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Q9EP73 (PD1L1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Programmed cell death 1 ligand 1
Short name=PD-L1
Short name=PDCD1 ligand 1
Short name=Programmed death ligand 1
Alternative name(s):
B7 homolog 1
Short name=B7-H1
CD_antigen=CD274
Gene names
Name:Cd274
Synonyms:B7h1, Pdcd1l1, Pdcd1lg1, Pdl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length290 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.2 Ref.5

Subunit structure

Interacts with PDCD1. Ref.1

Subcellular location

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

Tissue specificity

Highly expressed in the heart, thymus, skeletal muscle, and lung. Weakly expressed in the kidney, spleen, thyroid, and liver. Expressed on activated dendritic cells, B-cells and macrophages. Expressed in numerous tumor cells lines of lymphoid origin. Ref.1 Ref.2 Ref.4

Induction

Up-regulated by IFNG treatment in monocytes. Up-regulated on dendritic cells, B-cells and macrophages after activation by LPS and INFG. Ref.1 Ref.2

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cd80Q006094EBI-5258879,EBI-5258929

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 290272Programmed cell death 1 ligand 1
PRO_0000014554

Regions

Topological domain19 – 239221Extracellular Potential
Transmembrane240 – 26021Helical; Potential
Topological domain261 – 29030Cytoplasmic Potential
Domain19 – 127109Ig-like V-type
Domain133 – 22492Ig-like C2-type

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation1991N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Disulfide bond40 ↔ 114 By similarity
Disulfide bond154 ↔ 208 By similarity

Experimental info

Mutagenesis271L → A: PDCD1 binding. Ref.5
Mutagenesis311E → S: Significantly reduces the binding to PDCD1. Ref.5
Mutagenesis341S → Y: No effect on PDCD1 binding. Ref.5
Mutagenesis371T → Y: Significantly reduces the binding to PDCD1. Ref.5
Mutagenesis491D → S: No effect on PDCD1 binding. Ref.5
Mutagenesis561Y → S: No effect on PDCD1 binding. Ref.5
Mutagenesis581E → S: No effect on PDCD1 binding. Ref.5
Mutagenesis621E → S: No effect on PDCD1 binding. Ref.5
Mutagenesis671F → A: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells. Ref.5
Mutagenesis691A → F: No effect on PDCD1 binding. Ref.5
Mutagenesis721E → S: No effect on PDCD1 binding. Ref.5
Mutagenesis751K → S: No effect on PDCD1 binding. Ref.5
Mutagenesis891K → S: No effect on PDCD1 binding. Ref.5
Mutagenesis981A → F: No effect on PDCD1 binding. Ref.5
Mutagenesis1001Q → S: No effect on PDCD1 binding.
Mutagenesis1131C → Y: No effect on PDCD1 binding. Ref.5
Mutagenesis1151I → A: Abolishes the binding to PDCD1. Ref.5
Mutagenesis1171S → Y: No effect on PDCD1 binding. Ref.5
Mutagenesis1241K → A: Abolishes the binding to PDCD1. Ref.5
Mutagenesis1261I → A: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells. Ref.5
Mutagenesis1291K → S: Abolishes the binding to PDCD1. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9EP73 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: AB7C46CF853EBB02

FASTA29032,780
        10         20         30         40         50         60 
MRIFAGIIFT ACCHLLRAFT ITAPKDLYVV EYGSNVTMEC RFPVERELDL LALVVYWEKE 

        70         80         90        100        110        120 
DEQVIQFVAG EEDLKPQHSN FRGRASLPKD QLLKGNAALQ ITDVKLQDAG VYCCIISYGG 

       130        140        150        160        170        180 
ADYKRITLKV NAPYRKINQR ISVDPATSEH ELICQAEGYP EAEVIWTNSD HQPVSGKRSV 

       190        200        210        220        230        240 
TTSRTEGMLL NVTSSLRVNA TANDVFYCTF WRSQPGQNHT AELIIPELPA THPPQNRTHW 

       250        260        270        280        290 
VLLGSILLFL IVVSTVLLFL RKQVRMLDVE KCGVEDTSSK NRNDTQFEET

« Hide

References

« Hide 'large scale' references
[1]"Engagement of the PD-1 immunoinhibitory receptor by a novel B7-family member leads to negative regulation of lymphocyte activation."
Freeman G.J., Long A.J., Iwai Y., Bourque K., Chernova T., Nishimura H., Fitz L.J., Malenkovich N., Okazaki T., Byrne M.C., Horton H.F., Fouser L., Carter L., Ling V., Bowman M.R., Carreno B.M., Collins M., Wood C.R., Honjo T.
J. Exp. Med. 192:1027-1034(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PDCD1, TISSUE SPECIFICITY, INDUCTION.
Tissue: Spleen.
[2]"B7-H1 costimulation preferentially enhances CD28-independent T-helper cell function."
Tamura H., Dong H., Zhu G., Sica G.L., Flies D.B., Tamada K., Chen L.
Blood 97:1809-1816(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
Strain: C57BL/6.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CD-1.
Tissue: Neural stem cell.
[4]"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: TISSUE SPECIFICITY.
[5]"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 LEU-27; GLU-31; SER-34; THR-37; ASP-49; TYR-56; GLU-58; GLU-62; PHE-67; ALA-69; GLU-72; LYS-75; LYS-89; ALA-98; CYS-113; ILE-115; SER-117; LYS-124; ILE-126 AND LYS-129.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF233517 mRNA. Translation: AAG18509.1.
AF317088 mRNA. Translation: AAG31810.1.
BC066841 mRNA. Translation: AAH66841.1.
IPIIPI00109254.
RefSeqNP_068693.1. NM_021893.3.
UniGeneMm.245363.

3D structure databases

ProteinModelPortalQ9EP73.
SMRQ9EP73. Positions 19-229.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-46167N.
IntActQ9EP73. 2 interactions.

PTM databases

PhosphoSiteQ9EP73.

Proteomic databases

PRIDEQ9EP73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016640; ENSMUSP00000016640; ENSMUSG00000016496.
GeneID60533.
KEGGmmu:60533.

Organism-specific databases

CTD29126.
MGIMGI:1926446. Cd274.

Phylogenomic databases

eggNOGNOG43849.
GeneTreeENSGT00650000093373.
HOGENOMHOG000059625.
HOVERGENHBG082112.
InParanoidQ9EP73.
KOK06745.
OMAAEVIWTS.
OrthoDBEOG4DFPPP.

Gene expression databases

ArrayExpressQ9EP73.
BgeeQ9EP73.
CleanExMM_CD274.
GenevestigatorQ9EP73.
GermOnlineENSMUSG00000016496. Mus musculus.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
[Graphical view]
PfamPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD274. mouse.
NextBio314969.
SOURCESearch...

Entry information

Entry namePD1L1_MOUSE
AccessionPrimary (citable) accession number: Q9EP73
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: March 1, 2001
Last modified: April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents