CD86_HUMAN
ID CD86_HUMAN Reviewed; 329 AA.
AC P42081; A0N0P0; B7Z2F3; B7Z702; E7ETN5; E9PC27; Q13655; Q6FHB1; Q6GTS4;
AC Q7M4L5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=T-lymphocyte activation antigen CD86;
DE AltName: Full=Activation B7-2 antigen;
DE AltName: Full=B70;
DE AltName: Full=BU63;
DE AltName: Full=CTLA-4 counter-receptor B7.2;
DE AltName: Full=FUN-1;
DE AltName: CD_antigen=CD86;
DE Flags: Precursor;
GN Name=CD86; Synonyms=CD28LG2;
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), AND VARIANT ILE-185.
RX PubMed=7694153; DOI=10.1038/366076a0;
RA Azuma M., Ito D., Yagita K., Okumura K., Phillips J.H., Lanier L.L.,
RA Somoza C.;
RT "B70 antigen is a second ligand for CTLA-4 and CD28.";
RL Nature 366:76-79(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-185.
RX PubMed=7694363; DOI=10.1126/science.7694363;
RA Freeman G.J., Gribben J.G., Boussiotis V.A., Ng J.W., Restivo V.A. Jr.,
RA Lombard L.A., Gray G.S., Nadler L.M.;
RT "Cloning of B7-2: a CTLA-4 counter-receptor that costimulates human T cell
RT proliferation.";
RL Science 262:909-911(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND VARIANT ILE-185.
RX PubMed=11162656; DOI=10.1006/bbrc.2000.4102;
RA Magistrelli G., Caron G., Gauchat J.-F., Jeannin P., Bonnefoy J.-Y.,
RA Delneste Y.;
RT "Identification of an alternatively spliced variant of human CD86 mRNA.";
RL Biochem. Biophys. Res. Commun. 280:1211-1215(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-185.
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-185.
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANTS ILE-185
RP AND THR-310.
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ILE-185
RP AND THR-310.
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-329, AND VARIANT ILE-185.
RC TISSUE=Foreskin;
RX PubMed=7541777; DOI=10.1007/bf00178582;
RA Jellis C.L., Wang S.S., Rennert P., Borriello F., Sharpe A.H., Green N.R.,
RA Gray G.S.;
RT "Genomic organization of the gene coding for the costimulatory human B-
RT lymphocyte antigen B7-2 (CD86).";
RL Immunogenetics 42:85-89(1995).
RN [10]
RP CHARACTERIZATION.
RX PubMed=7527824;
RA Lanier L.L., O'Fallon S., Somoza C., Phillips J.H., Linsley P.S.,
RA Okumura K., Ito D., Azuma M.;
RT "CD80 (B7) and CD86 (B70) provide similar costimulatory signals for T cell
RT proliferation, cytokine production, and generation of CTL.";
RL J. Immunol. 154:97-105(1995).
RN [11]
RP IDENTIFICATION AS CD86.
RX PubMed=7520767;
RA Engel P., Gribben J.G., Freeman G.J., Zhou L.J., Nozawa Y., Abe M.,
RA Nadler L.M., Wakasa H., Tedder T.F.;
RT "The B7-2 (B70) costimulatory molecule expressed by monocytes and activated
RT B lymphocytes is the CD86 differentiation antigen.";
RL Blood 84:1402-1407(1994).
RN [12]
RP UBIQUITINATION, AND INTERACTION WITH MARCH8.
RX PubMed=12582153; DOI=10.1074/jbc.m211285200;
RA Goto E., Ishido S., Sato Y., Ohgimoto S., Ohgimoto K., Nagano-Fujii M.,
RA Hotta H.;
RT "c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus
RT proteins MIR1 and MIR2 and has similar activity.";
RL J. Biol. Chem. 278:14657-14668(2003).
RN [13]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENOVIRUS SUBGROUP B
RP FIBER PROTEINS.
RX PubMed=16920215; DOI=10.1016/j.virusres.2006.07.009;
RA Short J.J., Vasu C., Holterman M.J., Curiel D.T., Pereboev A.;
RT "Members of adenovirus species B utilize CD80 and CD86 as cellular
RT attachment receptors.";
RL Virus Res. 122:144-153(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 26-134 IN COMPLEX WITH CTLA4.
RX PubMed=11279501; DOI=10.1038/35069112;
RA Schwartz J.C., Zhang X., Fedorov A.A., Nathenson S.G., Almo S.C.;
RT "Structural basis for co-stimulation by the human CTLA-4/B7-2 complex.";
RL Nature 410:604-608(2001).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 26-134, SUBUNIT, AND DISULFIDE
RP BOND.
RX PubMed=12606712; DOI=10.1073/pnas.252771499;
RA Zhang X., Schwartz J.C., Almo S.C., Nathenson S.G.;
RT "Crystal structure of the receptor-binding domain of human B7-2: insights
RT into organization and signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2586-2591(2003).
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 (PubMed:7527824). Also involved in the regulation of B cells
CC function, plays a role in regulating the level of IgG(1) produced. Upon
CC CD40 engagement, activates NF-kappa-B signaling pathway via
CC phospholipase C and protein kinase C activation (By similarity).
CC {ECO:0000250|UniProtKB:P42082, ECO:0000269|PubMed:7527824}.
CC -!- FUNCTION: [Isoform 2]: Interferes with the formation of CD86 clusters,
CC and thus acts as a negative regulator of T-cell activation.
CC {ECO:0000269|PubMed:7527824}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for adenovirus
CC subgroup B. {ECO:0000269|PubMed:16920215}.
CC -!- SUBUNIT: Homodimer. Interacts with MARCH8. Interacts (via cytoplasmic
CC domain) with PHB1 and PHB2; the interactions increases after priming
CC with CD40 (By similarity). {ECO:0000250|UniProtKB:P42082,
CC ECO:0000269|PubMed:11279501, ECO:0000269|PubMed:12582153,
CC ECO:0000269|PubMed:12606712, ECO:0000305}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus subgroup b
CC fiber protein. {ECO:0000269|PubMed:16920215}.
CC -!- INTERACTION:
CC P42081; P16410: CTLA4; NbExp=3; IntAct=EBI-1030956, EBI-1030991;
CC P42081-3; P01552: entB; Xeno; NbExp=5; IntAct=EBI-15945259, EBI-1027464;
CC P42081-3; Q99XW1: smeZ; Xeno; NbExp=2; IntAct=EBI-15945259, EBI-16212640;
CC P42081-3; PRO_0000035619 [P06886]: tst; Xeno; NbExp=2; IntAct=EBI-15945259, EBI-16211350;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P42081-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42081-3; Sequence=VSP_023124;
CC Name=3; Synonyms=CD86 deltaEC;
CC IsoId=P42081-2; Sequence=VSP_023124, VSP_009125;
CC Name=4; Synonyms=CD86 deltaTM;
CC IsoId=P42081-4; Sequence=VSP_023124, VSP_040324;
CC Name=5;
CC IsoId=P42081-5; Sequence=VSP_047221;
CC Name=6;
CC IsoId=P42081-6; Sequence=VSP_047220;
CC -!- TISSUE SPECIFICITY: Expressed by activated B-lymphocytes and monocytes.
CC -!- PTM: Polyubiquitinated; which is promoted by MARCH8 and results in
CC endocytosis and lysosomal degradation. {ECO:0000269|PubMed:12582153}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD86 entry;
CC URL="https://en.wikipedia.org/wiki/CD86";
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DR EMBL; U04343; AAB03814.1; -; mRNA.
DR EMBL; L25259; AAA58389.1; -; mRNA.
DR EMBL; CR541844; CAG46642.1; -; mRNA.
DR EMBL; EF064748; ABK41931.1; -; Genomic_DNA.
DR EMBL; AK294663; BAH11839.1; -; mRNA.
DR EMBL; AK301237; BAH13438.1; -; mRNA.
DR EMBL; AK316203; BAH14574.1; -; mRNA.
DR EMBL; AC068630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040261; AAH40261.1; -; mRNA.
DR EMBL; U17722; AAA86473.1; -; Genomic_DNA.
DR EMBL; U17717; AAA86473.1; JOINED; Genomic_DNA.
DR EMBL; U17718; AAA86473.1; JOINED; Genomic_DNA.
DR EMBL; U17719; AAA86473.1; JOINED; Genomic_DNA.
DR EMBL; U17721; AAA86473.1; JOINED; Genomic_DNA.
DR CCDS; CCDS3009.1; -. [P42081-1]
DR CCDS; CCDS43138.1; -. [P42081-3]
DR CCDS; CCDS56272.1; -. [P42081-5]
DR CCDS; CCDS56273.1; -. [P42081-6]
DR CCDS; CCDS74991.1; -. [P42081-4]
DR PIR; A48754; A48754.
DR PIR; JC7605; JC7605.
DR RefSeq; NP_001193853.1; NM_001206924.1. [P42081-5]
DR RefSeq; NP_001193854.1; NM_001206925.1. [P42081-6]
DR RefSeq; NP_008820.3; NM_006889.4. [P42081-3]
DR RefSeq; NP_787058.4; NM_175862.4. [P42081-1]
DR RefSeq; NP_795711.1; NM_176892.1. [P42081-4]
DR PDB; 1I85; X-ray; 3.20 A; A/B=26-134.
DR PDB; 1NCN; X-ray; 2.70 A; A/B=26-134.
DR PDB; 5YXK; X-ray; 1.90 A; A/B/C/D=26-134.
DR PDBsum; 1I85; -.
DR PDBsum; 1NCN; -.
DR PDBsum; 5YXK; -.
DR AlphaFoldDB; P42081; -.
DR SMR; P42081; -.
DR BioGRID; 107380; 7.
DR DIP; DIP-35606N; -.
DR IntAct; P42081; 8.
DR STRING; 9606.ENSP00000332049; -.
DR ChEMBL; CHEMBL2364156; -.
DR DrugBank; DB01281; Abatacept.
DR DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DR DrugBank; DB06681; Belatacept.
DR DrugBank; DB11752; Bryostatin 1.
DR DrugCentral; P42081; -.
DR GuidetoPHARMACOLOGY; 2745; -.
DR GlyGen; P42081; 8 sites.
DR iPTMnet; P42081; -.
DR PhosphoSitePlus; P42081; -.
DR BioMuta; CD86; -.
DR DMDM; 317373339; -.
DR MassIVE; P42081; -.
DR PaxDb; P42081; -.
DR PeptideAtlas; P42081; -.
DR PRIDE; P42081; -.
DR ProteomicsDB; 18249; -.
DR ProteomicsDB; 19349; -.
DR ProteomicsDB; 55481; -. [P42081-1]
DR ProteomicsDB; 55482; -. [P42081-2]
DR ProteomicsDB; 55483; -. [P42081-3]
DR ProteomicsDB; 55484; -. [P42081-4]
DR ABCD; P42081; 17 sequenced antibodies.
DR Antibodypedia; 3810; 2104 antibodies from 50 providers.
DR DNASU; 942; -.
DR Ensembl; ENST00000264468.9; ENSP00000264468.6; ENSG00000114013.16. [P42081-4]
DR Ensembl; ENST00000330540.7; ENSP00000332049.2; ENSG00000114013.16. [P42081-1]
DR Ensembl; ENST00000393627.6; ENSP00000377248.2; ENSG00000114013.16. [P42081-3]
DR Ensembl; ENST00000469710.5; ENSP00000418988.1; ENSG00000114013.16. [P42081-6]
DR Ensembl; ENST00000493101.5; ENSP00000420230.1; ENSG00000114013.16. [P42081-5]
DR GeneID; 942; -.
DR KEGG; hsa:942; -.
DR MANE-Select; ENST00000330540.7; ENSP00000332049.2; NM_175862.5; NP_787058.5.
DR UCSC; uc003eet.4; human. [P42081-1]
DR CTD; 942; -.
DR DisGeNET; 942; -.
DR GeneCards; CD86; -.
DR HGNC; HGNC:1705; CD86.
DR HPA; ENSG00000114013; Tissue enhanced (lymphoid).
DR MIM; 601020; gene.
DR neXtProt; NX_P42081; -.
DR OpenTargets; ENSG00000114013; -.
DR PharmGKB; PA26243; -.
DR VEuPathDB; HostDB:ENSG00000114013; -.
DR eggNOG; ENOG502S1FF; Eukaryota.
DR GeneTree; ENSGT00940000161500; -.
DR HOGENOM; CLU_1271925_0_0_1; -.
DR InParanoid; P42081; -.
DR OMA; HEVYYGQ; -.
DR OrthoDB; 1051626at2759; -.
DR PhylomeDB; P42081; -.
DR TreeFam; TF331083; -.
DR PathwayCommons; P42081; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-389356; CD28 co-stimulation.
DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
DR Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SignaLink; P42081; -.
DR SIGNOR; P42081; -.
DR BioGRID-ORCS; 942; 69 hits in 1066 CRISPR screens.
DR ChiTaRS; CD86; human.
DR EvolutionaryTrace; P42081; -.
DR GeneWiki; CD86; -.
DR GenomeRNAi; 942; -.
DR Pharos; P42081; Tclin.
DR PRO; PR:P42081; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P42081; protein.
DR Bgee; ENSG00000114013; Expressed in monocyte and 145 other tissues.
DR ExpressionAtlas; P42081; baseline and differential.
DR Genevisible; P42081; HS.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0015026; F:coreceptor activity; NAS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISS:UniProtKB.
DR GO; GO:1990051; P:activation of protein kinase C activity; ISS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
DR GO; GO:0023035; P:CD40 signaling pathway; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; NAS:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; NAS:UniProtKB.
DR GO; GO:0032761; P:positive regulation of lymphotoxin A production; NAS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; NAS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0031295; P:T cell costimulation; IBA:GO_Central.
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; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Immunity; Immunoglobulin domain; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..329
FT /note="T-lymphocyte activation antigen CD86"
FT /id="PRO_0000014550"
FT TOPO_DOM 24..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..131
FT /note="Ig-like V-type"
FT DOMAIN 150..225
FT /note="Ig-like C2-type"
FT REGION 277..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..329
FT /note="Polar residues"
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 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 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:12606712"
FT DISULFID 157..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_047220"
FT VAR_SEQ 1..6
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11162656,
FT ECO:0000303|PubMed:7694153, ECO:0000303|Ref.4"
FT /id="VSP_023124"
FT VAR_SEQ 22..234
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11162656"
FT /id="VSP_009125"
FT VAR_SEQ 22..133
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047221"
FT VAR_SEQ 235..282
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11162656"
FT /id="VSP_040324"
FT VARIANT 170
FT /note="S -> N (in dbSNP:rs9282642)"
FT /id="VAR_021916"
FT VARIANT 185
FT /note="V -> I (in dbSNP:rs2681417)"
FT /evidence="ECO:0000269|PubMed:11162656,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7541777, ECO:0000269|PubMed:7694153,
FT ECO:0000269|PubMed:7694363, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5"
FT /id="VAR_055003"
FT VARIANT 310
FT /note="A -> T (in dbSNP:rs1129055)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_014650"
FT VARIANT 323
FT /note="D -> N (in dbSNP:rs9282648)"
FT /id="VAR_021917"
FT CONFLICT 27
FT /note="K -> E (in Ref. 9; AAA86473)"
FT /evidence="ECO:0000305"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:5YXK"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:5YXK"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:5YXK"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:5YXK"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:5YXK"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5YXK"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:5YXK"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5YXK"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5YXK"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:5YXK"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:5YXK"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5YXK"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:5YXK"
FT STRAND 117..133
FT /evidence="ECO:0007829|PDB:5YXK"
SQ SEQUENCE 329 AA; 37682 MW; C249DAEEB889D911 CRC64;
MDPQCTMGLS NILFVMAFLL SGAAPLKIQA YFNETADLPC QFANSQNQSL SELVVFWQDQ
ENLVLNEVYL GKEKFDSVHS KYMGRTSFDS DSWTLRLHNL QIKDKGLYQC IIHHKKPTGM
IRIHQMNSEL SVLANFSQPE IVPISNITEN VYINLTCSSI HGYPEPKKMS VLLRTKNSTI
EYDGVMQKSQ DNVTELYDVS ISLSVSFPDV TSNMTIFCIL ETDKTRLLSS PFSIELEDPQ
PPPDHIPWIT AVLPTVIICV MVFCLILWKW KKKKRPRNSY KCGTNTMERE ESEQTKKREK
IHIPERSDEA QRVFKSSKTS SCDKSDTCF
