CD86_MOUSE
ID CD86_MOUSE Reviewed; 309 AA.
AC P42082;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=T-lymphocyte activation antigen CD86;
DE AltName: Full=Activation B7-2 antigen;
DE AltName: Full=Early T-cell costimulatory molecule 1;
DE Short=ETC-1;
DE AltName: CD_antigen=CD86;
DE Flags: Precursor;
GN Name=Cd86;
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] (ISOFORM 1).
RX PubMed=7504059; DOI=10.1084/jem.178.6.2185;
RA Freeman G.J., Borriello F., Hodes R.J., Reiser H., Gribben J.G., Ng J.W.,
RA Kim J., Goldberg J.M., Hathcock K., Laszlo G., Lombard L.A., Wang S.,
RA Gray G.S., Nadler L.M., Sharpe A.H.;
RT "Murine B7-2, an alternative CTLA4 counter-receptor that costimulates T
RT cell proliferation and interleukin 2 production.";
RL J. Exp. Med. 178:2185-2192(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7513726;
RA Chen C., Gault A., Shen L., Nabavi N.;
RT "Molecular cloning and expression of early T cell costimulatory molecule-1
RT and its characterization as B7-2 molecule.";
RL J. Immunol. 152:4929-4936(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=129;
RX PubMed=7499829;
RA Borriello F., Oliveros J., Freeman G.J., Nadler L.M., Sharpe A.H.;
RT "Differential expression of alternate mB7-2 transcripts.";
RL J. Immunol. 155:5490-5497(1995).
RN [4]
RP FUNCTION, AND INTERACTION WITH PHB1 AND PHB2.
RX PubMed=23241883; DOI=10.4049/jimmunol.1201646;
RA Lucas C.R., Cordero-Nieves H.M., Erbe R.S., McAlees J.W., Bhatia S.,
RA Hodes R.J., Campbell K.S., Sanders V.M.;
RT "Prohibitins and the cytoplasmic domain of CD86 cooperate to mediate CD86
RT signaling in B lymphocytes.";
RL J. Immunol. 190:723-736(2013).
CC -!- FUNCTION: Receptor involved in the costimulatory signal essential for
CC T-lymphocyte proliferation and interleukin-2 production, by binding
CC CD28 or CTLA-4. May play a critical role in the early events of T-cell
CC activation and costimulation of naive T-cells, such as deciding between
CC immunity and anergy that is made by T-cells within 24 hours after
CC activation. Also involved in the regulation of B cells function, plays
CC a role in regulating the level of IgG(1) produced. Upon CD40
CC engagement, activates NF-kappa-B signaling pathway via phospholipase C
CC and protein kinase C activation (PubMed:23241883).
CC {ECO:0000269|PubMed:23241883}.
CC -!- SUBUNIT: Homodimer. Interacts with MARCH8 (By similarity). Interacts
CC (via cytoplasmic domain) with PHB1 and PHB2; the interactions increases
CC after priming with CD40 (PubMed:23241883).
CC {ECO:0000250|UniProtKB:P42081, ECO:0000269|PubMed:23241883}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42082-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42082-2; Sequence=VSP_023125;
CC -!- TISSUE SPECIFICITY: Expressed on activated B-cells.
CC -!- PTM: Polyubiquitinated; which is promoted by MARCH8 and results in
CC endocytosis and lysosomal degradation. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB30744.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L25606; AAA79770.1; -; mRNA.
DR EMBL; S70108; AAB30744.2; ALT_INIT; mRNA.
DR EMBL; U39456; AAC52334.1; -; Genomic_DNA.
DR EMBL; U39459; AAC52334.1; JOINED; Genomic_DNA.
DR EMBL; U39461; AAC52334.1; JOINED; Genomic_DNA.
DR EMBL; U39462; AAC52334.1; JOINED; Genomic_DNA.
DR EMBL; U39463; AAC52334.1; JOINED; Genomic_DNA.
DR EMBL; U39464; AAC52334.1; JOINED; Genomic_DNA.
DR EMBL; U39465; AAC52334.1; JOINED; Genomic_DNA.
DR EMBL; U39466; AAC52334.1; JOINED; Genomic_DNA.
DR EMBL; U39456; AAC52336.1; -; Genomic_DNA.
DR EMBL; U39461; AAC52336.1; JOINED; Genomic_DNA.
DR EMBL; U39462; AAC52336.1; JOINED; Genomic_DNA.
DR EMBL; U39463; AAC52336.1; JOINED; Genomic_DNA.
DR EMBL; U39464; AAC52336.1; JOINED; Genomic_DNA.
DR EMBL; U39465; AAC52336.1; JOINED; Genomic_DNA.
DR EMBL; U39466; AAC52336.1; JOINED; Genomic_DNA.
DR CCDS; CCDS28155.1; -. [P42082-1]
DR PIR; I49522; I49522.
DR RefSeq; NP_062261.3; NM_019388.3. [P42082-1]
DR RefSeq; XP_011244114.1; XM_011245812.1. [P42082-2]
DR AlphaFoldDB; P42082; -.
DR SMR; P42082; -.
DR STRING; 10090.ENSMUSP00000087047; -.
DR GlyGen; P42082; 9 sites.
DR iPTMnet; P42082; -.
DR PhosphoSitePlus; P42082; -.
DR SwissPalm; P42082; -.
DR MaxQB; P42082; -.
DR PaxDb; P42082; -.
DR PeptideAtlas; P42082; -.
DR PRIDE; P42082; -.
DR ProteomicsDB; 265631; -. [P42082-1]
DR ProteomicsDB; 265632; -. [P42082-2]
DR ABCD; P42082; 62 sequenced antibodies.
DR Antibodypedia; 3810; 2104 antibodies from 50 providers.
DR DNASU; 12524; -.
DR Ensembl; ENSMUST00000089620; ENSMUSP00000087047; ENSMUSG00000022901. [P42082-1]
DR GeneID; 12524; -.
DR KEGG; mmu:12524; -.
DR UCSC; uc007zcq.2; mouse. [P42082-1]
DR CTD; 942; -.
DR MGI; MGI:101773; Cd86.
DR VEuPathDB; HostDB:ENSMUSG00000022901; -.
DR eggNOG; ENOG502S1FF; Eukaryota.
DR GeneTree; ENSGT00940000161500; -.
DR HOGENOM; CLU_071073_0_0_1; -.
DR InParanoid; P42082; -.
DR OMA; HEVYYGQ; -.
DR PhylomeDB; P42082; -.
DR TreeFam; TF331083; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-389356; CD28 co-stimulation.
DR Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR BioGRID-ORCS; 12524; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Cd86; mouse.
DR PRO; PR:P42082; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P42082; protein.
DR Bgee; ENSMUSG00000022901; Expressed in spleen and 99 other tissues.
DR ExpressionAtlas; P42082; baseline and differential.
DR Genevisible; P42082; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB.
DR GO; GO:1990051; P:activation of protein kinase C activity; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; IDA:UniProtKB.
DR GO; GO:0023035; P:CD40 signaling pathway; IDA:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0051607; P:defense response to virus; IDA:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0002668; P:negative regulation of T cell anergy; ISO:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IDA:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IGI:MGI.
DR GO; GO:0031295; P:T cell costimulation; IBA:GO_Central.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IMP:UniProtKB.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IDA:MGI.
DR CDD; cd16087; IgV_CD86; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR037677; CD86_IgV.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..309
FT /note="T-lymphocyte activation antigen CD86"
FT /id="PRO_0000014551"
FT TOPO_DOM 24..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..128
FT /note="Ig-like V-type"
FT DOMAIN 150..223
FT /note="Ig-like C2-type"
FT REGION 269..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_023125"
SQ SEQUENCE 309 AA; 34666 MW; 8F58DCD1FB81D5EA CRC64;
MDPRCTMGLA ILIFVTVLLI SDAVSVETQA YFNGTAYLPC PFTKAQNISL SELVVFWQDQ
QKLVLYEHYL GTEKLDSVNA KYLGRTSFDR NNWTLRLHNV QIKDMGSYDC FIQKKPPTGS
IILQQTLTEL SVIANFSEPE IKLAQNVTGN SGINLTCTSK QGHPKPKKMY FLITNSTNEY
GDNMQISQDN VTELFSISNS LSLSFPDGVW HMTVVCVLET ESMKISSKPL NFTQEFPSPQ
TYWKEITASV TVALLLVMLL IIVCHKKPNQ PSRPSNTASK LERDSNADRE TINLKELEPQ
IASAKPNAE
