05413.
OMAiIANFSEP.
OrthoDBiEOG70PC0G.
TreeFamiTF331083.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
[Graphical view]
SMARTiSM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35531-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYVVKTCVTC TMYLGILFSV LAYLLSDAVP VKRQAYFNST AYLPCPFTKA
60 70 80 90 100
QNISPSELVV FWQDRKKSVL YEHYLGAEKL DNVNAKYLGR TSFDRDNQAL
110 120 130 140 150
RLHNVQIKDT GLYDCFIQQK TPTGSIILQQ WETELSVIAN FSEPEIEEAQ
160 170 180 190 200
NETRNTGINL TCSSKQGYPK PTKMYFLITN STNEYGDNMQ ISQDNVTKLF
210 220 230 240 250
SVSISLSLPF PDGVYNMTIV CILETESMNI SSKPHNMVFS QPQFDRKTWI
260 270 280 290 300
QIAGPSSLLC CLFLLVVYKA VKKCLKMQNQ PGRPSRKTCE SKQDSGVDES
310
INLEEVEPQL HQQ
Length:313
Mass (Da):35,574
Last modified:January 1, 1998 - v1
Checksum:i3106246B8901B5D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07034349 Genomic DNA. No translation available.
D50558 mRNA. Translation: BAA23470.1.
CH473967 Genomic DNA. Translation: EDM11277.1.
RefSeqiNP_064466.1. NM_020081.1.
UniGeneiRn.229570.

Genome annotation databases

EnsembliENSRNOT00000003129; ENSRNOP00000003129; ENSRNOG00000038835.
GeneIDi56822.
KEGGirno:56822.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07034349 Genomic DNA. No translation available.
D50558 mRNA. Translation: BAA23470.1.
CH473967 Genomic DNA. Translation: EDM11277.1.
RefSeqiNP_064466.1. NM_020081.1.
UniGeneiRn.229570.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000003129; ENSRNOP00000003129; ENSRNOG00000038835.
GeneIDi56822.
KEGGirno:56822.

Organism-specific databases

CTDi942.
RGDi628714. Cd86.

Phylogenomic databases

eggNOGiENOG410IYP1. Eukaryota.
ENOG410ZD66. LUCA.
GeneTreeiENSGT00720000108819.
HOGENOMiHOG000276893.
HOVERGENiHBG004093.
KOiK05413.
OMAiIANFSEP.
OrthoDBiEOG70PC0G.
TreeFamiTF331083.

Enzyme and pathway databases

ReactomeiR-RNO-1257604. PIP3 activates AKT signaling.
R-RNO-389356. CD28 co-stimulation.
R-RNO-389357. CD28 dependent PI3K/Akt signaling.
R-RNO-389359. CD28 dependent Vav1 pathway.
R-RNO-389513. CTLA4 inhibitory signaling.
R-RNO-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
[Graphical view]
SMARTiSM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of rat CD80 and CD86 by molecular cloning and mAb."
    Maeda K., Sato T., Azuma M., Yagita H., Okumura K.
    Int. Immunol. 9:993-1000(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Wistar LewisImported.
    Tissue: LymphomaImported.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiO35531_RAT
AccessioniPrimary (citable) accession number: O35531
Secondary accession number(s): F1LNG0
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.