PD1L1_HUMAN
ID PD1L1_HUMAN Reviewed; 290 AA.
AC Q9NZQ7; B2RBA2; B4DU27; Q14CJ2; Q2V8D5; Q66RK1; Q6WEX4; Q9NUZ5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Programmed cell death 1 ligand 1 {ECO:0000303|PubMed:28813417};
DE Short=PD-L1 {ECO:0000303|PubMed:28813410, ECO:0000303|PubMed:28813417};
DE Short=PDCD1 ligand 1;
DE Short=Programmed death ligand 1;
DE Short=hPD-L1 {ECO:0000303|PubMed:26602187};
DE AltName: Full=B7 homolog 1 {ECO:0000303|PubMed:10581077};
DE Short=B7-H1 {ECO:0000303|PubMed:10581077};
DE AltName: CD_antigen=CD274;
DE Flags: Precursor;
GN Name=CD274 {ECO:0000312|HGNC:HGNC:17635};
GN Synonyms=B7H1, PDCD1L1, PDCD1LG1, PDL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RX PubMed=10581077; DOI=10.1038/70932;
RA Dong H., Zhu G., Tamada K., Chen L.;
RT "B7-H1, a third member of the B7 family, co-stimulates T-cell proliferation
RT and interleukin-10 secretion.";
RL Nat. Med. 5:1365-1369(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH PDCD1,
RP TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Placenta;
RX PubMed=11015443; DOI=10.1084/jem.192.7.1027;
RA Freeman G.J., Long A.J., Iwai Y., Bourque K., Chernova T., Nishimura H.,
RA Fitz L.J., Malenkovich N., Okazaki T., Byrne M.C., Horton H.F., Fouser L.,
RA Carter L., Ling V., Bowman M.R., Carreno B.M., Collins M., Wood C.R.,
RA Honjo T.;
RT "Engagement of the PD-1 immunoinhibitory receptor by a novel B7-family
RT member leads to negative regulation of lymphocyte activation.";
RL J. Exp. Med. 192:1027-1034(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND SUBCELLULAR LOCATION
RP (ISOFORMS 1 AND 2).
RX PubMed=15780196; DOI=10.1111/j.1745-7254.2005.00086.x;
RA He X.-H., Xu L.-H., Liu Y.;
RT "Identification of a novel splice variant of human PD-L1 mRNA encoding an
RT isoform-lacking Igv-like domain.";
RL Acta Pharmacol. Sin. 26:462-468(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Gastric carcinoma;
RA Chi X.-Y., Zha Q.-B., Xu L.-H., Jia Q.-T., Li F.-Y., He X.-H.;
RT "Expression and significance of PD-L1 variant within tissues of human
RT gastric carcinoma.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CMTM6, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=28813417; DOI=10.1038/nature23643;
RA Burr M.L., Sparbier C.E., Chan Y.C., Williamson J.C., Woods K.,
RA Beavis P.A., Lam E.Y.N., Henderson M.A., Bell C.C., Stolzenburg S.,
RA Gilan O., Bloor S., Noori T., Morgens D.W., Bassik M.C., Neeson P.J.,
RA Behren A., Darcy P.K., Dawson S.J., Voskoboinik I., Trapani J.A., Cebon J.,
RA Lehner P.J., Dawson M.A.;
RT "CMTM6 maintains the expression of PD-L1 and regulates anti-tumour
RT immunity.";
RL Nature 549:101-105(2017).
RN [11]
RP INVOLVEMENT IN CANCERS.
RX PubMed=27281199; DOI=10.1038/nature18294;
RA Kataoka K., Shiraishi Y., Takeda Y., Sakata S., Matsumoto M., Nagano S.,
RA Maeda T., Nagata Y., Kitanaka A., Mizuno S., Tanaka H., Chiba K., Ito S.,
RA Watatani Y., Kakiuchi N., Suzuki H., Yoshizato T., Yoshida K., Sanada M.,
RA Itonaga H., Imaizumi Y., Totoki Y., Munakata W., Nakamura H., Hama N.,
RA Shide K., Kubuki Y., Hidaka T., Kameda T., Masuda K., Minato N.,
RA Kashiwase K., Izutsu K., Takaori-Kondo A., Miyazaki Y., Takahashi S.,
RA Shibata T., Kawamoto H., Akatsuka Y., Shimoda K., Takeuchi K., Seya T.,
RA Miyano S., Ogawa S.;
RT "Aberrant PD-L1 expression through 3'-UTR disruption in multiple cancers.";
RL Nature 534:402-406(2016).
RN [12]
RP FUNCTION, INDUCTION BY IFNG, SUBCELLULAR LOCATION, INTERACTION WITH CMTM4
RP AND CMTM6, IDENTIFICATION BY MASS SPECTROMETRY, AND UBIQUITINATION.
RX PubMed=28813410; DOI=10.1038/nature23669;
RA Mezzadra R., Sun C., Jae L.T., Gomez-Eerland R., de Vries E., Wu W.,
RA Logtenberg M.E.W., Slagter M., Rozeman E.A., Hofland I., Broeks A.,
RA Horlings H.M., Wessels L.F.A., Blank C.U., Xiao Y., Heck A.J.R., Borst J.,
RA Brummelkamp T.R., Schumacher T.N.M.;
RT "Identification of CMTM6 and CMTM4 as PD-L1 protein regulators.";
RL Nature 549:106-110(2017).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 18-239 IN COMPLEX WITH MOUSE
RP PDCD1, AND DISULFIDE BONDS.
RX PubMed=18287011; DOI=10.1073/pnas.0712278105;
RA Lin D.Y., Tanaka Y., Iwasaki M., Gittis A.G., Su H.P., Mikami B.,
RA Okazaki T., Honjo T., Minato N., Garboczi D.N.;
RT "The PD-1/PD-L1 complex resembles the antigen-binding Fv domains of
RT antibodies and T cell receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3011-3016(2008).
RN [14] {ECO:0007744|PDB:4ZQK, ECO:0007744|PDB:5C3T}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 18-134 IN COMPLEX WITH PDCD1, AND
RP DISULFIDE BOND.
RX PubMed=26602187; DOI=10.1016/j.str.2015.09.010;
RA Zak K.M., Kitel R., Przetocka S., Golik P., Guzik K., Musielak B.,
RA Domling A., Dubin G., Holak T.A.;
RT "Structure of the complex of human programmed death 1, PD-1, and its ligand
RT PD-L1.";
RL Structure 23:2341-2348(2015).
CC -!- FUNCTION: Plays a critical role in induction and maintenance of immune
CC tolerance to self (PubMed:11015443, PubMed:28813417, PubMed:28813410).
CC As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the
CC activation threshold of T-cells and limits T-cell effector response
CC (PubMed:11015443, PubMed:28813417, PubMed:28813410). Through a yet
CC unknown activating receptor, may costimulate T-cell subsets that
CC predominantly produce interleukin-10 (IL10) (PubMed:10581077).
CC {ECO:0000269|PubMed:10581077, ECO:0000269|PubMed:11015443,
CC ECO:0000269|PubMed:28813410, ECO:0000269|PubMed:28813417}.
CC -!- FUNCTION: The PDCD1-mediated inhibitory pathway is exploited by tumors
CC to attenuate anti-tumor immunity and escape destruction by the immune
CC system, thereby facilitating tumor survival (PubMed:28813417,
CC PubMed:28813410). The interaction with PDCD1/PD-1 inhibits cytotoxic T
CC lymphocytes (CTLs) effector function (By similarity). The blockage of
CC the PDCD1-mediated pathway results in the reversal of the exhausted T-
CC cell phenotype and the normalization of the anti-tumor response,
CC providing a rationale for cancer immunotherapy (By similarity).
CC {ECO:0000250|UniProtKB:Q9EP73, ECO:0000269|PubMed:28813410,
CC ECO:0000269|PubMed:28813417}.
CC -!- SUBUNIT: Interacts with PDCD1 (PubMed:11015443, PubMed:18287011,
CC PubMed:26602187). Interacts (via transmembrane domain) with CMTM4 and
CC CMTM6 (PubMed:28813417, PubMed:28813410). {ECO:0000269|PubMed:11015443,
CC ECO:0000269|PubMed:18287011, ECO:0000269|PubMed:26602187,
CC ECO:0000269|PubMed:28813410, ECO:0000269|PubMed:28813417}.
CC -!- INTERACTION:
CC Q9NZQ7; P33681: CD80; NbExp=11; IntAct=EBI-4314282, EBI-1031024;
CC Q9NZQ7; Q8IZR5: CMTM4; NbExp=3; IntAct=EBI-4314282, EBI-3925367;
CC Q9NZQ7; Q9NX76: CMTM6; NbExp=14; IntAct=EBI-4314282, EBI-1054315;
CC Q9NZQ7; Q15116: PDCD1; NbExp=17; IntAct=EBI-4314282, EBI-4314328;
CC Q9NZQ7-1; Q15116: PDCD1; NbExp=2; IntAct=EBI-15686469, EBI-4314328;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28813410,
CC ECO:0000269|PubMed:28813417}; Single-pass type I membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:28813417};
CC Single-pass type I membrane protein {ECO:0000255}. Recycling endosome
CC membrane {ECO:0000269|PubMed:28813417}; Single-pass type I membrane
CC protein {ECO:0000255}. Note=Associates with CMTM6 at recycling
CC endosomes, where it is protected from being targeted for lysosomal
CC degradation. {ECO:0000269|PubMed:28813417}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:15780196}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endomembrane system
CC {ECO:0000269|PubMed:15780196}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=PD-L1I;
CC IsoId=Q9NZQ7-1; Sequence=Displayed;
CC Name=2; Synonyms=PD-L1II;
CC IsoId=Q9NZQ7-2; Sequence=VSP_013735;
CC Name=3;
CC IsoId=Q9NZQ7-3; Sequence=VSP_013736, VSP_013737;
CC -!- TISSUE SPECIFICITY: Highly expressed in the heart, skeletal muscle,
CC placenta and lung. Weakly expressed in the thymus, spleen, kidney and
CC liver. Expressed on activated T- and B-cells, dendritic cells,
CC keratinocytes and monocytes. {ECO:0000269|PubMed:10581077,
CC ECO:0000269|PubMed:11015443}.
CC -!- INDUCTION: Up-regulated on T- and B-cells, dendritic cells,
CC keratinocytes and monocytes after LPS and IFNG activation. Up-regulated
CC in B-cells activated by surface Ig cross-linking.
CC {ECO:0000269|PubMed:10581077, ECO:0000269|PubMed:11015443,
CC ECO:0000269|PubMed:28813410}.
CC -!- PTM: Ubiquitinated; STUB1 likely mediates polyubiquitination of PD-
CC L1/CD274 triggering its degradation. {ECO:0000269|PubMed:28813410}.
CC -!- DISEASE: Note=Truncation of the 3'-untranslated (3'-UTR) region of
CC CD274 transcripts leads to elevated expression of CD274 in multiple
CC cancers including T-cell leukemia, diffuse large B-cell lymphoma and
CC stomach adenocarcinoma (PubMed:27281199). Disruption of 3'-UTR region
CC is caused by structural variants that stabilize CD274 transcripts,
CC leading to overexpression (PubMed:27281199). Increased expression in
CC tumors promotes immune evasion and tumor cell growth by allowing
CC malignant cells to escape destruction by the immune system
CC (PubMed:27281199). {ECO:0000269|PubMed:27281199}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91966.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF177937; AAF25807.1; -; mRNA.
DR EMBL; AF233516; AAG18508.1; -; mRNA.
DR EMBL; AY254342; AAP13470.1; -; mRNA.
DR EMBL; AY291313; AAP42144.1; -; mRNA.
DR EMBL; AY714881; AAU09634.1; -; mRNA.
DR EMBL; DQ286582; ABB90152.1; -; mRNA.
DR EMBL; AK001894; BAA91966.1; ALT_INIT; mRNA.
DR EMBL; AK300470; BAG62189.1; -; mRNA.
DR EMBL; AK314567; BAG37149.1; -; mRNA.
DR EMBL; AL162253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58763.1; -; Genomic_DNA.
DR EMBL; BC069381; AAH69381.1; -; mRNA.
DR EMBL; BC074984; AAH74984.1; -; mRNA.
DR EMBL; BC113734; AAI13735.1; -; mRNA.
DR EMBL; BC113736; AAI13737.1; -; mRNA.
DR CCDS; CCDS59118.1; -. [Q9NZQ7-2]
DR CCDS; CCDS6464.1; -. [Q9NZQ7-1]
DR RefSeq; NP_001254635.1; NM_001267706.1. [Q9NZQ7-2]
DR RefSeq; NP_054862.1; NM_014143.3. [Q9NZQ7-1]
DR PDB; 3BIK; X-ray; 2.65 A; A=18-239.
DR PDB; 3BIS; X-ray; 2.64 A; A/B=18-239.
DR PDB; 3FN3; X-ray; 2.70 A; A/B=19-238.
DR PDB; 3SBW; X-ray; 2.28 A; C=19-239.
DR PDB; 4Z18; X-ray; 1.95 A; A/B=19-239.
DR PDB; 4ZQK; X-ray; 2.45 A; A=18-132.
DR PDB; 5C3T; X-ray; 1.80 A; A=18-134.
DR PDB; 5GGT; X-ray; 2.80 A; A=18-134.
DR PDB; 5GRJ; X-ray; 3.21 A; A=18-238.
DR PDB; 5IUS; X-ray; 2.89 A; C/D=18-239.
DR PDB; 5J89; X-ray; 2.20 A; A/B/C/D=2-134.
DR PDB; 5J8O; X-ray; 2.30 A; A/B=18-134.
DR PDB; 5JDR; X-ray; 2.70 A; A/B=18-239.
DR PDB; 5JDS; X-ray; 1.70 A; A=18-132.
DR PDB; 5N2D; X-ray; 2.35 A; A/B/C/D=2-134.
DR PDB; 5N2F; X-ray; 1.70 A; A/B=18-134.
DR PDB; 5NIU; X-ray; 2.01 A; A/B/C/D=18-134.
DR PDB; 5O45; X-ray; 0.99 A; A=17-134.
DR PDB; 5O4Y; X-ray; 2.30 A; B/C/E=18-132.
DR PDB; 5X8L; X-ray; 3.10 A; A/B/C/D/E=18-134.
DR PDB; 5X8M; X-ray; 2.66 A; A=18-134.
DR PDB; 5XJ4; X-ray; 2.30 A; A=19-238.
DR PDB; 5XXY; X-ray; 2.90 A; A=18-133.
DR PDB; 6L8R; NMR; -; A=260-290.
DR PDB; 6NM7; X-ray; 2.43 A; A/B=19-134.
DR PDB; 6NM8; X-ray; 2.79 A; A/B=19-134.
DR PDB; 6NNV; X-ray; 1.92 A; A/B/C/D=18-134.
DR PDB; 6NOJ; X-ray; 2.33 A; A/B=18-134.
DR PDB; 6NOS; X-ray; 2.70 A; A/B=18-134.
DR PDB; 6NP9; X-ray; 1.27 A; A=18-134.
DR PDB; 6PV9; X-ray; 2.00 A; A=19-239.
DR PDB; 6R3K; X-ray; 2.20 A; A/B/C/D=18-134.
DR PDB; 6RPG; X-ray; 2.70 A; A/B=18-134.
DR PDB; 6VQN; X-ray; 2.49 A; A/B/C=18-134.
DR PDB; 6YCR; X-ray; 1.54 A; A=18-134.
DR PDB; 7BEA; X-ray; 2.45 A; A/B=18-134.
DR PDB; 7C88; X-ray; 2.00 A; C/M=1-136.
DR PDB; 7CZD; X-ray; 1.64 A; B/D=19-134.
DR PDB; 7DY7; X-ray; 2.42 A; A/B=18-134.
DR PDB; 7NLD; X-ray; 2.30 A; A/B/C/D/E/F=18-134.
DR PDB; 7OUN; X-ray; 1.90 A; A=17-134.
DR PDB; 7TPS; X-ray; 3.15 A; B/D=19-227.
DR PDBsum; 3BIK; -.
DR PDBsum; 3BIS; -.
DR PDBsum; 3FN3; -.
DR PDBsum; 3SBW; -.
DR PDBsum; 4Z18; -.
DR PDBsum; 4ZQK; -.
DR PDBsum; 5C3T; -.
DR PDBsum; 5GGT; -.
DR PDBsum; 5GRJ; -.
DR PDBsum; 5IUS; -.
DR PDBsum; 5J89; -.
DR PDBsum; 5J8O; -.
DR PDBsum; 5JDR; -.
DR PDBsum; 5JDS; -.
DR PDBsum; 5N2D; -.
DR PDBsum; 5N2F; -.
DR PDBsum; 5NIU; -.
DR PDBsum; 5O45; -.
DR PDBsum; 5O4Y; -.
DR PDBsum; 5X8L; -.
DR PDBsum; 5X8M; -.
DR PDBsum; 5XJ4; -.
DR PDBsum; 5XXY; -.
DR PDBsum; 6L8R; -.
DR PDBsum; 6NM7; -.
DR PDBsum; 6NM8; -.
DR PDBsum; 6NNV; -.
DR PDBsum; 6NOJ; -.
DR PDBsum; 6NOS; -.
DR PDBsum; 6NP9; -.
DR PDBsum; 6PV9; -.
DR PDBsum; 6R3K; -.
DR PDBsum; 6RPG; -.
DR PDBsum; 6VQN; -.
DR PDBsum; 6YCR; -.
DR PDBsum; 7BEA; -.
DR PDBsum; 7C88; -.
DR PDBsum; 7CZD; -.
DR PDBsum; 7DY7; -.
DR PDBsum; 7NLD; -.
DR PDBsum; 7OUN; -.
DR PDBsum; 7TPS; -.
DR AlphaFoldDB; Q9NZQ7; -.
DR SMR; Q9NZQ7; -.
DR BioGRID; 118891; 284.
DR DIP; DIP-29731N; -.
DR IntAct; Q9NZQ7; 34.
DR STRING; 9606.ENSP00000370989; -.
DR BindingDB; Q9NZQ7; -.
DR ChEMBL; CHEMBL3580522; -.
DR DrugBank; DB15773; anti-OX40 antibody BMS 986178.
DR DrugBank; DB11595; Atezolizumab.
DR DrugBank; DB15771; AUNP-12.
DR DrugBank; DB11945; Avelumab.
DR DrugBank; DB15772; CA-170.
DR DrugBank; DB15770; Cosibelimab.
DR DrugBank; DB11714; Durvalumab.
DR DrugBank; DB15769; Envafolimab.
DR DrugCentral; Q9NZQ7; -.
DR TCDB; 8.A.23.5.1; the basigin (basigin) family.
DR GlyGen; Q9NZQ7; 5 sites.
DR iPTMnet; Q9NZQ7; -.
DR PhosphoSitePlus; Q9NZQ7; -.
DR SwissPalm; Q9NZQ7; -.
DR BioMuta; CD274; -.
DR DMDM; 83287884; -.
DR EPD; Q9NZQ7; -.
DR jPOST; Q9NZQ7; -.
DR MassIVE; Q9NZQ7; -.
DR MaxQB; Q9NZQ7; -.
DR PaxDb; Q9NZQ7; -.
DR PeptideAtlas; Q9NZQ7; -.
DR PRIDE; Q9NZQ7; -.
DR ProteomicsDB; 83483; -. [Q9NZQ7-1]
DR ProteomicsDB; 83484; -. [Q9NZQ7-2]
DR ProteomicsDB; 83485; -. [Q9NZQ7-3]
DR ABCD; Q9NZQ7; 138 sequenced antibodies.
DR Antibodypedia; 24139; 1926 antibodies from 54 providers.
DR CPTC; Q9NZQ7; 1 antibody.
DR DNASU; 29126; -.
DR Ensembl; ENST00000381573.8; ENSP00000370985.4; ENSG00000120217.14. [Q9NZQ7-2]
DR Ensembl; ENST00000381577.4; ENSP00000370989.3; ENSG00000120217.14. [Q9NZQ7-1]
DR GeneID; 29126; -.
DR KEGG; hsa:29126; -.
DR MANE-Select; ENST00000381577.4; ENSP00000370989.3; NM_014143.4; NP_054862.1.
DR UCSC; uc003zje.4; human. [Q9NZQ7-1]
DR CTD; 29126; -.
DR DisGeNET; 29126; -.
DR GeneCards; CD274; -.
DR HGNC; HGNC:17635; CD274.
DR HPA; ENSG00000120217; Tissue enhanced (lung).
DR MIM; 605402; gene.
DR neXtProt; NX_Q9NZQ7; -.
DR OpenTargets; ENSG00000120217; -.
DR PharmGKB; PA134915280; -.
DR VEuPathDB; HostDB:ENSG00000120217; -.
DR eggNOG; ENOG502S1Y9; Eukaryota.
DR GeneTree; ENSGT00940000161430; -.
DR HOGENOM; CLU_1744717_0_0_1; -.
DR InParanoid; Q9NZQ7; -.
DR OMA; AGVYCCM; -.
DR OrthoDB; 892262at2759; -.
DR PhylomeDB; Q9NZQ7; -.
DR TreeFam; TF331083; -.
DR PathwayCommons; Q9NZQ7; -.
DR Reactome; R-HSA-389948; PD-1 signaling.
DR Reactome; R-HSA-9701898; STAT3 nuclear events downstream of ALK signaling.
DR SignaLink; Q9NZQ7; -.
DR SIGNOR; Q9NZQ7; -.
DR BioGRID-ORCS; 29126; 16 hits in 1073 CRISPR screens.
DR ChiTaRS; CD274; human.
DR EvolutionaryTrace; Q9NZQ7; -.
DR GeneWiki; PD-L1; -.
DR GenomeRNAi; 29126; -.
DR Pharos; Q9NZQ7; Tclin.
DR PRO; PR:Q9NZQ7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NZQ7; protein.
DR Bgee; ENSG00000120217; Expressed in cartilage tissue and 144 other tissues.
DR Genevisible; Q9NZQ7; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IDA:UniProtKB.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:UniProtKB.
DR GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IDA:UniProtKB.
DR GO; GO:2001186; P:negative regulation of CD8-positive, alpha-beta T cell activation; IMP:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:1903556; P:negative regulation of tumor necrosis factor superfamily cytokine production; IMP:UniProtKB.
DR GO; GO:1905404; P:positive regulation of activated CD8-positive, alpha-beta T cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central.
DR GO; GO:0002845; P:positive regulation of tolerance induction to tumor cell; IMP:UniProtKB.
DR GO; GO:0034097; P:response to cytokine; IDA:AgBase.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0031295; P:T cell costimulation; IDA:UniProtKB.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Disulfide bond; Endosome; Glycoprotein; Immunity; Immunoglobulin domain;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..290
FT /note="Programmed cell death 1 ligand 1"
FT /id="PRO_0000014553"
FT TOPO_DOM 19..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..127
FT /note="Ig-like V-type"
FT DOMAIN 133..225
FT /note="Ig-like C2-type"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:18287011, ECO:0000269|PubMed:26602187"
FT DISULFID 155..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:18287011"
FT VAR_SEQ 19..132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15780196, ECO:0000303|Ref.4"
FT /id="VSP_013735"
FT VAR_SEQ 178
FT /note="K -> D (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15780196"
FT /id="VSP_013736"
FT VAR_SEQ 179..290
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15780196"
FT /id="VSP_013737"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:5O45"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:5O45"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5C3T"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:5O45"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5O45"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5O45"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6NP9"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5O45"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:5O45"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5O45"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5O45"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:5O45"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:5O45"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5O45"
FT STRAND 110..131
FT /evidence="ECO:0007829|PDB:5O45"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:4Z18"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:4Z18"
FT STRAND 150..161
FT /evidence="ECO:0007829|PDB:4Z18"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4Z18"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:4Z18"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4Z18"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:4Z18"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:4Z18"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:4Z18"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:4Z18"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:6L8R"
SQ SEQUENCE 290 AA; 33275 MW; FE957086E62A31A8 CRC64;
MRIFAVFIFM TYWHLLNAFT VTVPKDLYVV EYGSNMTIEC KFPVEKQLDL AALIVYWEME
DKNIIQFVHG EEDLKVQHSS YRQRARLLKD QLSLGNAALQ ITDVKLQDAG VYRCMISYGG
ADYKRITVKV NAPYNKINQR ILVVDPVTSE HELTCQAEGY PKAEVIWTSS DHQVLSGKTT
TTNSKREEKL FNVTSTLRIN TTTNEIFYCT FRRLDPEENH TAELVIPELP LAHPPNERTH
LVILGAILLC LGVALTFIFR LRKGRMMDVK KCGIQDTNSK KQSDTHLEET
