ID PD1L2_MOUSE Reviewed; 247 AA. AC Q9WUL5; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=Programmed cell death 1 ligand 2; DE Short=PD-1 ligand 2; DE Short=PD-L2; DE Short=PDCD1 ligand 2; DE Short=Programmed death ligand 2; DE AltName: Full=Butyrophilin B7-DC; DE Short=B7-DC; DE AltName: CD_antigen=CD273; DE Flags: Precursor; GN Name=Pdcd1lg2; Synonyms=B7dc, Btdc, Cd273, Pdl2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PDCD1, AND TISSUE RP SPECIFICITY. RC STRAIN=BALB/cJ; RX PubMed=11283156; DOI=10.1084/jem.193.7.839; RA Tseng S.-Y., Otsuji M., Gorski K., Huang X., Slansky J.E., Pai S.I., RA Shalabi A., Shin T., Pardoll D.M., Tsuchiya H.; RT "B7-DC, a new dendritic cell molecule with potent costimulatory properties RT for T cells."; RL J. Exp. Med. 193:839-846(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=11224527; DOI=10.1038/85330; RA Latchman Y., Wood C.R., Chernova T., Chaudhary D., Borde M., Chernova I., RA Iwai Y., Long A.J., Brown J.A., Nunes R., Greenfield E.A., Bourque K., RA Boussiotis V.A., Carter L.L., Carreno B.M., Malenkovich N., Nishimura H., RA Okazaki T., Honjo T., Sharpe A.H., Freeman G.J.; RT "PD-L2 is a second ligand for PD-1 and inhibits T cell activation."; RL Nat. Immunol. 2:261-268(2001). RN [4] RP FUNCTION, AND MUTAGENESIS OF ASP-33; SER-39; GLU-41; ARG-56; SER-58; RP ASP-65; SER-67; GLU-71; ARG-72; LYS-84; HIS-88; ARG-101; LEU-103; ILE-105; RP ASP-111; LYS-113 AND THR-116. RX PubMed=12719480; DOI=10.1084/jem.20021752; RA Wang S., Bajorath J., Flies D.B., Dong H., Honjo T., Chen L.; RT "Molecular modeling and functional mapping of B7-H1 and B7-DC uncouple RT costimulatory function from PD-1 interaction."; RL J. Exp. Med. 197:1083-1091(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-220 IN COMPLEX WITH PDCD1, AND RP DISULFIDE BOND. RX PubMed=18641123; DOI=10.1073/pnas.0804453105; RA Lazar-Molnar E., Yan Q., Cao E., Ramagopal U., Nathenson S.G., Almo S.C.; RT "Crystal structure of the complex between programmed death-1 (PD-1) and its RT ligand PD-L2."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10483-10488(2008). CC -!- FUNCTION: Involved in the costimulatory signal essential for T-cell CC proliferation and IFNG production in a PDCD1-independent manner. CC Interaction with PDCD1 inhibits T-cell proliferation by blocking cell CC cycle progression and cytokine production. CC {ECO:0000269|PubMed:11224527, ECO:0000269|PubMed:11283156, CC ECO:0000269|PubMed:12719480}. CC -!- SUBUNIT: Interacts with PDCD1. {ECO:0000269|PubMed:11283156, CC ECO:0000269|PubMed:18641123}. CC -!- INTERACTION: CC Q9WUL5; Q02242: Pdcd1; NbExp=2; IntAct=EBI-15716794, EBI-5258903; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BQ51}; CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BQ51, CC ECO:0000305|PubMed:18641123}. CC -!- TISSUE SPECIFICITY: Expressed in immature and mature bone marrow- CC derived dendritic cells and splenic dendritic cells. Highly expressed CC in placenta, liver and weakly expressed in heart, spleen, lymph nodes CC and thymus. Also expressed in some tumor cell lines of lymphoid origin. CC {ECO:0000269|PubMed:11224527, ECO:0000269|PubMed:11283156}. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF142780; AAD33892.1; -; mRNA. DR EMBL; AK089369; BAC40858.1; -; mRNA. DR CCDS; CCDS29736.1; -. DR RefSeq; NP_067371.1; NM_021396.2. DR PDB; 3BOV; X-ray; 1.77 A; A=20-123. DR PDB; 3BP5; X-ray; 1.80 A; B=20-220. DR PDB; 3BP6; X-ray; 1.60 A; B=20-220. DR PDB; 3RNK; X-ray; 1.74 A; B=20-123. DR PDB; 3RNQ; X-ray; 1.60 A; B=20-220. DR PDBsum; 3BOV; -. DR PDBsum; 3BP5; -. DR PDBsum; 3BP6; -. DR PDBsum; 3RNK; -. DR PDBsum; 3RNQ; -. DR AlphaFoldDB; Q9WUL5; -. DR SMR; Q9WUL5; -. DR BioGRID; 208388; 1. DR DIP; DIP-46166N; -. DR IntAct; Q9WUL5; 1. DR STRING; 10090.ENSMUSP00000158422; -. DR BindingDB; Q9WUL5; -. DR ChEMBL; CHEMBL4523499; -. DR GlyCosmos; Q9WUL5; 4 sites, No reported glycans. DR GlyGen; Q9WUL5; 4 sites. DR PhosphoSitePlus; Q9WUL5; -. DR PaxDb; 10090-ENSMUSP00000108195; -. DR ProteomicsDB; 294037; -. DR ABCD; Q9WUL5; 27 sequenced antibodies. DR Antibodypedia; 2736; 1253 antibodies from 43 providers. DR DNASU; 58205; -. DR Ensembl; ENSMUST00000112576.4; ENSMUSP00000108195.3; ENSMUSG00000016498.11. DR Ensembl; ENSMUST00000235164.2; ENSMUSP00000158422.2; ENSMUSG00000016498.11. DR GeneID; 58205; -. DR KEGG; mmu:58205; -. DR UCSC; uc008hdk.2; mouse. DR AGR; MGI:1930125; -. DR CTD; 80380; -. DR MGI; MGI:1930125; Pdcd1lg2. DR VEuPathDB; HostDB:ENSMUSG00000016498; -. DR eggNOG; ENOG502S1Y9; Eukaryota. DR GeneTree; ENSGT00940000161373; -. DR HOGENOM; CLU_013137_8_3_1; -. DR InParanoid; Q9WUL5; -. DR OMA; ELYIVEH; -. DR OrthoDB; 5315576at2759; -. DR PhylomeDB; Q9WUL5; -. DR TreeFam; TF331083; -. DR Reactome; R-MMU-389948; PD-1 signaling. DR BioGRID-ORCS; 58205; 1 hit in 81 CRISPR screens. DR ChiTaRS; Pdcd1lg2; mouse. DR EvolutionaryTrace; Q9WUL5; -. DR PRO; PR:Q9WUL5; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q9WUL5; Protein. DR Bgee; ENSMUSG00000016498; Expressed in gastrula and 25 other cell types or tissues. DR ExpressionAtlas; Q9WUL5; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISO:MGI. DR GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:MGI. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:MGI. DR GO; GO:0032689; P:negative regulation of type II interferon production; ISO:MGI. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI. DR GO; GO:0031295; P:T cell costimulation; IBA:GO_Central. DR CDD; cd20986; IgC1_PD-L2; 1. DR CDD; cd20983; IgV_PD-L2; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR25466:SF1; PROGRAMMED CELL DEATH 1 LIGAND 2; 1. DR PANTHER; PTHR25466; T-LYMPHOCYTE ACTIVATION ANTIGEN; 1. DR Pfam; PF08205; C2-set_2; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR Genevisible; Q9WUL5; MM. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Cell membrane; Disulfide bond; KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000250|UniProtKB:Q9BQ51" FT CHAIN 20..247 FT /note="Programmed cell death 1 ligand 2" FT /id="PRO_0000014556" FT TOPO_DOM 20..221 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 222..242 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 243..247 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 21..118 FT /note="Ig-like V-type" FT DOMAIN 122..203 FT /note="Ig-like C2-type" FT CARBOHYD 64 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 157 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 163 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 189 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 42..102 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 143..192 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:18641123" FT MUTAGEN 33 FT /note="D->S: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 39 FT /note="S->Y: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 41 FT /note="E->S: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 56 FT /note="R->S: Significantly reduces the binding to PDCD1." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 58 FT /note="S->Y: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 65 FT /note="D->S: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 67 FT /note="S->Y: Significantly reduces the binding to PDCD1." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 71 FT /note="E->S: Significantly reduces the binding to PDCD1." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 72 FT /note="R->S: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 84 FT /note="K->S: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 88 FT /note="H->A: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 101 FT /note="R->S: Significantly reduces the binding to PDCD1." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 103 FT /note="L->A: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 105 FT /note="I->A: Abolishes the binding to PDCD1." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 111 FT /note="D->S: Abolishes the binding to PDCD1. Costimulates FT proliferation and IFNG production of T-cells." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 113 FT /note="K->S: Abolishes the binding to PDCD1. Costimulates FT proliferation and IFNG production of T-cells." FT /evidence="ECO:0000269|PubMed:12719480" FT MUTAGEN 116 FT /note="T->Y: No effect on PDCD1 binding." FT /evidence="ECO:0000269|PubMed:12719480" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 38..44 FT /evidence="ECO:0007829|PDB:3BP6" FT TURN 46..48 FT /evidence="ECO:0007829|PDB:3RNQ" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:3RNQ" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:3RNK" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:3RNQ" FT HELIX 77..82 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:3BP6" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 98..106 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 109..121 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 126..132 FT /evidence="ECO:0007829|PDB:3BP6" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 139..149 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 152..155 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 163..168 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 174..182 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 190..196 FT /evidence="ECO:0007829|PDB:3BP6" FT TURN 197..200 FT /evidence="ECO:0007829|PDB:3BP6" FT STRAND 201..207 FT /evidence="ECO:0007829|PDB:3BP6" SQ SEQUENCE 247 AA; 27820 MW; 9BFDDE14F3EC138F CRC64; MLLLLPILNL SLQLHPVAAL FTVTAPKEVY TVDVGSSVSL ECDFDRRECT ELEGIRASLQ KVENDTSLQS ERATLLEEQL PLGKALFHIP SVQVRDSGQY RCLVICGAAW DYKYLTVKVK ASYMRIDTRI LEVPGTGEVQ LTCQARGYPL AEVSWQNVSV PANTSHIRTP EGLYQVTSVL RLKPQPSRNF SCMFWNAHMK ELTSAIIDPL SRMEPKVPRT WPLHVFIPAC TIALIFLAIV IIQRKRI //