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Programmed cell death 1 ligand 2 (PD-1 ligand 2) (PD-L2) (PDCD1 ligand 2) (Programmed death ligand 2) (Butyrophilin B7-DC) (B7-DC) (CD antigen CD273)

 PD1L2_MOUSE             Reviewed;         247 AA.
Q9WUL5;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
28-FEB-2018, entry version 124.
RecName: Full=Programmed cell death 1 ligand 2;
Short=PD-1 ligand 2;
Short=PD-L2;
Short=PDCD1 ligand 2;
Short=Programmed death ligand 2;
AltName: Full=Butyrophilin B7-DC;
Short=B7-DC;
AltName: CD_antigen=CD273;
Flags: Precursor;
Name=Pdcd1lg2; Synonyms=B7dc, Btdc, Cd273, Pdl2;
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, AND
TISSUE SPECIFICITY.
STRAIN=BALB/cJ;
PubMed=11283156; DOI=10.1084/jem.193.7.839;
Tseng S.-Y., Otsuji M., Gorski K., Huang X., Slansky J.E., Pai S.I.,
Shalabi A., Shin T., Pardoll D.M., Tsuchiya H.;
"B7-DC, a new dendritic cell molecule with potent costimulatory
properties for T cells.";
J. Exp. Med. 193:839-846(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
FUNCTION, AND 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).
[4]
FUNCTION, AND MUTAGENESIS OF ASP-33; SER-39; GLU-41; ARG-56; SER-58;
ASP-65; SER-67; GLU-71; ARG-72; LYS-84; HIS-88; ARG-101; LEU-103;
ILE-105; ASP-111; LYS-113 AND THR-116.
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).
[5]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-220 IN COMPLEX WITH PDCD1,
AND DISULFIDE BOND.
PubMed=18641123; DOI=10.1073/pnas.0804453105;
Lazar-Molnar E., Yan Q., Cao E., Ramagopal U., Nathenson S.G.,
Almo S.C.;
"Crystal structure of the complex between programmed death-1 (PD-1)
and its ligand PD-L2.";
Proc. Natl. Acad. Sci. U.S.A. 105:10483-10488(2008).
-!- FUNCTION: Involved in the costimulatory signal essential for T-
cell proliferation and IFNG production in a PDCD1-independent
manner. Interaction with PDCD1 inhibits T-cell proliferation by
blocking cell cycle progression and cytokine production.
{ECO:0000269|PubMed:11224527, ECO:0000269|PubMed:11283156,
ECO:0000269|PubMed:12719480}.
-!- SUBUNIT: Interacts with PDCD1. {ECO:0000269|PubMed:11283156,
ECO:0000269|PubMed:18641123}.
-!- INTERACTION:
Q02242:Pdcd1; NbExp=2; IntAct=EBI-15716794, EBI-5258903;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q9BQ51}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q9BQ51,
ECO:0000305|PubMed:18641123}.
-!- TISSUE SPECIFICITY: Expressed in immature and mature bone marrow-
derived dendritic cells and splenic dendritic cells. Highly
expressed in placenta, liver and weakly expressed in heart,
spleen, lymph nodes and thymus. Also expressed in some tumor cell
lines of lymphoid origin. {ECO:0000269|PubMed:11224527,
ECO:0000269|PubMed:11283156}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF142780; AAD33892.1; -; mRNA.
EMBL; AK089369; BAC40858.1; -; mRNA.
CCDS; CCDS29736.1; -.
RefSeq; NP_067371.1; NM_021396.2.
UniGene; Mm.116737; -.
PDB; 3BOV; X-ray; 1.77 A; A=20-123.
PDB; 3BP5; X-ray; 1.80 A; B=20-220.
PDB; 3BP6; X-ray; 1.60 A; B=20-220.
PDB; 3RNK; X-ray; 1.74 A; B=20-123.
PDB; 3RNQ; X-ray; 1.60 A; B=20-220.
PDBsum; 3BOV; -.
PDBsum; 3BP5; -.
PDBsum; 3BP6; -.
PDBsum; 3RNK; -.
PDBsum; 3RNQ; -.
ProteinModelPortal; Q9WUL5; -.
SMR; Q9WUL5; -.
BioGrid; 208388; 1.
DIP; DIP-46166N; -.
IntAct; Q9WUL5; 1.
STRING; 10090.ENSMUSP00000108195; -.
PhosphoSitePlus; Q9WUL5; -.
PaxDb; Q9WUL5; -.
PRIDE; Q9WUL5; -.
Ensembl; ENSMUST00000112576; ENSMUSP00000108195; ENSMUSG00000016498.
GeneID; 58205; -.
KEGG; mmu:58205; -.
UCSC; uc008hdk.2; mouse.
CTD; 80380; -.
MGI; MGI:1930125; Pdcd1lg2.
eggNOG; ENOG410IVCK; Eukaryota.
eggNOG; ENOG4111V14; LUCA.
GeneTree; ENSGT00650000093373; -.
HOGENOM; HOG000059625; -.
HOVERGEN; HBG082112; -.
InParanoid; Q9WUL5; -.
KO; K06708; -.
OMA; VAWDYKY; -.
OrthoDB; EOG091G0F5W; -.
PhylomeDB; Q9WUL5; -.
TreeFam; TF331083; -.
Reactome; R-MMU-389948; PD-1 signaling.
EvolutionaryTrace; Q9WUL5; -.
PRO; PR:Q9WUL5; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000016498; -.
CleanEx; MM_PDCD1LG2; -.
ExpressionAtlas; Q9WUL5; baseline and differential.
Genevisible; Q9WUL5; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISO:MGI.
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:0042102; P:positive regulation of T cell proliferation; IDA: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.
Pfam; PF08205; C2-set_2; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000250|UniProtKB:Q9BQ51}.
CHAIN 20 247 Programmed cell death 1 ligand 2.
/FTId=PRO_0000014556.
TOPO_DOM 20 221 Extracellular. {ECO:0000255}.
TRANSMEM 222 242 Helical. {ECO:0000255}.
TOPO_DOM 243 247 Cytoplasmic. {ECO:0000255}.
DOMAIN 21 118 Ig-like V-type.
DOMAIN 122 203 Ig-like C2-type.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 189 189 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 102 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 143 192 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:18641123}.
MUTAGEN 33 33 D->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 39 39 S->Y: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 41 41 E->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 56 56 R->S: Significantly reduces the binding
to PDCD1. {ECO:0000269|PubMed:12719480}.
MUTAGEN 58 58 S->Y: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 65 65 D->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 67 67 S->Y: Significantly reduces the binding
to PDCD1. {ECO:0000269|PubMed:12719480}.
MUTAGEN 71 71 E->S: Significantly reduces the binding
to PDCD1. {ECO:0000269|PubMed:12719480}.
MUTAGEN 72 72 R->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 84 84 K->S: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 88 88 H->A: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 101 101 R->S: Significantly reduces the binding
to PDCD1. {ECO:0000269|PubMed:12719480}.
MUTAGEN 103 103 L->A: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 105 105 I->A: Abolishes the binding to PDCD1.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 111 111 D->S: Abolishes the binding to PDCD1.
Costimulates proliferation and IFNG
production of T-cells.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 113 113 K->S: Abolishes the binding to PDCD1.
Costimulates proliferation and IFNG
production of T-cells.
{ECO:0000269|PubMed:12719480}.
MUTAGEN 116 116 T->Y: No effect on PDCD1 binding.
{ECO:0000269|PubMed:12719480}.
STRAND 28 33 {ECO:0000244|PDB:3BP6}.
STRAND 38 44 {ECO:0000244|PDB:3BP6}.
TURN 46 48 {ECO:0000244|PDB:3RNQ}.
HELIX 52 54 {ECO:0000244|PDB:3RNQ}.
STRAND 55 61 {ECO:0000244|PDB:3BP6}.
STRAND 63 69 {ECO:0000244|PDB:3RNK}.
STRAND 73 75 {ECO:0000244|PDB:3RNQ}.
HELIX 77 82 {ECO:0000244|PDB:3BP6}.
STRAND 84 89 {ECO:0000244|PDB:3BP6}.
HELIX 94 96 {ECO:0000244|PDB:3BP6}.
STRAND 98 106 {ECO:0000244|PDB:3BP6}.
STRAND 109 121 {ECO:0000244|PDB:3BP6}.
STRAND 126 132 {ECO:0000244|PDB:3BP6}.
TURN 134 136 {ECO:0000244|PDB:3BP6}.
STRAND 139 149 {ECO:0000244|PDB:3BP6}.
STRAND 152 155 {ECO:0000244|PDB:3BP6}.
STRAND 163 168 {ECO:0000244|PDB:3BP6}.
STRAND 174 182 {ECO:0000244|PDB:3BP6}.
STRAND 190 196 {ECO:0000244|PDB:3BP6}.
TURN 197 200 {ECO:0000244|PDB:3BP6}.
STRAND 201 207 {ECO:0000244|PDB:3BP6}.
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


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