Cd274
entrez
60533
canonical
uniprot
Q9EP73
canonical
ensembl
ENSMUSG00000016496
resolver
ensp
ENSMUSP00000016640
resolver
enst
ENSMUST00000016640
resolver
genesymbol
Cd274
resolver
genesymbol_syn
B7h1
resolver
genesymbol_syn
Pdcd1l1
resolver
genesymbol_syn
Pdcd1lg1
resolver
genesymbol_syn
Pdl1
resolver
uniprot
Q3U472
resolver
uniprot_entry
PD1L1_MOUSE
resolver
uniprot_entry
Q3U472_MOUSE
resolver
amino_acid_sequence
MRIFAGIIFTACCHLLRAFTITAPKDLYVVEYGSNVTMECRFPVERELDLLALVVYWEKEDEQVIQFVAGEEDLKPQHSNFRGRASLPKDQLLKGNAALQITDVKLQDAGVYCCIISYGGADYKRITLKVNAPYRKINQRISVDPATSEHELICQAEGYPEAEVIWTNSDHQPVSGKRSVTTSRTEGMLLNVTSSLRVNATANDVFYCTFWRSQPGQNHTAELIIPELPATHPPQNRTHWVLLGSILLFLIVVSTVLLFLRKQVRMLDVEKCGVEDTSSKNRNDTQFEET
uniprot
proteins
function
FUNCTION: Plays a critical role in induction and maintenance of immune tolerance to self (PubMed:11238124). As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the activation threshold of T-cells and limits T-cell effector response (PubMed:11238124). Through a yet unknown activating receptor, may costimulate T-cell subsets that predominantly produce interleukin-10 (IL10) (PubMed:11015443, PubMed:12719480). {ECO:0000269|PubMed:11015443, ECO:0000269|PubMed:11238124, ECO:0000269|PubMed:12719480}.; FUNCTION: The PDCD1-mediated inhibitory pathway is exploited by tumors to attenuate anti-tumor immunity and escape destruction by the immune system, thereby facilitating tumor survival (PubMed:12218188, PubMed:27281199). The interaction with PDCD1/PD-1 inhibits cytotoxic T lymphocytes (CTLs) effector function (PubMed:12218188). The blockage of the PDCD1-mediated pathway results in the reversal of the exhausted T-cell phenotype and the normalization of the anti-tumor response, providing a rationale for cancer immunotherapy (PubMed:12218188). {ECO:0000269|PubMed:12218188, ECO:0000269|PubMed:27281199}.
uniprot
proteins
mass_dalton
32780
uniprot
proteins
mutagenesis
MUTAGEN 27; /note="L->A: PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 31; /note="E->S: Significantly reduces the binding to PDCD1."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 34; /note="S->Y: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 37; /note="T->Y: Significantly reduces the binding to PDCD1."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 49; /note="D->S: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 56; /note="Y->S: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 58; /note="E->S: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 62; /note="E->S: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 67; /note="F->A: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 69; /note="A->F: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 72; /note="E->S: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 75; /note="K->S: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 89; /note="K->S: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 98; /note="A->F: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 100; /note="Q->S: No effect on PDCD1 binding."; MUTAGEN 113; /note="C->Y: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 115; /note="I->A: Abolishes the binding to PDCD1."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 117; /note="S->Y: No effect on PDCD1 binding."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 124; /note="K->A: Abolishes the binding to PDCD1."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 126; /note="I->A: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells."; /evidence="ECO:0000269|PubMed:12719480"; MUTAGEN 129; /note="K->S: Abolishes the binding to PDCD1."; /evidence="ECO:0000269|PubMed:12719480
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated; STUB1 likely mediates polyubiquitination of PD-L1/CD274 triggering its degradation. Ubiquitinated by MARCHF8; leading to degradation. Deubiquitinated by USP22; leading to stabilization. {ECO:0000250|UniProtKB:Q9NZQ7}.
uniprot
proteins
protein_family
BTN/MOG family
uniprot
proteins
protein_family
Immunoglobulin superfamily
uniprot
proteins
pubmed
11015443
uniprot
proteins
pubmed
11224527
uniprot
proteins
pubmed
11238124
uniprot
proteins
pubmed
12218188
uniprot
proteins
pubmed
12719480
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
27281199
uniprot
proteins
sequence_length
290
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NZQ7}; Single-pass type I membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9NZQ7}; Single-pass type I membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q9NZQ7}; Single-pass type I membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 240..260; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins