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Q9WUL5 (PD1L2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Pdcd1lg2
Synonyms:B7dc, Btdc, Cd273, Pdl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.3 Ref.4

Subunit structure

Interacts with PDCD1. Ref.1

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

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. Ref.1 Ref.3

Sequence similarities

Belongs to the immunoglobulin superfamily. BTN/MOG family.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 247228Programmed cell death 1 ligand 2
PRO_0000014556

Regions

Topological domain20 – 221202Extracellular Potential
Transmembrane222 – 24221Helical; Potential
Topological domain243 – 2475Cytoplasmic Potential
Domain21 – 11898Ig-like V-type
Domain122 – 20382Ig-like C2-type

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation1891N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 102 By similarity
Disulfide bond143 ↔ 192 Ref.5

Experimental info

Mutagenesis331D → S: No effect on PDCD1 binding. Ref.4
Mutagenesis391S → Y: No effect on PDCD1 binding. Ref.4
Mutagenesis411E → S: No effect on PDCD1 binding. Ref.4
Mutagenesis561R → S: Significantly reduces the binding to PDCD1. Ref.4
Mutagenesis581S → Y: No effect on PDCD1 binding. Ref.4
Mutagenesis651D → S: No effect on PDCD1 binding. Ref.4
Mutagenesis671S → Y: Significantly reduces the binding to PDCD1. Ref.4
Mutagenesis711E → S: Significantly reduces the binding to PDCD1. Ref.4
Mutagenesis721R → S: No effect on PDCD1 binding. Ref.4
Mutagenesis841K → S: No effect on PDCD1 binding. Ref.4
Mutagenesis881H → A: No effect on PDCD1 binding. Ref.4
Mutagenesis1011R → S: Significantly reduces the binding to PDCD1. Ref.4
Mutagenesis1031L → A: No effect on PDCD1 binding. Ref.4
Mutagenesis1051I → A: Abolishes the binding to PDCD1. Ref.4
Mutagenesis1111D → S: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells. Ref.4
Mutagenesis1131K → S: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells. Ref.4
Mutagenesis1161T → Y: No effect on PDCD1 binding. Ref.4

Secondary structure

........................................ 247
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WUL5 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 9BFDDE14F3EC138F

FASTA24727,820
        10         20         30         40         50         60 
MLLLLPILNL SLQLHPVAAL FTVTAPKEVY TVDVGSSVSL ECDFDRRECT ELEGIRASLQ 

        70         80         90        100        110        120 
KVENDTSLQS ERATLLEEQL PLGKALFHIP SVQVRDSGQY RCLVICGAAW DYKYLTVKVK 

       130        140        150        160        170        180 
ASYMRIDTRI LEVPGTGEVQ LTCQARGYPL AEVSWQNVSV PANTSHIRTP EGLYQVTSVL 

       190        200        210        220        230        240 
RLKPQPSRNF SCMFWNAHMK ELTSAIIDPL SRMEPKVPRT WPLHVFIPAC TIALIFLAIV 


IIQRKRI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"PD-L2 is a second ligand for PD-1 and inhibits T cell activation."
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. expand/collapse author list , Honjo T., Sharpe A.H., Freeman G.J.
Nat. Immunol. 2:261-268(2001) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF142780 mRNA. Translation: AAD33892.1.
AK089369 mRNA. Translation: BAC40858.1.
RefSeqNP_067371.1. NM_021396.2.
UniGeneMm.116737.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BOVX-ray1.77A20-123[»]
3BP5X-ray1.80B20-220[»]
3BP6X-ray1.60B20-220[»]
3RNKX-ray1.74B20-123[»]
3RNQX-ray1.60B20-220[»]
ProteinModelPortalQ9WUL5.
SMRQ9WUL5. Positions 20-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208388. 1 interaction.
DIPDIP-46166N.

PTM databases

PhosphoSiteQ9WUL5.

Proteomic databases

PRIDEQ9WUL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000112576; ENSMUSP00000108195; ENSMUSG00000016498.
GeneID58205.
KEGGmmu:58205.
UCSCuc008hdk.2. mouse.

Organism-specific databases

CTD80380.
MGIMGI:1930125. Pdcd1lg2.

Phylogenomic databases

eggNOGNOG39387.
GeneTreeENSGT00650000093373.
HOGENOMHOG000059625.
HOVERGENHBG082112.
InParanoidQ9WUL5.
KOK06708.
OMAVAWDYKY.
OrthoDBEOG7T7GTP.
PhylomeDBQ9WUL5.
TreeFamTF331083.

Gene expression databases

ArrayExpressQ9WUL5.
BgeeQ9WUL5.
CleanExMM_PDCD1LG2.
GenevestigatorQ9WUL5.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9WUL5.
NextBio314189.
PROQ9WUL5.
SOURCESearch...

Entry information

Entry namePD1L2_MOUSE
AccessionPrimary (citable) accession number: Q9WUL5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot