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T-lymphocyte activation antigen CD80 (Activation B7-1 antigen) (BB1) (CTLA-4 counter-receptor B7.1) (B7) (CD antigen CD80)

 CD80_HUMAN              Reviewed;         288 AA.
P33681; Q5DTA9; Q5DTB0;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
07-NOV-2018, entry version 185.
RecName: Full=T-lymphocyte activation antigen CD80;
AltName: Full=Activation B7-1 antigen;
AltName: Full=BB1;
AltName: Full=CTLA-4 counter-receptor B7.1;
Short=B7;
AltName: CD_antigen=CD80;
Flags: Precursor;
Name=CD80; Synonyms=CD28LG, CD28LG1, LAB7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lymphoid tissue;
PubMed=2794510;
Freeman G.J., Freedman A.S., Segil J.M., Lee G., Whitman J.F.,
Nadler L.M.;
"B7, a new member of the Ig superfamily with unique expression on
activated and neoplastic B cells.";
J. Immunol. 143:2714-2722(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1377173; DOI=10.1007/BF00661094;
Selvakumar A., Mohanraj B.K., Eddy R.L., Shows T.B., White P.C.,
Dupont B.;
"Genomic organization and chromosomal location of the human gene
encoding the B-lymphocyte activation antigen B7.";
Immunogenetics 36:175-181(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND ALTERNATIVE
SPLICING.
PubMed=17953528; DOI=10.1111/j.1365-3083.2007.02009.x;
Kakoulidou M., Giscombe R., Zhao X., Lefvert A.K., Wang X.;
"Human Soluble CD80 is generated by alternative splicing, and
recombinant soluble CD80 binds to CD28 and CD152 influencing T-cell
activation.";
Scand. J. Immunol. 66:529-537(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 35-38.
PubMed=1714935; DOI=10.1084/jem.174.3.625;
Freeman G.J., Gray G.S., Gimmi C.D., Lombard D.B., Zhou L.-J.,
White M., Fingeroth J.D., Gribben J.G., Nadler L.M.;
"Structure, expression, and T cell costimulatory activity of the
murine homologue of the human B lymphocyte activation antigen B7.";
J. Exp. Med. 174:625-631(1991).
[7]
CHARACTERIZATION.
PubMed=7527824;
Lanier L.L., O'Fallon S., Somoza C., Phillips J.H., Linsley P.S.,
Okumura K., Ito D., Azuma M.;
"CD80 (B7) and CD86 (B70) provide similar costimulatory signals for T
cell proliferation, cytokine production, and generation of CTL.";
J. Immunol. 154:97-105(1995).
[8]
FUNCTION, AND INTERACTION WITH CTLA4.
PubMed=10583602; DOI=10.1046/j.1365-2567.1999.00888.x;
Vandenborre K., Van Gool S.W., Kasran A., Ceuppens J.L.,
Boogaerts M.A., Vandenberghe P.;
"Interaction of CTLA-4 (CD152) with CD80 or CD86 inhibits human T-cell
activation.";
Immunology 98:413-421(1999).
[9]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENOVIRUS
SUBGROUP B FIBER PROTEINS.
PubMed=16920215; DOI=10.1016/j.virusres.2006.07.009;
Short J.J., Vasu C., Holterman M.J., Curiel D.T., Pereboev A.;
"Members of adenovirus species B utilize CD80 and CD86 as cellular
attachment receptors.";
Virus Res. 122:144-153(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-234.
PubMed=10661405; DOI=10.1016/S1074-7613(00)80158-2;
Ikemizu S., Gilbert R.J., Fennelly J.A., Collins A.V., Harlos K.,
Jones E.Y., Stuart D.I., Davis S.J.;
"Structure and dimerization of a soluble form of B7-1.";
Immunity 12:51-60(2000).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-242 IN COMPLEX WITH CTLA4,
SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-53; ASN-89;
ASN-186; ASN-207 AND ASN-226.
PubMed=11279502; DOI=10.1038/35069118;
Stamper C.C., Zhang Y., Tobin J.F., Erbe D.V., Ikemizu S., Davis S.J.,
Stahl M.L., Seehra J., Somers W.S., Mosyak L.;
"Crystal structure of the B7-1/CTLA-4 complex that inhibits human
immune responses.";
Nature 410:608-611(2001).
-!- FUNCTION: Involved in the costimulatory signal essential for T-
lymphocyte activation. T-cell proliferation and cytokine
production is induced by the binding of CD28, binding to CTLA-4
has opposite effects and inhibits T-cell activation.
{ECO:0000269|PubMed:10583602}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for adenovirus
subgroup B. {ECO:0000269|PubMed:16920215}.
-!- SUBUNIT: Homodimer; CD80 dimers on the antigen presenting cells
(APCs) bridge CTLA4/CD152 dimers on T-cells in a periodic zipper-
like arrangement. {ECO:0000269|PubMed:10583602,
ECO:0000269|PubMed:11279502}.
-!- SUBUNIT: (Microbial infection) Interacts with adenovirus subgroup
B fiber proteins. {ECO:0000269|PubMed:16920215}.
-!- INTERACTION:
Q9NZQ7:CD274; NbExp=10; IntAct=EBI-1031024, EBI-4314282;
P16410:CTLA4; NbExp=7; IntAct=EBI-1031024, EBI-1030991;
P08138:NGFR; NbExp=3; IntAct=EBI-1031024, EBI-1387782;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P33681-1; Sequence=Displayed;
Name=2; Synonyms=s1CD80;
IsoId=P33681-2; Sequence=VSP_047700;
Note=Soluble isoform. Expressed in unstimulated B-cells and
monocytes, but not T-cells.;
Name=3; Synonyms=s2CD80;
IsoId=P33681-3; Sequence=VSP_047698, VSP_047699;
Note=Soluble isoform. Expressed in T-cells activated by ConA,
non-activated monocytes and monocytes activated with IFN-c.;
-!- TISSUE SPECIFICITY: Expressed on activated B-cells, macrophages
and dendritic cells.
-----------------------------------------------------------------------
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EMBL; M27533; AAA36045.1; -; mRNA.
EMBL; M83077; AAA58390.1; -; Genomic_DNA.
EMBL; M83072; AAA58390.1; JOINED; Genomic_DNA.
EMBL; M83073; AAA58390.1; JOINED; Genomic_DNA.
EMBL; M83074; AAA58390.1; JOINED; Genomic_DNA.
EMBL; AY197777; AAO39208.1; -; mRNA.
EMBL; AY197778; AAO39209.1; -; mRNA.
EMBL; AC073352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC042665; AAH42665.1; -; mRNA.
CCDS; CCDS2989.1; -. [P33681-1]
PIR; I54495; A45803.
RefSeq; NP_005182.1; NM_005191.3. [P33681-1]
UniGene; Hs.838; -.
PDB; 1DR9; X-ray; 3.00 A; A=35-233.
PDB; 1I8L; X-ray; 3.00 A; A/B=35-242.
PDBsum; 1DR9; -.
PDBsum; 1I8L; -.
ProteinModelPortal; P33681; -.
SMR; P33681; -.
BioGrid; 107379; 75.
DIP; DIP-6044N; -.
IntAct; P33681; 6.
STRING; 9606.ENSP00000264246; -.
ChEMBL; CHEMBL2364157; -.
DrugBank; DB01281; Abatacept.
DrugBank; DB06681; Belatacept.
DrugBank; DB04901; Galiximab.
GuidetoPHARMACOLOGY; 2744; -.
iPTMnet; P33681; -.
PhosphoSitePlus; P33681; -.
BioMuta; CD80; -.
DMDM; 461606; -.
PaxDb; P33681; -.
PeptideAtlas; P33681; -.
PRIDE; P33681; -.
ProteomicsDB; 54922; -.
Ensembl; ENST00000264246; ENSP00000264246; ENSG00000121594. [P33681-1]
Ensembl; ENST00000383669; ENSP00000373165; ENSG00000121594. [P33681-2]
Ensembl; ENST00000478182; ENSP00000418364; ENSG00000121594. [P33681-1]
GeneID; 941; -.
KEGG; hsa:941; -.
UCSC; uc003ecq.4; human. [P33681-1]
CTD; 941; -.
DisGeNET; 941; -.
EuPathDB; HostDB:ENSG00000121594.11; -.
GeneCards; CD80; -.
HGNC; HGNC:1700; CD80.
HPA; CAB025368; -.
HPA; HPA050092; -.
MIM; 112203; gene.
neXtProt; NX_P33681; -.
OpenTargets; ENSG00000121594; -.
PharmGKB; PA26239; -.
eggNOG; ENOG410J3XE; Eukaryota.
eggNOG; ENOG411154Z; LUCA.
GeneTree; ENSGT00720000108819; -.
HOGENOM; HOG000036959; -.
HOVERGEN; HBG055207; -.
InParanoid; P33681; -.
KO; K05412; -.
OMA; VRIYWQK; -.
OrthoDB; EOG091G0QRI; -.
PhylomeDB; P33681; -.
TreeFam; TF351094; -.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-389356; CD28 co-stimulation.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SIGNOR; P33681; -.
EvolutionaryTrace; P33681; -.
GeneWiki; CD80; -.
GenomeRNAi; 941; -.
PRO; PR:P33681; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000121594; Expressed in 74 organ(s), highest expression level in gastrocnemius.
CleanEx; HS_CD80; -.
ExpressionAtlas; P33681; baseline and differential.
Genevisible; P33681; HS.
GO; GO:0009986; C:cell surface; HDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098636; C:protein complex involved in cell adhesion; IDA:MGI.
GO; GO:0015026; F:coreceptor activity; NAS:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central.
GO; GO:0045425; P:positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process; NAS:UniProtKB.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; NAS:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0009967; P:positive regulation of signal transduction; NAS:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central.
GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; NAS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
GO; GO:0031295; P:T cell costimulation; IBA:GO_Central.
CDD; cd16083; IgC_CD80; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR037676; CD80_IgC.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction;
Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 34 {ECO:0000269|PubMed:1714935}.
CHAIN 35 288 T-lymphocyte activation antigen CD80.
/FTId=PRO_0000014547.
TOPO_DOM 35 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 263 Helical. {ECO:0000255}.
TOPO_DOM 264 288 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 135 Ig-like V-type.
DOMAIN 145 230 Ig-like C2-type.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11279502}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11279502}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11279502}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11279502}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11279502}.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 116 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:11279502}.
DISULFID 162 216 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:11279502}.
VAR_SEQ 140 140 A -> G (in isoform 3).
{ECO:0000303|PubMed:17953528}.
/FTId=VSP_047698.
VAR_SEQ 141 266 Missing (in isoform 3).
{ECO:0000303|PubMed:17953528}.
/FTId=VSP_047699.
VAR_SEQ 234 266 TKQEHFPDNLLPSWAITLISVNGIFVICCLTYC -> S
(in isoform 2).
{ECO:0000303|PubMed:17953528}.
/FTId=VSP_047700.
STRAND 37 41 {ECO:0000244|PDB:1DR9}.
STRAND 46 48 {ECO:0000244|PDB:1DR9}.
HELIX 58 61 {ECO:0000244|PDB:1DR9}.
STRAND 63 68 {ECO:0000244|PDB:1DR9}.
STRAND 71 77 {ECO:0000244|PDB:1DR9}.
STRAND 80 83 {ECO:0000244|PDB:1DR9}.
HELIX 85 88 {ECO:0000244|PDB:1DR9}.
STRAND 91 95 {ECO:0000244|PDB:1DR9}.
TURN 96 99 {ECO:0000244|PDB:1DR9}.
STRAND 100 103 {ECO:0000244|PDB:1DR9}.
HELIX 108 110 {ECO:0000244|PDB:1DR9}.
STRAND 112 120 {ECO:0000244|PDB:1DR9}.
STRAND 127 139 {ECO:0000244|PDB:1DR9}.
STRAND 146 151 {ECO:0000244|PDB:1DR9}.
STRAND 157 169 {ECO:0000244|PDB:1DR9}.
STRAND 171 179 {ECO:0000244|PDB:1DR9}.
STRAND 185 191 {ECO:0000244|PDB:1DR9}.
TURN 193 195 {ECO:0000244|PDB:1DR9}.
STRAND 198 207 {ECO:0000244|PDB:1DR9}.
STRAND 212 220 {ECO:0000244|PDB:1DR9}.
STRAND 225 231 {ECO:0000244|PDB:1DR9}.
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


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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