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Programmed cell death protein 1 (Protein PD-1) (mPD-1) (CD antigen CD279)

 PDCD1_MOUSE             Reviewed;         288 AA.
Q02242;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
25-OCT-2017, entry version 140.
RecName: Full=Programmed cell death protein 1;
Short=Protein PD-1;
Short=mPD-1;
AltName: CD_antigen=CD279;
Flags: Precursor;
Name=Pdcd1; Synonyms=Pd1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1396582;
Ishida Y., Agata Y., Shibahara K., Honjo T.;
"Induced expression of PD-1, a novel member of the immunoglobulin gene
superfamily, upon programmed cell death.";
EMBO J. 11:3887-3895(1992).
[2]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-150, SUBUNIT, AND
DISULFIDE BOND.
PubMed=15030777; DOI=10.1016/S1074-7613(04)00051-2;
Zhang X., Schwartz J.C., Guo X., Bhatia S., Cao E., Lorenz M.,
Cammer M., Chen L., Zhang Z.-Y., Edidin M.A., Nathenson S.G.,
Almo S.C.;
"Structural and functional analysis of the costimulatory receptor
programmed death-1.";
Immunity 20:337-347(2004).
[3]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-157 IN COMPLEX WITH
CD274, AND DISULFIDE BOND.
PubMed=18287011; DOI=10.1073/pnas.0712278105;
Lin D.Y., Tanaka Y., Iwasaki M., Gittis A.G., Su H.P., Mikami B.,
Okazaki T., Honjo T., Minato N., Garboczi D.N.;
"The PD-1/PD-L1 complex resembles the antigen-binding Fv domains of
antibodies and T cell receptors.";
Proc. Natl. Acad. Sci. U.S.A. 105:3011-3016(2008).
[4]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 34-150 IN COMPLEX WITH
PDCD1LG2, AND DISULFIDE BOND.
PubMed=18641123; DOI=10.1073/pnas.0804453105;
Lazar-Molnar E., Yan Q., Cao E., Ramagopal U., Nathenson S.G.,
Almo S.C.;
"Crystal structure of the complex between programmed death-1 (PD-1)
and its ligand PD-L2.";
Proc. Natl. Acad. Sci. U.S.A. 105:10483-10488(2008).
-!- FUNCTION: Inhibitory cell surface receptor involved in the
regulation of T-cell function during immunity and tolerance. Upon
ligand binding, inhibits T-cell effector functions in an antigen-
specific manner. Possible cell death inducer, in association with
other factors (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15030777,
ECO:0000269|PubMed:18287011, ECO:0000269|PubMed:18641123}.
-!- INTERACTION:
Q9EP73:Cd274; NbExp=2; IntAct=EBI-5258903, EBI-5258879;
Q9WUL5:Pdcd1lg2; NbExp=2; IntAct=EBI-5258903, EBI-15716794;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Thymus.
-!- DEVELOPMENTAL STAGE: Induced at programmed cell death.
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EMBL; X67914; CAA48113.1; -; mRNA.
CCDS; CCDS15200.1; -.
PIR; S28029; S28029.
RefSeq; NP_032824.1; NM_008798.2.
UniGene; Mm.5024; -.
PDB; 1NPU; X-ray; 2.00 A; A=34-150.
PDB; 3BIK; X-ray; 2.65 A; B/C=25-157.
PDB; 3BP5; X-ray; 1.80 A; A=34-150.
PDB; 3BP6; X-ray; 1.60 A; A=34-150.
PDB; 3RNK; X-ray; 1.74 A; A=34-150.
PDB; 3RNQ; X-ray; 1.60 A; A=34-150.
PDB; 3SBW; X-ray; 2.28 A; A/B=34-150.
PDBsum; 1NPU; -.
PDBsum; 3BIK; -.
PDBsum; 3BP5; -.
PDBsum; 3BP6; -.
PDBsum; 3RNK; -.
PDBsum; 3RNQ; -.
PDBsum; 3SBW; -.
ProteinModelPortal; Q02242; -.
SMR; Q02242; -.
DIP; DIP-29730N; -.
IntAct; Q02242; 3.
STRING; 10090.ENSMUSP00000027507; -.
iPTMnet; Q02242; -.
PhosphoSitePlus; Q02242; -.
SwissPalm; Q02242; -.
PaxDb; Q02242; -.
PRIDE; Q02242; -.
Ensembl; ENSMUST00000027507; ENSMUSP00000027507; ENSMUSG00000026285.
GeneID; 18566; -.
KEGG; mmu:18566; -.
UCSC; uc007cev.1; mouse.
CTD; 5133; -.
MGI; MGI:104879; Pdcd1.
eggNOG; ENOG410J26W; Eukaryota.
eggNOG; ENOG41116U6; LUCA.
GeneTree; ENSGT00390000013662; -.
HOGENOM; HOG000253959; -.
HOVERGEN; HBG053534; -.
InParanoid; Q02242; -.
KO; K06744; -.
OMA; DFQWREK; -.
OrthoDB; EOG091G0EE8; -.
PhylomeDB; Q02242; -.
TreeFam; TF336181; -.
Reactome; R-MMU-389948; PD-1 signaling.
EvolutionaryTrace; Q02242; -.
PRO; PR:Q02242; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026285; -.
CleanEx; MM_PDCD1; -.
ExpressionAtlas; Q02242; baseline and differential.
Genevisible; Q02242; MM.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0002644; P:negative regulation of tolerance induction; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0070234; P:positive regulation of T cell apoptotic process; ISO:MGI.
Gene3D; 2.60.40.10; -; 1.
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; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 288 Programmed cell death protein 1.
/FTId=PRO_0000014893.
TOPO_DOM 21 169 Extracellular. {ECO:0000255}.
TRANSMEM 170 190 Helical. {ECO:0000255}.
TOPO_DOM 191 288 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 139 Ig-like V-type.
CARBOHYD 49 49 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 123 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:15030777,
ECO:0000269|PubMed:18287011,
ECO:0000269|PubMed:18641123}.
STRAND 35 38 {ECO:0000244|PDB:3BP6}.
STRAND 40 45 {ECO:0000244|PDB:3BP6}.
STRAND 50 58 {ECO:0000244|PDB:3BP6}.
STRAND 64 70 {ECO:0000244|PDB:3BP6}.
STRAND 76 83 {ECO:0000244|PDB:3BP6}.
STRAND 86 91 {ECO:0000244|PDB:3BP6}.
STRAND 95 99 {ECO:0000244|PDB:3BP6}.
STRAND 103 112 {ECO:0000244|PDB:3BP6}.
HELIX 115 117 {ECO:0000244|PDB:3BP6}.
STRAND 119 127 {ECO:0000244|PDB:3BP6}.
STRAND 129 131 {ECO:0000244|PDB:3BP6}.
STRAND 133 136 {ECO:0000244|PDB:3BP6}.
STRAND 140 145 {ECO:0000244|PDB:3BP6}.
SEQUENCE 288 AA; 31842 MW; 4AD3C5F0F9D4200A CRC64;
MWVRQVPWSF TWAVLQLSWQ SGWLLEVPNG PWRSLTFYPA WLTVSEGANA TFTCSLSNWS
EDLMLNWNRL SPSNQTEKQA AFCNGLSQPV QDARFQIIQL PNRHDFHMNI LDTRRNDSGI
YLCGAISLHP KAKIEESPGA ELVVTERILE TSTRYPSPSP KPEGRFQGMV IGIMSALVGI
PVLLLLAWAL AVFCSTSMSE ARGAGSKDDT LKEEPSAAPV PSVAYEELDF QGREKTPELP
TACVHTEYAT IVFTEGLGAS AMGRRGSADG LQGPRPPRHE DGHCSWPL


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