O35235 (TNF11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tumor necrosis factor ligand superfamily member 11

Alternative name(s):
Osteoclast differentiation factor
Short name=ODF
Osteoprotegerin ligand
Short name=OPGL
Receptor activator of nuclear factor kappa-B ligand
Short name=RANKL
TNF-related activation-induced cytokine
Short name=TRANCE
CD_antigen=CD254

Cleaved into the following 2 chains:

1. Tumor necrosis factor ligand superfamily member 11, membrane form
2. Tumor necrosis factor ligand superfamily member 11, soluble form

Gene names

Name:	Tnfsf11
Synonyms:	Opgl, Rankl, Trance

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	316 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	Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.
Subunit structure	Homotrimer. Interacts with TNFRSF11A and TNFRSF11B. Ref.9 Ref.10 Ref.11
Subcellular location	Isoform 1: Cell membrane; Single-pass type II membrane protein. Isoform 2: Cell membrane; Single-pass type II membrane protein. Isoform 3: Cytoplasm. Tumor necrosis factor ligand superfamily member 11, soluble form: Secreted.
Tissue specificity	Highly expressed in thymus and lymph nodes, but not in non-lymphoid tissues and is abundantly expressed in T-cells but not in B-cells. A high level expression is also seen in the trabecular bone and lung.
Post-translational modification	N-glycosylated. Ref.8 The soluble form of isoform 1 derives from the membrane form by proteolytic processing. The cleavage may be catalyzed by ADAM17. A further shorter soluble form was observed.
Involvement in disease	Deficiency in Tnfsf11 results in failure to form lobulo-alveolar mammary structures during pregnancy, resulting in death of newborns. Trance-deficient mice show severe osteopetrosis, with no osteoclasts, marrow spaces, or tooth eruption, and exhibit profound growth retardation at several skeletal sites, including the limbs, skull, and vertebrae and have marked chondrodysplasia, with thick, irregular growth plates and a relative increase in hypertrophic chondrocytes.
Sequence similarities	Belongs to the tumor necrosis factor family.

Ontologies

Keywords
Biological process	Differentiation
Cellular component	Cell membrane Cytoplasm Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Cytokine Developmental protein Receptor
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ERK1 and ERK2 cascade Inferred from direct assay PubMed 19252502. Source: DFLAT activation of JUN kinase activity Inferred from direct assay PubMed 19252502. Source: DFLAT bone resorption Inferred from direct assay PubMed 12490655. Source: MGI calcium ion homeostasis Inferred from genetic interaction PubMed 21982707. Source: MGI immune response Inferred from electronic annotation. Source: InterPro lymph node development Traceable author statement PubMed 10687308. Source: MGI mammary gland alveolus development Inferred from mutant phenotype PubMed 11051546. Source: MGI mammary gland epithelial cell proliferation Inferred from mutant phenotype PubMed 11051546. Source: MGI monocyte chemotaxis Inferred from electronic annotation. Source: Compara organ morphogenesis Inferred from mutant phenotype PubMed 9950424. Source: MGI ossification Inferred from mutant phenotype PubMed 9950424. Source: MGI osteoclast differentiation Inferred from mutant phenotype PubMed 15750601. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade via TNFSF11-mediated signaling Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay PubMed 19298785. Source: MGI positive regulation of JNK cascade Inferred from genetic interaction PubMed 22073305. Source: MGI positive regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of T cell activation Inferred from electronic annotation. Source: Compara positive regulation of bone resorption Inferred from electronic annotation. Source: Compara positive regulation of corticotropin-releasing hormone secretion Inferred from direct assay PubMed 19940926. Source: BHF-UCL positive regulation of fever generation by positive regulation of prostaglandin secretion Inferred from direct assay PubMed 19940926. Source: BHF-UCL positive regulation of homotypic cell-cell adhesion Inferred from electronic annotation. Source: Compara positive regulation of osteoclast differentiation Inferred from direct assay PubMed 15657444PubMed 15724149. Source: MGI positive regulation of protein kinase B signaling cascade Inferred from mutant phenotype PubMed 11051546. Source: MGI positive regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 19940926. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from direct assay PubMed 11859102. Source: MGI tumor necrosis factor-mediated signaling pathway Inferred from genetic interaction PubMed 19940926. Source: BHF-UCL
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular Inferred from direct assay PubMed 19723499. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O35235-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O35235-2)

The sequence of this isoform differs from the canonical sequence as follows:
     14-44: SSEEMGSGPGVPHEGPLHPAPSAPAPAPPPA → TP

Isoform 3 (identifier: O35235-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 316

316

Tumor necrosis factor ligand superfamily member 11, membrane form

PRO_0000034516

Chain

139 – 316

178

Tumor necrosis factor ligand superfamily member 11, soluble form

PRO_0000034517

Regions

Topological domain

1 – 48

48

Cytoplasmic Potential

Transmembrane

49 – 69

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

70 – 316

247

Extracellular Potential

Sites

Site

138 – 139

2

Cleavage

Amino acid modifications

Glycosylation

197

1

N-linked (GlcNAc...) Potential

Glycosylation

262

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 117

117

Missing in isoform 3.

VSP_006448

Alternative sequence

14 – 44

31

SSEEM…APPPA → TP in isoform 2.

VSP_006449

Experimental info

Sequence conflict

99

1

D → G in AAC71061. Ref.1

Sequence conflict

99

1

D → G in AAC40113. Ref.3

Sequence conflict

99

1

D → G in BAA25425. Ref.4

Sequence conflict

99

1

D → G in BAA36970. Ref.5

Sequence conflict

99

1

D → G in BAA97257. Ref.6

Sequence conflict

99

1

D → G in BAA97259. Ref.6

Sequence conflict

141 – 143

3

Missing in BAA36970. Ref.5

Secondary structure

1

.

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.

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.

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.

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316

Helix Strand Turn

Details...

Beta strand

164 – 169

6

Helix

171 – 173

3

Beta strand

177 – 179

3

Beta strand

181 – 183

3

Beta strand

186 – 190

5

Beta strand

194 – 201

8

Beta strand

204 – 207

4

Beta strand

211 – 224

14

Helix

225 – 227

3

Beta strand

233 – 248

16

Beta strand

251 – 262

12

Beta strand

265 – 282

18

Beta strand

286 – 293

8

Helix

295 – 297

3

Turn

302 – 304

3

Beta strand

305 – 313

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 8AF3825F92E0A786	FASTA	316	35,003
	10 20 30 40 50 60 MRRASRDYGK YLRSSEEMGS GPGVPHEGPL HPAPSAPAPA PPPAASRSMF LALLGLGLGQ 70 80 90 100 110 120 VVCSIALFLY FRAQMDPNRI SEDSTHCFYR ILRLHENADL QDSTLESEDT LPDSCRRMKQ 130 140 150 160 170 180 AFQGAVQKEL QHIVGPQRFS GAPAMMEGSW LDVAQRGKPE AQPFAHLTIN AASIPSGSHK 190 200 210 220 230 240 VTLSSWYHDR GWAKISNMTL SNGKLRVNQD GFYYLYANIC FRHHETSGSV PTDYLQLMVY 250 260 270 280 290 300 VVKTSIKIPS SHNLMKGGST KNWSGNSEFH FYSINVGGFF KLRAGEEISI QVSNPSLLDP 310 DQDATYFGAF KVQDID
	Isoform 2 [UniParc]. Checksum: 09000919EB550530	FASTA	287	32,293
	10 20 30 40 50 60 MRRASRDYGK YLRTPASRSM FLALLGLGLG QVVCSIALFL YFRAQMDPNR ISEDSTHCFY 70 80 90 100 110 120 RILRLHENAD LQDSTLESED TLPDSCRRMK QAFQGAVQKE LQHIVGPQRF SGAPAMMEGS 130 140 150 160 170 180 WLDVAQRGKP EAQPFAHLTI NAASIPSGSH KVTLSSWYHD RGWAKISNMT LSNGKLRVNQ 190 200 210 220 230 240 DGFYYLYANI CFRHHETSGS VPTDYLQLMV YVVKTSIKIP SSHNLMKGGS TKNWSGNSEF 250 260 270 280 HFYSINVGGF FKLRAGEEIS IQVSNPSLLD PDQDATYFGA FKVQDID
	Isoform 3 [UniParc]. Checksum: 401C13EB5E8CE166	FASTA	199	22,150
	10 20 30 40 50 60 MKQAFQGAVQ KELQHIVGPQ RFSGAPAMME GSWLDVAQRG KPEAQPFAHL TINAASIPSG 70 80 90 100 110 120 SHKVTLSSWY HDRGWAKISN MTLSNGKLRV NQDGFYYLYA NICFRHHETS GSVPTDYLQL 130 140 150 160 170 180 MVYVVKTSIK IPSSHNLMKG GSTKNWSGNS EFHFYSINVG GFFKLRAGEE ISIQVSNPSL 190 LDPDQDATYF GAFKVQDID

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TRANCE is a novel ligand of the tumor necrosis factor receptor family that activates c-Jun N-terminal kinase in T cells." Wong B.R., Rho J., Arron J., Robinson E., Orlinick J., Chao M., Kalachikov S., Cayani E., Bartlett F.S. III, Frankel W.N., Lee S.Y., Choi Y. J. Biol. Chem. 272:25190-25194(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Hybridoma.
[2]	"A homologue of the TNF receptor and its ligand enhance T-cell growth and dendritic-cell function." Anderson D.M., Maraskovsky E., Billingsley W.L., Dougall W.C., Tometsko M.E., Roux E.R., Teepe M.C., DuBose R.F., Cosman D., Galibert L. Nature 390:175-179(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Thymic lymphoma.
[3]	"Osteoprotegerin ligand is a cytokine that regulates osteoclast differentiation and activation." Lacey D.L., Timms E., Tan H.-L., Kelley M.J., Dunstan C.R., Burgess T., Elliott R., Colombero A., Elliott G., Scully S., Hsu H., Sullivan J., Hawkins N., Davy E., Capparelli C., Eli A., Qian Y.-X., Kaufman S. , Sarosi I., Shalhoub V., Senaldi G., Guo J., Delaney J., Boyle W.J. Cell 93:165-176(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Bone marrow.
[4]	"Osteoclast differentiation factor is a ligand for osteoprotegerin/osteoclastogenesis-inhibitory factor and is identical to TRANCE/RANKL." Yasuda H., Shima N., Nakagawa N., Yamaguchi K., Kinosaki M., Mochizuki S., Tomoyasu A., Yano K., Goto M., Murakami A., Tsuda E., Morinaga T., Higashio K., Udagawa N., Takahashi N., Suda T. Proc. Natl. Acad. Sci. U.S.A. 95:3597-3602(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Bone marrow stroma.
[5]	"Cloning and characterization of the gene encoding mouse osteoclast differentiation factor." Kodaira K., Kodaira K., Mizuno A., Yasuda H., Shima N., Murakami A., Ueda M., Higashio K. Gene 230:121-127(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). Strain: 129.
[6]	"Determination of three isoforms of the receptor activator of nuclear factor-kappaB ligand and their differential expression in bone and thymus." Ikeda T., Kasai M., Utsuyama M., Hirokawa K. Endocrinology 142:1419-1426(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[7]	"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] (ISOFORM 1). Strain: C57BL/6J.
[8]	"Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival." Lum L., Wong B.R., Josien R., Becherer J.D., Erdjument-Bromage H., Schloendorff J., Tempst P., Choi Y., Blobel C.P. J. Biol. Chem. 274:13613-13618(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 139-147, PROTEOLYTIC PROCESSING, GLYCOSYLATION.
[9]	"Crystal structure of the TRANCE/RANKL cytokine reveals determinants of receptor-ligand specificity." Lam J., Nelson C.A., Ross F.P., Teitelbaum S.L., Fremont D.H. J. Clin. Invest. 108:971-979(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 158-316, SUBUNIT.
[10]	"Crystal structure of the extracellular domain of mouse RANK ligand at 2.2-A resolution." Ito S., Wakabayashi K., Ubukata O., Hayashi S., Okada F., Hata T. J. Biol. Chem. 277:6631-6636(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 137-316, SUBUNIT.
[11]	"Structural and functional insights of RANKL-RANK interaction and signaling." Liu C., Walter T.S., Huang P., Zhang S., Zhu X., Wu Y., Wedderburn L.R., Tang P., Owens R.J., Stuart D.I., Ren J., Gao B. J. Immunol. 184:6910-6919(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 158-316 IN COMPLEX WITH TNFRSF11A, INTERACTION WITH TNFRSF11A, SUBUNIT.
[12]	"RANKL employs distinct binding modes to engage RANK and the osteoprotegerin decoy receptor." Nelson C.A., Warren J.T., Wang M.W., Teitelbaum S.L., Fremont D.H. Structure 20:1971-1982(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 162-316 IN COMPLEX WITH TNFRSF11B.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF013170 mRNA. Translation: AAC71061.1.
AF019048 mRNA. Translation: AAB86812.1.
AF053713 mRNA. Translation: AAC40113.1.
AB008426 mRNA. Translation: BAA25425.1.
AB022039 Genomic DNA. Translation: BAA36970.1.
AB032771 mRNA. Translation: BAA97257.1.
AB032772 mRNA. Translation: BAA97258.1.
AB036798 mRNA. Translation: BAA97259.1.
AK159498 mRNA. Translation: BAE35131.1.

IPI

IPI00128604.
IPI00227894.
IPI00875021.

RefSeq

NP_035743.2. NM_011613.3.

UniGene

Mm.249221.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IQA	X-ray	2.20	A/B/C	157-316	[»]
1JTZ	X-ray	2.60	X/Y/Z	156-316	[»]
1S55	X-ray	1.90	A/B/C	161-316	[»]
3ME2	X-ray	2.80	A	158-316	[»]
3QBQ	X-ray	2.50	A/C	157-316	[»]
4E4D	X-ray	2.70	X	162-316	[»]
4GIQ	X-ray	2.70	A	158-316	[»]

ProteinModelPortal

O35235.

SMR

O35235. Positions 161-316.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59480N.

PTM databases

PhosphoSite

O35235.

Proteomic databases

PRIDE

O35235.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000022592; ENSMUSP00000022592; ENSMUSG00000022015.

GeneID

21943.

KEGG

mmu:21943.

Organism-specific databases

CTD

8600.

MGI

MGI:1100089. Tnfsf11.

Phylogenomic databases

eggNOG

NOG40842.

GeneTree

ENSGT00530000063443.

HOGENOM

HOG000132981.

HOVERGEN

HBG054257.

InParanoid

Q3TWY5.

KO

K05473.

OMA

GKLIVNQ.

OrthoDB

EOG4FTW12.

Gene expression databases

Bgee

O35235.

Genevestigator

O35235.

GermOnline

ENSMUSG00000022015. Mus musculus.

Family and domain databases

Gene3D

2.60.120.40. 1 hit.

InterPro

IPR006052. TNF.
IPR017355. TNF_ligand_10/11.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]

Pfam

PF00229. TNF. 1 hit.
[Graphical view]

PIRSF

PIRSF038013. TNF10_TNF11. 1 hit.

SMART

SM00207. TNF. 1 hit.
[Graphical view]

SUPFAM

SSF49842. TNF_like. 1 hit.

PROSITE

PS00251. TNF_1. False negative.
PS50049. TNF_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TNFSF11. mouse.

EvolutionaryTrace

O35235.

NextBio

301584.

PMAP-CutDB

Q3TWY5.

SOURCE

Search...

Entry information

Entry name

TNF11_MOUSE

Accession

Primary (citable) accession number: O35235
Secondary accession number(s): O35306 , Q3TWY5, Q9JJK8, Q9JJK9, Q9R1Y0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program