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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_HUMAN             Reviewed;         273 AA.
Q9BQ51; Q14CN8; Q5T7Z6; Q6JXL8; Q6JXL9;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 2.
23-MAY-2018, entry version 137.
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, CD273, PDCD1L2, PDL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND VARIANT
SER-229.
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION,
AND VARIANT SER-229.
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION
(ISOFORMS 1; 2 AND 3), AND VARIANT SER-229.
PubMed=15253154; DOI=10.1093/abbs/36.4.284;
He X.-H., Liu Y., Xu L.-H., Zeng Y.-Y.;
"Cloning and identification of two novel splice variants of human PD-
L2.";
Acta Biochim. Biophys. Sin. 36:284-289(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-229.
TISSUE=Brain, and Lung;
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).
[6]
PROTEIN SEQUENCE OF 20-34.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
-!- 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 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with PDCD1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted
{ECO:0000305|PubMed:15253154}.
-!- SUBCELLULAR LOCATION: Isoform 2: Endomembrane system
{ECO:0000269|PubMed:15253154}; Single-pass type I membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:15253154}; Single-pass type I membrane protein
{ECO:0000250|UniProtKB:Q9WUL5, ECO:0000305|PubMed:15340161}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=PD-L2I, Type I;
IsoId=Q9BQ51-1; Sequence=Displayed;
Name=2; Synonyms=PD-L2II, Type II;
IsoId=Q9BQ51-2; Sequence=VSP_013740;
Name=3; Synonyms=PD-L2III, Type III;
IsoId=Q9BQ51-3; Sequence=VSP_013738, VSP_013739;
-!- TISSUE SPECIFICITY: Highly expressed in heart, placenta, pancreas,
lung and liver and weakly expressed in spleen, lymph nodes and
thymus. {ECO:0000269|PubMed:11224527}.
-!- INDUCTION: Up-regulated by IFNG/IFN-gamma stimulation in monocytes
and induced on dendritic cells grown from peripheral blood
mononuclear cells with CSF2 and IL4/interleukin-4.
{ECO:0000269|PubMed:11224527, ECO:0000269|PubMed:11283156}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF329193; AAK31105.1; -; mRNA.
EMBL; AF344424; AAK15370.1; -; mRNA.
EMBL; AY254343; AAP13471.1; -; mRNA.
EMBL; AY271901; AAP49000.1; -; mRNA.
EMBL; AY271902; AAP49001.1; -; mRNA.
EMBL; AL162253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC074766; AAH74766.1; -; mRNA.
EMBL; BC113678; AAI13679.1; -; mRNA.
EMBL; BC113680; AAI13681.1; -; mRNA.
CCDS; CCDS6465.1; -. [Q9BQ51-1]
RefSeq; NP_079515.2; NM_025239.3. [Q9BQ51-1]
UniGene; Hs.532279; -.
UniGene; Hs.617872; -.
ProteinModelPortal; Q9BQ51; -.
SMR; Q9BQ51; -.
BioGrid; 123259; 12.
IntAct; Q9BQ51; 1.
STRING; 9606.ENSP00000380855; -.
iPTMnet; Q9BQ51; -.
PhosphoSitePlus; Q9BQ51; -.
SwissPalm; Q9BQ51; -.
BioMuta; PDCD1LG2; -.
DMDM; 73917618; -.
MaxQB; Q9BQ51; -.
PaxDb; Q9BQ51; -.
PeptideAtlas; Q9BQ51; -.
PRIDE; Q9BQ51; -.
DNASU; 80380; -.
Ensembl; ENST00000397747; ENSP00000380855; ENSG00000197646. [Q9BQ51-1]
GeneID; 80380; -.
KEGG; hsa:80380; -.
UCSC; uc003zjg.5; human. [Q9BQ51-1]
CTD; 80380; -.
DisGeNET; 80380; -.
EuPathDB; HostDB:ENSG00000197646.7; -.
GeneCards; PDCD1LG2; -.
H-InvDB; HIX0007901; -.
HGNC; HGNC:18731; PDCD1LG2.
HPA; HPA013411; -.
MIM; 605723; gene.
neXtProt; NX_Q9BQ51; -.
OpenTargets; ENSG00000197646; -.
PharmGKB; PA134891547; -.
eggNOG; ENOG410IVCK; Eukaryota.
eggNOG; ENOG4111V14; LUCA.
GeneTree; ENSGT00650000093373; -.
HOGENOM; HOG000059625; -.
HOVERGEN; HBG082112; -.
InParanoid; Q9BQ51; -.
KO; K06708; -.
OMA; VAWDYKY; -.
OrthoDB; EOG091G0F5W; -.
PhylomeDB; Q9BQ51; -.
TreeFam; TF331083; -.
Reactome; R-HSA-389948; PD-1 signaling.
ChiTaRS; PDCD1LG2; human.
GeneWiki; PDCD1LG2; -.
GenomeRNAi; 80380; -.
PRO; PR:Q9BQ51; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000197646; -.
CleanEx; HS_PDCD1LG2; -.
Genevisible; Q9BQ51; HS.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:UniProtKB.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
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; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000269|PubMed:15340161}.
CHAIN 20 273 Programmed cell death 1 ligand 2.
/FTId=PRO_0000014555.
TOPO_DOM 20 220 Extracellular. {ECO:0000255}.
TRANSMEM 221 241 Helical. {ECO:0000255}.
TOPO_DOM 242 273 Cytoplasmic. {ECO:0000255}.
DOMAIN 21 118 Ig-like V-type.
DOMAIN 122 203 Ig-like C2-type.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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}.
VAR_SEQ 121 211 ASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVP
ANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVREL
TLASIDLQS -> G (in isoform 2).
{ECO:0000303|PubMed:15253154}.
/FTId=VSP_013740.
VAR_SEQ 121 182 ASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVP
ANTSHSRTPEGLYQVTSVLRL -> DGTQDPSNLAASHFHP
LLHHCFHFHSHSDSPKKTTLSKAVFFKRHNKKTCHHNKEGS
EQCYL (in isoform 3).
{ECO:0000303|PubMed:15253154}.
/FTId=VSP_013738.
VAR_SEQ 183 273 Missing (in isoform 3).
{ECO:0000303|PubMed:15253154}.
/FTId=VSP_013739.
VARIANT 58 58 S -> T (in dbSNP:rs12339171).
/FTId=VAR_049842.
VARIANT 229 229 F -> S (in dbSNP:rs7854303).
{ECO:0000269|PubMed:11224527,
ECO:0000269|PubMed:11283156,
ECO:0000269|PubMed:15253154,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_022449.
VARIANT 241 241 I -> T (in dbSNP:rs7854413).
/FTId=VAR_049843.
SEQUENCE 273 AA; 30957 MW; 8B7E963C9BA26ED9 CRC64;
MIFLLLMLSL ELQLHQIAAL FTVTVPKELY IIEHGSNVTL ECNFDTGSHV NLGAITASLQ
KVENDTSPHR ERATLLEEQL PLGKASFHIP QVQVRDEGQY QCIIIYGVAW DYKYLTLKVK
ASYRKINTHI LKVPETDEVE LTCQATGYPL AEVSWPNVSV PANTSHSRTP EGLYQVTSVL
RLKPPPGRNF SCVFWNTHVR ELTLASIDLQ SQMEPRTHPT WLLHIFIPFC IIAFIFIATV
IALRKQLCQK LYSSKDTTKR PVTTTKREVN SAI


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