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Q9WUL5

- PD1L2_MOUSE

UniProt

Q9WUL5 - PD1L2_MOUSE

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Protein

Programmed cell death 1 ligand 2

Gene

Pdcd1lg2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Biological processi

  1. negative regulation of T cell proliferation Source: MGI
  2. positive regulation of T cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Programmed cell death 1 ligand 2
Short name:
PD-1 ligand 2
Short name:
PD-L2
Short name:
PDCD1 ligand 2
Short name:
Programmed death ligand 2
Alternative name(s):
Butyrophilin B7-DC
Short name:
B7-DC
CD_antigen: CD273
Gene namesi
Name:Pdcd1lg2
Synonyms:B7dc, Btdc, Cd273, Pdl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1930125. Pdcd1lg2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331D → S: No effect on PDCD1 binding. 1 Publication
Mutagenesisi39 – 391S → Y: No effect on PDCD1 binding. 1 Publication
Mutagenesisi41 – 411E → S: No effect on PDCD1 binding. 1 Publication
Mutagenesisi56 – 561R → S: Significantly reduces the binding to PDCD1. 1 Publication
Mutagenesisi58 – 581S → Y: No effect on PDCD1 binding. 1 Publication
Mutagenesisi65 – 651D → S: No effect on PDCD1 binding. 1 Publication
Mutagenesisi67 – 671S → Y: Significantly reduces the binding to PDCD1. 1 Publication
Mutagenesisi71 – 711E → S: Significantly reduces the binding to PDCD1. 1 Publication
Mutagenesisi72 – 721R → S: No effect on PDCD1 binding. 1 Publication
Mutagenesisi84 – 841K → S: No effect on PDCD1 binding. 1 Publication
Mutagenesisi88 – 881H → A: No effect on PDCD1 binding. 1 Publication
Mutagenesisi101 – 1011R → S: Significantly reduces the binding to PDCD1. 1 Publication
Mutagenesisi103 – 1031L → A: No effect on PDCD1 binding. 1 Publication
Mutagenesisi105 – 1051I → A: Abolishes the binding to PDCD1. 1 Publication
Mutagenesisi111 – 1111D → S: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells. 1 Publication
Mutagenesisi113 – 1131K → S: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells. 1 Publication
Mutagenesisi116 – 1161T → Y: No effect on PDCD1 binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 247228Programmed cell death 1 ligand 2PRO_0000014556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 102PROSITE-ProRule annotation
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi143 ↔ 1921 PublicationPROSITE-ProRule annotation
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9WUL5.

PTM databases

PhosphoSiteiQ9WUL5.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9WUL5.
CleanExiMM_PDCD1LG2.
ExpressionAtlasiQ9WUL5. baseline and differential.
GenevestigatoriQ9WUL5.

Interactioni

Subunit structurei

Interacts with PDCD1.2 Publications

Protein-protein interaction databases

BioGridi208388. 1 interaction.
DIPiDIP-46166N.

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 336
Beta strandi38 – 447
Turni46 – 483
Helixi52 – 543
Beta strandi55 – 617
Beta strandi63 – 697
Beta strandi73 – 753
Helixi77 – 826
Beta strandi84 – 896
Helixi94 – 963
Beta strandi98 – 1069
Beta strandi109 – 12113
Beta strandi126 – 1327
Turni134 – 1363
Beta strandi139 – 14911
Beta strandi152 – 1554
Beta strandi163 – 1686
Beta strandi174 – 1829
Beta strandi190 – 1967
Turni197 – 2004
Beta strandi201 – 2077

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BOVX-ray1.77A20-123[»]
3BP5X-ray1.80B20-220[»]
3BP6X-ray1.60B20-220[»]
3RNKX-ray1.74B20-123[»]
3RNQX-ray1.60B20-220[»]
ProteinModelPortaliQ9WUL5.
SMRiQ9WUL5. Positions 20-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WUL5.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 221202ExtracellularSequence AnalysisAdd
BLAST
Topological domaini243 – 2475CytoplasmicSequence Analysis

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei222 – 24221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 11898Ig-like V-typeAdd
BLAST
Domaini122 – 20382Ig-like C2-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG39387.
GeneTreeiENSGT00650000093373.
HOGENOMiHOG000059625.
HOVERGENiHBG082112.
InParanoidiQ9WUL5.
KOiK06708.
OMAiVAWDYKY.
OrthoDBiEOG7T7GTP.
PhylomeDBiQ9WUL5.
TreeFamiTF331083.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WUL5 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLLLPILNL SLQLHPVAAL FTVTAPKEVY TVDVGSSVSL ECDFDRRECT
60 70 80 90 100
ELEGIRASLQ KVENDTSLQS ERATLLEEQL PLGKALFHIP SVQVRDSGQY
110 120 130 140 150
RCLVICGAAW DYKYLTVKVK ASYMRIDTRI LEVPGTGEVQ LTCQARGYPL
160 170 180 190 200
AEVSWQNVSV PANTSHIRTP EGLYQVTSVL RLKPQPSRNF SCMFWNAHMK
210 220 230 240
ELTSAIIDPL SRMEPKVPRT WPLHVFIPAC TIALIFLAIV IIQRKRI
Length:247
Mass (Da):27,820
Last modified:November 1, 1999 - v1
Checksum:i9BFDDE14F3EC138F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF142780 mRNA. Translation: AAD33892.1.
AK089369 mRNA. Translation: BAC40858.1.
CCDSiCCDS29736.1.
RefSeqiNP_067371.1. NM_021396.2.
UniGeneiMm.116737.

Genome annotation databases

EnsembliENSMUST00000112576; ENSMUSP00000108195; ENSMUSG00000016498.
GeneIDi58205.
KEGGimmu:58205.
UCSCiuc008hdk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF142780 mRNA. Translation: AAD33892.1 .
AK089369 mRNA. Translation: BAC40858.1 .
CCDSi CCDS29736.1.
RefSeqi NP_067371.1. NM_021396.2.
UniGenei Mm.116737.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BOV X-ray 1.77 A 20-123 [» ]
3BP5 X-ray 1.80 B 20-220 [» ]
3BP6 X-ray 1.60 B 20-220 [» ]
3RNK X-ray 1.74 B 20-123 [» ]
3RNQ X-ray 1.60 B 20-220 [» ]
ProteinModelPortali Q9WUL5.
SMRi Q9WUL5. Positions 20-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208388. 1 interaction.
DIPi DIP-46166N.

PTM databases

PhosphoSitei Q9WUL5.

Proteomic databases

PRIDEi Q9WUL5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000112576 ; ENSMUSP00000108195 ; ENSMUSG00000016498 .
GeneIDi 58205.
KEGGi mmu:58205.
UCSCi uc008hdk.2. mouse.

Organism-specific databases

CTDi 80380.
MGIi MGI:1930125. Pdcd1lg2.

Phylogenomic databases

eggNOGi NOG39387.
GeneTreei ENSGT00650000093373.
HOGENOMi HOG000059625.
HOVERGENi HBG082112.
InParanoidi Q9WUL5.
KOi K06708.
OMAi VAWDYKY.
OrthoDBi EOG7T7GTP.
PhylomeDBi Q9WUL5.
TreeFami TF331083.

Miscellaneous databases

EvolutionaryTracei Q9WUL5.
NextBioi 314189.
PROi Q9WUL5.
SOURCEi Search...

Gene expression databases

Bgeei Q9WUL5.
CleanExi MM_PDCD1LG2.
ExpressionAtlasi Q9WUL5. baseline and differential.
Genevestigatori Q9WUL5.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view ]
SMARTi SM00409. IG. 1 hit.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "B7-DC, a new dendritic cell molecule with potent costimulatory properties for T cells."
    Tseng S.-Y., Otsuji M., Gorski K., Huang X., Slansky J.E., Pai S.I., Shalabi A., Shin T., Pardoll D.M., Tsuchiya H.
    J. Exp. Med. 193:839-846(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PDCD1, TISSUE SPECIFICITY.
    Strain: BALB/c.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  3. Cited for: FUNCTION, TISSUE SPECIFICITY.
  4. "Molecular modeling and functional mapping of B7-H1 and B7-DC uncouple costimulatory function from PD-1 interaction."
    Wang S., Bajorath J., Flies D.B., Dong H., Honjo T., Chen L.
    J. Exp. Med. 197:1083-1091(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, 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.
  5. "Crystal structure of the complex between programmed death-1 (PD-1) and its ligand PD-L2."
    Lazar-Molnar E., Yan Q., Cao E., Ramagopal U., Nathenson S.G., Almo S.C.
    Proc. Natl. Acad. Sci. U.S.A. 105:10483-10488(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-220 IN COMPLEX WITH PDCD1, DISULFIDE BOND.

Entry informationi

Entry nameiPD1L2_MOUSE
AccessioniPrimary (citable) accession number: Q9WUL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3