Q9WUL5 (PD1L2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Pdcd1lg2
Synonyms:	B7dc, Btdc, Cd273, Pdl2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	247 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of T cell proliferation Inferred from direct assay Ref.3PubMed 17016562. Source: MGI positive regulation of T cell proliferation Inferred from direct assay Ref.1. Source: MGI
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

By similarity

Chain

20 – 247

228

Programmed cell death 1 ligand 2

PRO_0000014556

Regions

Topological domain

20 – 221

202

Extracellular Potential

Transmembrane

222 – 242

21

Helical; Potential

Topological domain

243 – 247

5

Cytoplasmic Potential

Domain

21 – 118

98

Ig-like V-type

Domain

122 – 203

82

Ig-like C2-type

Amino acid modifications

Glycosylation

64

1

N-linked (GlcNAc...) Potential

Glycosylation

157

1

N-linked (GlcNAc...) Potential

Glycosylation

163

1

N-linked (GlcNAc...) Potential

Glycosylation

189

1

N-linked (GlcNAc...) Potential

Disulfide bond

42 ↔ 102

By similarity

Disulfide bond

143 ↔ 192

Ref.5

Experimental info

Mutagenesis

33

1

D → S: No effect on PDCD1 binding. Ref.4

Mutagenesis

39

1

S → Y: No effect on PDCD1 binding. Ref.4

Mutagenesis

41

1

E → S: No effect on PDCD1 binding. Ref.4

Mutagenesis

56

1

R → S: Significantly reduces the binding to PDCD1. Ref.4

Mutagenesis

58

1

S → Y: No effect on PDCD1 binding. Ref.4

Mutagenesis

65

1

D → S: No effect on PDCD1 binding. Ref.4

Mutagenesis

67

1

S → Y: Significantly reduces the binding to PDCD1. Ref.4

Mutagenesis

71

1

E → S: Significantly reduces the binding to PDCD1. Ref.4

Mutagenesis

72

1

R → S: No effect on PDCD1 binding. Ref.4

Mutagenesis

84

1

K → S: No effect on PDCD1 binding. Ref.4

Mutagenesis

88

1

H → A: No effect on PDCD1 binding. Ref.4

Mutagenesis

101

1

R → S: Significantly reduces the binding to PDCD1. Ref.4

Mutagenesis

103

1

L → A: No effect on PDCD1 binding. Ref.4

Mutagenesis

105

1

I → A: Abolishes the binding to PDCD1. Ref.4

Mutagenesis

111

1

D → S: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells. Ref.4

Mutagenesis

113

1

K → S: Abolishes the binding to PDCD1. Costimulates proliferation and IFNG production of T-cells. Ref.4

Mutagenesis

116

1

T → Y: No effect on PDCD1 binding. Ref.4

Secondary structure

1

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247

Helix Strand Turn

Details...

Beta strand

28 – 33

6

Beta strand

38 – 44

7

Turn

46 – 48

3

Helix

52 – 54

3

Beta strand

55 – 61

7

Beta strand

63 – 69

7

Beta strand

73 – 75

3

Helix

77 – 82

6

Beta strand

84 – 89

6

Helix

94 – 96

3

Beta strand

98 – 106

9

Beta strand

109 – 121

13

Beta strand

126 – 132

7

Turn

134 – 136

3

Beta strand

139 – 149

11

Beta strand

152 – 155

4

Beta strand

163 – 168

6

Beta strand

174 – 182

9

Beta strand

190 – 196

7

Turn

197 – 200

4

Beta strand

201 – 207

7

Sequences

	Sequence		Length	Mass (Da)
	Q9WUL5 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 9BFDDE14F3EC138F	FASTA	247	27,820
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00124785.

RefSeq

NP_067371.1. NM_021396.2.

UniGene

Mm.116737.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9WUL5.

SMR

Q9WUL5. Positions 20-209.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46166N.

PTM databases

PhosphoSite

Q9WUL5.

Proteomic databases

PRIDE

Q9WUL5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000112576; ENSMUSP00000108195; ENSMUSG00000016498.

GeneID

58205.

KEGG

mmu:58205.

Organism-specific databases

CTD

80380.

MGI

MGI:1930125. Pdcd1lg2.

Phylogenomic databases

eggNOG

NOG39387.

GeneTree

ENSGT00650000093373.

HOGENOM

HOG000059625.

HOVERGEN

HBG082112.

InParanoid

Q9WUL5.

KO

K06708.

OMA

VAWDYKY.

OrthoDB

EOG4VHK74.

Gene expression databases

ArrayExpress

Q9WUL5.

Bgee

Q9WUL5.

CleanEx

MM_PDCD1LG2.

Genevestigator

Q9WUL5.

GermOnline

ENSMUSG00000016498. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]

SMART

SM00409. IG. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9WUL5.

NextBio

314189.

SOURCE

Search...

Entry information

Entry name

PD1L2_MOUSE

Accession

Primary (citable) accession number: Q9WUL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	November 1, 1999
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program