Pdcd1
entrez
18566
canonical
uniprot
Q02242
canonical
ensembl
ENSMUSG00000026285
resolver
ensp
ENSMUSP00000027507
resolver
enst
ENSMUST00000027507
resolver
genesymbol
Pdcd1
resolver
genesymbol_syn
Pd1
resolver
uniprot
Q544F3
resolver
uniprot_entry
PDCD1_MOUSE
resolver
uniprot_entry
Q544F3_MOUSE
resolver
amino_acid_sequence
MWVRQVPWSFTWAVLQLSWQSGWLLEVPNGPWRSLTFYPAWLTVSEGANATFTCSLSNWSEDLMLNWNRLSPSNQTEKQAAFCNGLSQPVQDARFQIIQLPNRHDFHMNILDTRRNDSGIYLCGAISLHPKAKIEESPGAELVVTERILETSTRYPSPSPKPEGRFQGMVIGIMSALVGIPVLLLLAWALAVFCSTSMSEARGAGSKDDTLKEEPSAAPVPSVAYEELDFQGREKTPELPTACVHTEYATIVFTEGLGASAMGRRGSADGLQGPRPPRHEDGHCSWPL
uniprot
proteins
function
FUNCTION: Inhibitory receptor on antigen activated T-cells that plays a critical role in induction and maintenance of immune tolerance to self (PubMed:10485649, PubMed:11209085, PubMed:11698646, PubMed:21300912). Delivers inhibitory signals upon binding to ligands, such as CD274/PDCD1L1 and CD273/PDCD1LG2 (PubMed:11015443, PubMed:11224527, PubMed:18287011, PubMed:18641123, PubMed:22641383). Following T-cell receptor (TCR) engagement, PDCD1 associates with TCR-CD3 in the immunological synapse and directly inhibits T-cell activation (PubMed:22641383). Suppresses T-cell activation through the recruitment of PTPN11/SHP-2: following ligand-binding, PDCD1 is phosphorylated within the ITSM motif, leading to the recruitment of the protein tyrosine phosphatase PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules, such as ZAP70, PRKCQ/PKCtheta and CD247/CD3zeta (PubMed:11698646, PubMed:22641383). The PDCD1-mediated inhibitory pathway is exploited by tumors to attenuate anti-tumor immunity and facilitate tumor survival (By similarity). {ECO:0000250|UniProtKB:Q15116, ECO:0000269|PubMed:10485649, ECO:0000269|PubMed:11015443, ECO:0000269|PubMed:11209085, ECO:0000269|PubMed:11224527, ECO:0000269|PubMed:11698646, ECO:0000269|PubMed:18287011, ECO:0000269|PubMed:18641123, ECO:0000269|PubMed:21300912, ECO:0000269|PubMed:22641383}.
uniprot
proteins
mass_dalton
31842
uniprot
proteins
mutagenesis
MUTAGEN 225; /note="Y->F: Reduced tyrosine phosphorylation. Decreased ability to mediate recruitment of PTPN11/SHP-2."; /evidence="ECO:0000269|PubMed:11698646, ECO:0000269|PubMed:22641383"; MUTAGEN 248; /note="Y->F: Reduced tyrosine phosphorylation. Abolished ability to mediate recruitment of PTPN11/SHP-2."; /evidence="ECO:0000269|PubMed:11698646, ECO:0000269|PubMed:22641383
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated at Lys-235 by the SCF(FBXO38) complex, leading to its proteasomal degradation. Ubiquitinated via 'Lys-48'-linked polyubiquitin chains. Deubiquitinated and thus stabilized by USP5. {ECO:0000250|UniProtKB:Q15116}.; PTM: Tyrosine phosphorylated at Tyr-225 (within ITIM motif) and Tyr-248 (ITSM motif) upon ligand binding (PubMed:11698646, PubMed:22641383). Phosphorylation at Tyr-248 by FYN promotes the recruitment of the protein tyrosine phosphatase PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules, such as ZAP70, PRKCQ/PKCtheta and CD247/CD3zeta (PubMed:22641383). Phosphorylation at Thr-236 promotes the recruitment of the deubiquitinase USP5 (By similarity). {ECO:0000250|UniProtKB:Q15116, ECO:0000269|PubMed:11698646, ECO:0000269|PubMed:22641383}.
uniprot
proteins
pubmed
10485649
uniprot
proteins
pubmed
11015443
uniprot
proteins
pubmed
11209085
uniprot
proteins
pubmed
11224527
uniprot
proteins
pubmed
11698646
uniprot
proteins
pubmed
1396582
uniprot
proteins
pubmed
15030777
uniprot
proteins
pubmed
18287011
uniprot
proteins
pubmed
18641123
uniprot
proteins
pubmed
21300912
uniprot
proteins
pubmed
22641383
uniprot
proteins
pubmed
30487606
uniprot
proteins
pubmed
9796923
uniprot
proteins
sequence_length
288
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22641383, ECO:0000269|PubMed:30487606}; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 170..190; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins