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Programmed cell death 1 ligand 1 (PD-L1) (PDCD1 ligand 1) (Programmed death ligand 1) (B7 homolog 1) (B7-H1) (CD antigen CD274)

 PD1L1_MOUSE             Reviewed;         290 AA.
Q9EP73;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
10-OCT-2018, entry version 129.
RecName: Full=Programmed cell death 1 ligand 1;
Short=PD-L1;
Short=PDCD1 ligand 1;
Short=Programmed death ligand 1;
AltName: Full=B7 homolog 1;
Short=B7-H1;
AltName: CD_antigen=CD274;
Flags: Precursor;
Name=Cd274; Synonyms=B7h1, Pdcd1l1, Pdcd1lg1, Pdl1;
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], FUNCTION, INTERACTION WITH PDCD1, TISSUE
SPECIFICITY, AND INDUCTION.
TISSUE=Spleen;
PubMed=11015443; DOI=10.1084/jem.192.7.1027;
Freeman G.J., Long A.J., Iwai Y., Bourque K., Chernova T.,
Nishimura H., Fitz L.J., Malenkovich N., Okazaki T., Byrne M.C.,
Horton H.F., Fouser L., Carter L., Ling V., Bowman M.R., Carreno B.M.,
Collins M., Wood C.R., Honjo T.;
"Engagement of the PD-1 immunoinhibitory receptor by a novel B7-family
member leads to negative regulation of lymphocyte activation.";
J. Exp. Med. 192:1027-1034(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=C57BL/6J;
PubMed=11238124; DOI=10.1182/blood.V97.6.1809;
Tamura H., Dong H., Zhu G., Sica G.L., Flies D.B., Tamada K., Chen L.;
"B7-H1 costimulation preferentially enhances CD28-independent T-helper
cell function.";
Blood 97:1809-1816(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=CD-1; TISSUE=Neural stem cell;
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).
[4]
TISSUE SPECIFICITY.
PubMed=11224527; DOI=10.1038/85330;
Latchman Y., Wood C.R., Chernova T., Chaudhary D., Borde M.,
Chernova I., Iwai Y., Long A.J., Brown J.A., Nunes R.,
Greenfield E.A., Bourque K., Boussiotis V.A., Carter L.L.,
Carreno B.M., Malenkovich N., Nishimura H., Okazaki T., Honjo T.,
Sharpe A.H., Freeman G.J.;
"PD-L2 is a second ligand for PD-1 and inhibits T cell activation.";
Nat. Immunol. 2:261-268(2001).
[5]
FUNCTION, AND MUTAGENESIS OF LEU-27; GLU-31; SER-34; THR-37; ASP-49;
TYR-56; GLU-58; GLU-62; PHE-67; ALA-69; GLU-72; LYS-75; LYS-89;
ALA-98; CYS-113; ILE-115; SER-117; LYS-124; ILE-126 AND LYS-129.
PubMed=12719480; DOI=10.1084/jem.20021752;
Wang S., Bajorath J., Flies D.B., Dong H., Honjo T., Chen L.;
"Molecular modeling and functional mapping of B7-H1 and B7-DC uncouple
costimulatory function from PD-1 interaction.";
J. Exp. Med. 197:1083-1091(2003).
-!- FUNCTION: Plays a critical role in induction and maintenance of
immune tolerance to self. As a ligand for the inhibitory receptor
PDCD1, modulates the activation threshold of T-cells and limits T-
cell effector response (PubMed:11238124). The PDCD1-mediated
inhibitory pathway is exploited by tumors to attenuate anti-tumor
immunity and facilitate tumor survival (By similarity). May
costimulate helper T-cell subsets through a yet unknown activating
receptor (PubMed:11015443, PubMed:12719480).
{ECO:0000250|UniProtKB:Q9NZQ7, ECO:0000269|PubMed:11015443,
ECO:0000269|PubMed:11238124, ECO:0000269|PubMed:12719480}.
-!- SUBUNIT: Interacts with PDCD1 (PubMed:11015443). Interacts with
CMTM4 and CMTM6 (By similarity). {ECO:0000250|UniProtKB:Q9NZQ7,
ECO:0000269|PubMed:11015443}.
-!- INTERACTION:
Q00609:Cd80; NbExp=5; IntAct=EBI-5258879, EBI-5258929;
Q02242:Pdcd1; NbExp=3; IntAct=EBI-5258879, EBI-5258903;
-!- 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}.
-!- TISSUE SPECIFICITY: Highly expressed in the heart, thymus,
skeletal muscle, and lung. Weakly expressed in the kidney, spleen,
thyroid, and liver. Expressed on activated dendritic cells, B-
cells and macrophages. Expressed in numerous tumor cells lines of
lymphoid origin. {ECO:0000269|PubMed:11015443,
ECO:0000269|PubMed:11224527, ECO:0000269|PubMed:11238124}.
-!- INDUCTION: Up-regulated by IFNG treatment in monocytes. Up-
regulated on dendritic cells, B-cells and macrophages after
activation by LPS and IFNG. {ECO:0000269|PubMed:11015443,
ECO:0000269|PubMed:11238124}.
-!- PTM: Ubiquitinated; STUB1 likely mediates polyubiquitination of
PD-L1/CD274 triggering its degradation.
{ECO:0000250|UniProtKB:Q9NZQ7}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF233517; AAG18509.1; -; mRNA.
EMBL; AF317088; AAG31810.1; -; mRNA.
EMBL; BC066841; AAH66841.1; -; mRNA.
CCDS; CCDS29735.1; -.
RefSeq; NP_068693.1; NM_021893.3.
UniGene; Mm.245363; -.
ProteinModelPortal; Q9EP73; -.
SMR; Q9EP73; -.
DIP; DIP-46167N; -.
IntAct; Q9EP73; 2.
STRING; 10090.ENSMUSP00000016640; -.
PhosphoSitePlus; Q9EP73; -.
MaxQB; Q9EP73; -.
PaxDb; Q9EP73; -.
PRIDE; Q9EP73; -.
Ensembl; ENSMUST00000016640; ENSMUSP00000016640; ENSMUSG00000016496.
GeneID; 60533; -.
KEGG; mmu:60533; -.
UCSC; uc008hdi.2; mouse.
CTD; 29126; -.
MGI; MGI:1926446; Cd274.
eggNOG; ENOG410IIBU; Eukaryota.
eggNOG; ENOG4111V14; LUCA.
GeneTree; ENSGT00650000093373; -.
HOGENOM; HOG000059625; -.
HOVERGEN; HBG082112; -.
InParanoid; Q9EP73; -.
KO; K06745; -.
OMA; IWTSSDH; -.
OrthoDB; EOG091G0F5W; -.
PhylomeDB; Q9EP73; -.
TreeFam; TF331083; -.
Reactome; R-MMU-389948; PD-1 signaling.
ChiTaRS; Cd274; mouse.
PRO; PR:Q9EP73; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000016496; Expressed in 101 organ(s), highest expression level in blood.
CleanEx; MM_CD274; -.
ExpressionAtlas; Q9EP73; baseline and differential.
Genevisible; Q9EP73; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
GO; GO:0006955; P:immune response; ISO:MGI.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISO:MGI.
GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; ISO:MGI.
GO; GO:2001186; P:negative regulation of CD8-positive, alpha-beta T cell activation; ISS:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:MGI.
GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:MGI.
GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:MGI.
GO; GO:1903556; P:negative regulation of tumor necrosis factor superfamily cytokine production; ISO:MGI.
GO; GO:1905404; P:positive regulation of activated CD8-positive, alpha-beta T cell apoptotic process; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:2001181; P:positive regulation of interleukin-10 secretion; ISO:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
GO; GO:0002845; P:positive regulation of tolerance induction to tumor cell; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; ISO:MGI.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0031295; P:T cell costimulation; ISO:MGI.
GO; GO:1901998; P:toxin transport; IMP:MGI.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR013162; CD80_C2-set.
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; 2.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Endosome;
Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 290 Programmed cell death 1 ligand 1.
/FTId=PRO_0000014554.
TOPO_DOM 19 239 Extracellular. {ECO:0000255}.
TRANSMEM 240 260 Helical. {ECO:0000255}.
TOPO_DOM 261 290 Cytoplasmic. {ECO:0000255}.
DOMAIN 19 127 Ig-like V-type.
DOMAIN 133 224 Ig-like C2-type.
CARBOHYD 35 35 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 218 218 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 40 114 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 154 208 {ECO:0000255|PROSITE-ProRule:PRU00114}.
MUTAGEN 27 27 L->A: PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 31 31 E->S: Significantly reduces the binding
to PDCD1. {ECO:0000269|PubMed:12719480}.
MUTAGEN 34 34 S->Y: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 37 37 T->Y: Significantly reduces the binding
to PDCD1. {ECO:0000269|PubMed:12719480}.
MUTAGEN 49 49 D->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 56 56 Y->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 58 58 E->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 62 62 E->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 67 67 F->A: Abolishes the binding to PDCD1.
Costimulates proliferation and IFNG
production of T-cells.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 69 69 A->F: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 72 72 E->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 75 75 K->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 89 89 K->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 98 98 A->F: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 100 100 Q->S: No effect on PDCD1 binding.
MUTAGEN 113 113 C->Y: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 115 115 I->A: Abolishes the binding to PDCD1.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 117 117 S->Y: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 124 124 K->A: Abolishes the binding to PDCD1.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 126 126 I->A: Abolishes the binding to PDCD1.
Costimulates proliferation and IFNG
production of T-cells.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 129 129 K->S: Abolishes the binding to PDCD1.
{ECO:0000269|PubMed:12719480}.
SEQUENCE 290 AA; 32780 MW; AB7C46CF853EBB02 CRC64;
MRIFAGIIFT ACCHLLRAFT ITAPKDLYVV EYGSNVTMEC RFPVERELDL LALVVYWEKE
DEQVIQFVAG EEDLKPQHSN FRGRASLPKD QLLKGNAALQ ITDVKLQDAG VYCCIISYGG
ADYKRITLKV NAPYRKINQR ISVDPATSEH ELICQAEGYP EAEVIWTNSD HQPVSGKRSV
TTSRTEGMLL NVTSSLRVNA TANDVFYCTF WRSQPGQNHT AELIIPELPA THPPQNRTHW
VLLGSILLFL IVVSTVLLFL RKQVRMLDVE KCGVEDTSSK NRNDTQFEET


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