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Q9WUL5

- PD1L2_MOUSE

UniProt

Q9WUL5 - PD1L2_MOUSE

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
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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 - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

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

    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. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiQ9WUL5.
    BgeeiQ9WUL5.
    CleanExiMM_PDCD1LG2.
    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.

    Q9WUL5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLLLPILNL SLQLHPVAAL FTVTAPKEVY TVDVGSSVSL ECDFDRRECT    50
    ELEGIRASLQ KVENDTSLQS ERATLLEEQL PLGKALFHIP SVQVRDSGQY 100
    RCLVICGAAW DYKYLTVKVK ASYMRIDTRI LEVPGTGEVQ LTCQARGYPL 150
    AEVSWQNVSV PANTSHIRTP EGLYQVTSVL RLKPQPSRNF SCMFWNAHMK 200
    ELTSAIIDPL SRMEPKVPRT WPLHVFIPAC TIALIFLAIV IIQRKRI 247
    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

    ArrayExpressi Q9WUL5.
    Bgeei Q9WUL5.
    CleanExi MM_PDCD1LG2.
    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

    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 1, 2014
    This is version 101 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