ID CD80_HUMAN Reviewed; 288 AA. AC P33681; Q5DTA9; Q5DTB0; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 02-SEP-2026, entry version 226. DE RecName: Full=T-lymphocyte activation antigen CD80; DE AltName: Full=Activation B7-1 antigen; DE AltName: Full=BB1; DE AltName: Full=CTLA-4 counter-receptor B7.1; DE Short=B7; DE AltName: CD_antigen=CD80; DE Flags: Precursor; GN Name=CD80; Synonyms=CD28LG, CD28LG1, LAB7; 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 1), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Lymphoid tissue; RX PubMed=2794510; DOI=10.4049/jimmunol.143.8.2714; RA Freeman G.J., Freedman A.S., Segil J.M., Lee G., Whitman J.F., Nadler L.M.; RT "B7, a new member of the Ig superfamily with unique expression on activated RT and neoplastic B cells."; RL J. Immunol. 143:2714-2722(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1377173; DOI=10.1007/bf00661094; RA Selvakumar A., Mohanraj B.K., Eddy R.L., Shows T.B., White P.C., Dupont B.; RT "Genomic organization and chromosomal location of the human gene encoding RT the B-lymphocyte activation antigen B7."; RL Immunogenetics 36:175-181(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND ALTERNATIVE SPLICING. RX PubMed=17953528; DOI=10.1111/j.1365-3083.2007.02009.x; RA Kakoulidou M., Giscombe R., Zhao X., Lefvert A.K., Wang X.; RT "Human Soluble CD80 is generated by alternative splicing, and recombinant RT soluble CD80 binds to CD28 and CD152 influencing T-cell activation."; RL Scand. J. Immunol. 66:529-537(2007). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [6] RP PROTEIN SEQUENCE OF 35-38. RX PubMed=1714935; DOI=10.1084/jem.174.3.625; RA Freeman G.J., Gray G.S., Gimmi C.D., Lombard D.B., Zhou L.-J., White M., RA Fingeroth J.D., Gribben J.G., Nadler L.M.; RT "Structure, expression, and T cell costimulatory activity of the murine RT homologue of the human B lymphocyte activation antigen B7."; RL J. Exp. Med. 174:625-631(1991). RN [7] RP CHARACTERIZATION. RX PubMed=7527824; DOI=10.4049/jimmunol.154.1.97; 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 [8] RP FUNCTION. RX PubMed=10583602; DOI=10.1046/j.1365-2567.1999.00888.x; RA Vandenborre K., Van Gool S.W., Kasran A., Ceuppens J.L., Boogaerts M.A., RA Vandenberghe P.; RT "Interaction of CTLA-4 (CD152) with CD80 or CD86 inhibits human T-cell RT activation."; RL Immunology 98:413-421(1999). RN [9] RP FUNCTION. RX PubMed=10438913; DOI=10.4049/jimmunol.163.4.1809; RA Boulougouris G., McLeod J.D., Patel Y.I., Ellwood C.N., Walker L.S., RA Sansom D.M.; RT "IL-2-independent activation and proliferation in human T cells induced by RT CD28."; RL J. Immunol. 163:1809-1816(1999). RN [10] RP FUNCTION. RX PubMed=12121659; DOI=10.1016/s1074-7613(02)00323-0; RA Frauwirth K.A., Riley J.L., Harris M.H., Parry R.V., Rathmell J.C., RA Plas D.R., Elstrom R.L., June C.H., Thompson C.B.; RT "The CD28 signaling pathway regulates glucose metabolism."; RL Immunity 16:769-777(2002). RN [11] RP INTERACTION WITH CD28, AND FUNCTION. RX PubMed=12196291; DOI=10.1016/s1074-7613(02)00362-x; RA Collins A.V., Brodie D.W., Gilbert R.J., Iaboni A., Manso-Sancho R., RA Walse B., Stuart D.I., van der Merwe P.A., Davis S.J.; RT "The interaction properties of costimulatory molecules revisited."; RL Immunity 17:201-210(2002). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH VACCINIA VIRUS RP OPG038/M2 PROTEIN. RX PubMed=30918073; DOI=10.1128/jvi.00207-19; RA Kleinpeter P., Remy-Ziller C., Winter E., Gantzer M., Nourtier V., RA Kempf J., Hortelano J., Schmitt D., Schultz H., Geist M., Brua C., RA Hoffmann C., Schlesinger Y., Villeval D., Thioudellet C., Erbs P., RA Foloppe J., Silvestre N., Fend L., Quemeneur E., Marchand J.B.; RT "By Binding CD80 and CD86, the Vaccinia Virus M2 Protein Blocks Their RT Interactions with both CD28 and CTLA4 and Potentiates CD80 Binding to PD- RT L1."; RL J. Virol. 93:0-0(2019). RN [15] RP FUNCTION, AND INTERACTION WITH PDL1/CD274. RX PubMed=36727298; DOI=10.15252/embj.2022111556; RA Kennedy A., Robinson M.A., Hinze C., Waters E., Williams C., Halliday N., RA Dovedi S., Sansom D.M.; RT "The CTLA-4 immune checkpoint protein regulates PD-L1:PD-1 interaction via RT transendocytosis of its ligand CD80."; RL EMBO J. 42:e111556-e111556(2023). RN [16] RP FUNCTION, PALMITOYLATION AT CYS-261; CYS-262; CYS-266 AND CYS-271, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-261; CYS-262; CYS-266 AND RP CYS-271. RX PubMed=38467718; DOI=10.1038/s41401-024-01248-1; RA Lu B., Sun Y.Y., Chen B.Y., Yang B., He Q.J., Li J., Cao J.; RT "zDHHC20-driven S-palmitoylation of CD80 is required for its costimulatory RT function."; RL Acta Pharmacol. Sin. 0:0-0(2024). RN [17] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-234. RX PubMed=10661405; DOI=10.1016/s1074-7613(00)80158-2; RA Ikemizu S., Gilbert R.J., Fennelly J.A., Collins A.V., Harlos K., RA Jones E.Y., Stuart D.I., Davis S.J.; RT "Structure and dimerization of a soluble form of B7-1."; RL Immunity 12:51-60(2000). RN [18] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-242 IN COMPLEX WITH CTLA4, RP FUNCTION, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-53; ASN-89; RP ASN-186; ASN-207 AND ASN-226. RX PubMed=11279502; DOI=10.1038/35069118; RA Stamper C.C., Zhang Y., Tobin J.F., Erbe D.V., Ikemizu S., Davis S.J., RA Stahl M.L., Seehra J., Somers W.S., Mosyak L.; RT "Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune RT responses."; RL Nature 410:608-611(2001). CC -!- FUNCTION: Costimulatory molecule that belongs to the immunoglobulin CC superfamily that plays an important role in T-lymphocyte activation CC (PubMed:38467718). Acts as the primary auxiliary signal augmenting the CC MHC/TCR signal in naive T-cells by acting as a ligand for the CD28 CC receptor which is constitutively expressed on the cell surface of T- CC cells (PubMed:12196291). In turn, activates different signaling CC pathways such as NF-kappa-B or MAPK leading to the production of CC different cytokines (PubMed:10438913). Also acts as an inhibitor of T- CC cell activation by acting as a ligand for CTLA4, a decoy receptor, CC thereby blocking CD28-mediated T-cell priming (PubMed:10583602, CC PubMed:11279502). In addition, CD28/CD80 costimulatory signal CC stimulates glucose metabolism and ATP synthesis of T-cells by CC activating the PI3K/Akt signaling pathway (PubMed:12121659). Also acts CC as a regulator of PDL1/PDCD1 interactions to limit excess engagement of CC PDL1 and its inhibitory role in immune responses (PubMed:36727298). CC Expressed on B-cells, plays a critical role in regulating interactions CC between B-cells and T-cells in both early and late germinal center CC responses, which are crucial for the generation of effective humoral CC immune responses (By similarity). {ECO:0000250|UniProtKB:Q00609, CC ECO:0000269|PubMed:10438913, ECO:0000269|PubMed:10583602, CC ECO:0000269|PubMed:11279502, ECO:0000269|PubMed:12121659, CC ECO:0000269|PubMed:12196291, ECO:0000269|PubMed:36727298, CC ECO:0000269|PubMed:38467718}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for adenovirus CC subgroup B. {ECO:0000269|PubMed:16920215}. CC -!- SUBUNIT: Homodimer (PubMed:11279502). Interacts with PDL1/CD274; this CC interaction blocks PDL1/PDCD1 binding and thus PDL1/CD274 inhibitory CC function (PubMed:36727298). Interacts with CD28 (PubMed:12196291). CC {ECO:0000269|PubMed:11279502, ECO:0000269|PubMed:12196291, CC ECO:0000269|PubMed:36727298}. CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus subgroup B CC fiber proteins. {ECO:0000269|PubMed:16920215}. CC -!- SUBUNIT: (Microbial infection) Interacts with Orthopoxvirus OPG038/M2 CC protein, inhibiting the interaction with CTLA4/CD152. CC {ECO:0000269|PubMed:30918073}. CC -!- INTERACTION: CC P33681; Q9NZQ7: CD274; NbExp=15; IntAct=EBI-1031024, EBI-4314282; CC P33681; P10747: CD28; NbExp=3; IntAct=EBI-1031024, EBI-4314301; CC P33681; P16410: CTLA4; NbExp=10; IntAct=EBI-1031024, EBI-1030991; CC P33681; P08138: NGFR; NbExp=7; IntAct=EBI-1031024, EBI-1387782; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2794510, CC ECO:0000269|PubMed:38467718}; Single-pass type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P33681-1; Sequence=Displayed; CC Name=2; Synonyms=s1CD80; CC IsoId=P33681-2; Sequence=VSP_047700; CC Name=3; Synonyms=s2CD80; CC IsoId=P33681-3; Sequence=VSP_047698, VSP_047699; CC -!- TISSUE SPECIFICITY: Expressed on the surfaces of antigen-presenting CC cells. {ECO:0000269|PubMed:2794510}. CC -!- PTM: Palmitoylated by ZDHHC20; palmitoylation protects CD80 from CC ubiquitin-mediated degradation, regulating the protein stability, and CC ensures its accurate plasma membrane localization. CC {ECO:0000269|PubMed:38467718}. CC -!- MISCELLANEOUS: [Isoform 2]: Soluble isoform. Expressed in unstimulated CC B-cells and monocytes, but not T-cells. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Soluble isoform. Expressed in T-cells CC activated by ConA, non-activated monocytes and monocytes activated with CC IFN-c. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M27533; AAA36045.1; -; mRNA. DR EMBL; M83077; AAA58390.1; -; Genomic_DNA. DR EMBL; M83072; AAA58390.1; JOINED; Genomic_DNA. DR EMBL; M83073; AAA58390.1; JOINED; Genomic_DNA. DR EMBL; M83074; AAA58390.1; JOINED; Genomic_DNA. DR EMBL; AY197777; AAO39208.1; -; mRNA. DR EMBL; AY197778; AAO39209.1; -; mRNA. DR EMBL; AC073352; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC042665; AAH42665.1; -; mRNA. DR CCDS; CCDS2989.1; -. [P33681-1] DR PIR; I54495; A45803. DR RefSeq; NP_005182.1; NM_005191.4. [P33681-1] DR PDB; 1DR9; X-ray; 3.00 A; A=35-235. DR PDB; 1I8L; X-ray; 3.00 A; A/B=35-242. DR PDB; 7TPS; X-ray; 3.15 A; A/C=35-140. DR PDB; 8FXW; EM; 2.70 A; C/E/G/H/J/L=35-235. DR PDB; 8FXZ; EM; 2.86 A; C/E/G/H/J/L/N=35-235. DR PDB; 8HXA; EM; 3.04 A; G/H/I/J/K/L=35-234. DR AlphaFoldDB; P33681; -. DR EMDB; EMD-29546; -. DR EMDB; EMD-29549; -. DR EMDB; EMD-35074; -. DR MDposit; P33681; -. DR SMR; P33681; -. DR BioGRID; 107379; 259. DR DIP; DIP-6044N; -. DR FunCoup; P33681; 404. DR IntAct; P33681; 163. DR NDEx; IQUERY-CP-CD80; 19 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000264246; -. DR ChEMBL; CHEMBL2364157; -. DR DrugBank; DB01281; Abatacept. DR DrugBank; DB06681; Belatacept. DR DrugBank; DB04901; Galiximab. DR DrugCentral; P33681; -. DR GuidetoPHARMACOLOGY; 2744; -. DR GlyCosmos; P33681; 8 sites, No reported glycans. DR GlyGen; P33681; 9 sites, 2 N-linked glycans (1 site). DR iPTMnet; P33681; -. DR PhosphoSitePlus; P33681; -. DR BioMuta; CD80; -. DR DMDM; 461606; -. DR MassIVE; P33681; -. DR PaxDb; 9606-ENSP00000264246; -. DR PeptideAtlas; P33681; -. DR ProteomicsDB; 54922; -. [P33681-1] DR ProteomicsDB; 62752; -. DR ProteomicsDB; 62753; -. DR ABCD; P33681; 21 sequenced antibodies. DR Antibodypedia; 16574; 2409 antibodies from 56 providers. DR DNASU; 941; -. DR Ensembl; ENST00000264246.8; ENSP00000264246.3; ENSG00000121594.13. [P33681-1] DR Ensembl; ENST00000383669.3; ENSP00000373165.3; ENSG00000121594.13. [P33681-2] DR Ensembl; ENST00000478182.5; ENSP00000418364.1; ENSG00000121594.13. [P33681-1] DR Ensembl; ENST00000853991.1; ENSP00000524050.1; ENSG00000121594.13. [P33681-1] DR Ensembl; ENST00000853992.1; ENSP00000524051.1; ENSG00000121594.13. [P33681-1] DR GeneID; 941; -. DR KEGG; hsa:941; -. DR MANE-Select; ENST00000264246.8; ENSP00000264246.3; NM_005191.4; NP_005182.1. DR UCSC; uc003ecq.4; human. [P33681-1] DR AGR; HGNC:1700; -. DR CIViC; 941; 1 evidence item across 1 molecular profile. DR ClinPGx; PA26239; -. DR CTD; 941; -. DR DisGeNET; 941; -. DR GeneCards; CD80; -. DR HGNC; HGNC:1700; CD80. DR HPA; ENSG00000121594; Tissue enhanced (lung, lymphoid tissue). DR MIM; 112203; gene. DR OpenTargets; ENSG00000121594; -. DR VEuPathDB; HostDB:ENSG00000121594; -. DR eggNOG; ENOG502S5B5; Eukaryota. DR GeneTree; ENSGT00940000162632; -. DR HOGENOM; CLU_071073_2_0_1; -. DR InParanoid; P33681; -. DR OMA; HMTSVML; -. DR OrthoDB; 9904387at2759; -. DR PAN-GO; P33681; 7 GO annotations based on evolutionary models. DR PhylomeDB; P33681; -. DR PathwayCommons; P33681; -. 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; Co-stimulation by CD28. DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling. DR Reactome; R-HSA-389359; CD28 dependent Vav1 pathway. DR Reactome; R-HSA-389513; Co-inhibition by CTLA4. DR Reactome; R-HSA-6783783; Interleukin-10 signaling. DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR SignaLink; P33681; -. DR SIGNOR; P33681; -. DR Agora; ENSG00000121594; -. DR BioGRID-ORCS; 941; 7 hits in 1168 CRISPR screens. DR ChiTaRS; CD80; human. DR EvolutionaryTrace; P33681; -. DR GeneWiki; CD80; -. DR GenomeRNAi; 941; -. DR Pharos; P33681; Tclin. DR PRO; PR:P33681; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P33681; protein. DR Bgee; ENSG00000121594; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 101 other cell types or tissues. DR ExpressionAtlas; P33681; baseline and differential. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProt. DR GO; GO:0098636; C:protein complex involved in cell adhesion; IDA:MGI. DR GO; GO:0015026; F:coreceptor activity; NAS:UniProtKB. DR GO; GO:0048018; F:receptor ligand activity; IDA: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:0035556; P:intracellular signal transduction; NAS:UniProtKB. DR GO; GO:0002710; P:negative regulation of T cell mediated immunity; IDA:UniProt. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; NAS:UniProtKB. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; NAS:UniProtKB. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0009967; P:positive regulation of signal transduction; NAS:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central. DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; NAS:UniProtKB. DR GO; GO:0042110; P:T cell activation; IDA:UniProt. DR GO; GO:0031295; P:T cell costimulation; IBA:GO_Central. DR CDD; cd16083; IgC1_CD80; 1. DR CDD; cd16086; IgV_CD80; 1. DR FunFam; 2.60.40.10:FF:000910; T-lymphocyte activation antigen CD80; 1. DR FunFam; 2.60.40.10:FF:001077; T-lymphocyte activation antigen CD80; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR037676; CD80_IgC. DR InterPro; IPR042711; CD80_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 InterPro; IPR051713; T-cell_Activation_Regulation. DR PANTHER; PTHR25466; T-LYMPHOCYTE ACTIVATION ANTIGEN; 1. DR PANTHER; PTHR25466:SF4; T-LYMPHOCYTE ACTIVATION ANTIGEN CD80; 1. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR PDBsum; 1DR9; -. DR PDBsum; 1I8L; -. DR PDBsum; 7TPS; -. DR PDBsum; 8FXW; -. DR PDBsum; 8FXZ; -. DR PDBsum; 8HXA; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; KW Immunoglobulin domain; Lipoprotein; Membrane; Palmitate; Phosphoprotein; KW Proteomics identification; Receptor; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..34 FT /evidence="ECO:0000269|PubMed:1714935" FT CHAIN 35..288 FT /note="T-lymphocyte activation antigen CD80" FT /id="PRO_0000014547" FT TOPO_DOM 35..242 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 243..263 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 264..288 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 35..135 FT /note="Ig-like V-type" FT DOMAIN 145..230 FT /note="Ig-like C2-type" FT MOD_RES 284 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT LIPID 261 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:38467718" FT LIPID 262 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:38467718" FT LIPID 266 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:38467718" FT LIPID 271 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:38467718" FT CARBOHYD 53 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11279502" FT CARBOHYD 89 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11279502" FT CARBOHYD 98 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 186 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11279502" FT CARBOHYD 207 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11279502" FT CARBOHYD 211 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 226 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11279502" FT CARBOHYD 232 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 50..116 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:11279502" FT DISULFID 162..216 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:11279502" FT VAR_SEQ 140 FT /note="A -> G (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17953528" FT /id="VSP_047698" FT VAR_SEQ 141..266 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17953528" FT /id="VSP_047699" FT VAR_SEQ 234..266 FT /note="TKQEHFPDNLLPSWAITLISVNGIFVICCLTYC -> S (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:17953528" FT /id="VSP_047700" FT MUTAGEN 261 FT /note="C->S: Loss of costimulatory function upon T-cell FT activation; when associated with S-262, S-266 and S-271." FT /evidence="ECO:0000269|PubMed:38467718" FT MUTAGEN 262 FT /note="C->S: Loss of costimulatory function upon T-cell FT activation; when associated with S-261, S-266 and S-271." FT /evidence="ECO:0000269|PubMed:38467718" FT MUTAGEN 266 FT /note="C->S: Loss of costimulatory function upon T-cell FT activation; when associated with S-261, S-262 and S-271." FT /evidence="ECO:0000269|PubMed:38467718" FT MUTAGEN 271 FT /note="C->S: Loss of costimulatory function upon T-cell FT activation; when associated with S-261, S-262 and S-266." FT /evidence="ECO:0000269|PubMed:38467718" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:8FXW" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:8FXW" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:8FXW" FT STRAND 62..68 FT /evidence="ECO:0007829|PDB:8FXW" FT STRAND 71..77 FT /evidence="ECO:0007829|PDB:8FXW" FT STRAND 80..83 FT /evidence="ECO:0007829|PDB:8FXW" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:8FXW" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:8FXW" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:8FXW" FT TURN 96..99 FT /evidence="ECO:0007829|PDB:8FXW" FT STRAND 100..105 FT /evidence="ECO:0007829|PDB:8FXW" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:8FXW" FT STRAND 112..122 FT /evidence="ECO:0007829|PDB:8FXW" FT STRAND 125..139 FT /evidence="ECO:0007829|PDB:8FXW" FT HELIX 141..145 FT /evidence="ECO:0007829|PDB:1DR9" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:1DR9" FT STRAND 157..169 FT /evidence="ECO:0007829|PDB:1DR9" FT STRAND 171..179 FT /evidence="ECO:0007829|PDB:1DR9" FT STRAND 185..191 FT /evidence="ECO:0007829|PDB:1DR9" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:1DR9" FT STRAND 198..207 FT /evidence="ECO:0007829|PDB:1DR9" FT STRAND 212..220 FT /evidence="ECO:0007829|PDB:1DR9" FT STRAND 225..231 FT /evidence="ECO:0007829|PDB:1DR9" SQ SEQUENCE 288 AA; 33048 MW; BA453EE34528B1F4 CRC64; MGHTRRQGTS PSKCPYLNFF QLLVLAGLSH FCSGVIHVTK EVKEVATLSC GHNVSVEELA QTRIYWQKEK KMVLTMMSGD MNIWPEYKNR TIFDITNNLS IVILALRPSD EGTYECVVLK YEKDAFKREH LAEVTLSVKA DFPTPSISDF EIPTSNIRRI ICSTSGGFPE PHLSWLENGE ELNAINTTVS QDPETELYAV SSKLDFNMTT NHSFMCLIKY GHLRVNQTFN WNTTKQEHFP DNLLPSWAIT LISVNGIFVI CCLTYCFAPR CRERRRNERL RRESVRPV //