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Q8CI19 (PDGFC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Platelet-derived growth factor C

Short name=PDGF-C
Alternative name(s):
Fallotein
Spinal cord-derived growth factor
Short name=SCDGF
VEGF-E

Cleaved into the following 2 chains:

  1. Platelet-derived growth factor C, latent form
    Short name=PDGFC latent form
  2. Platelet-derived growth factor C, receptor-binding form
    Short name=PDGFC receptor-binding form
Gene names
Name:Pdgfc
Synonyms:Scdgf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen and chemoattractant for cells of mesenchymal origin. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function. Ref.6 Ref.7 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.22

Subunit structure

Homodimer; disulfide-linked. Interacts with PDGFRA homodimers, and with heterodimers formed by PDGFRA and PDGFRB. Interacts (via CUB domain) with PLAT (via kringle domain) By similarity. Ref.6 Ref.7

Subcellular location

Cytoplasm. Secreted. Nucleus. Cytoplasmic granule By similarity. Note: Sumoylated form is predominant in the nucleus. Stored in alpha granules in platelets By similarity. Membrane associated when bound to receptors By similarity. Secretion increased by TGFB1. Ref.14 Ref.20

Tissue specificity

Mainly expressed in kidney, testis, liver, heart and brain (at protein level). Highly expressed in airway epithelium, interstitial cells and alveolar macrophages in the lung of mice overexpressing IL13. Expressed in the ovaries. Ref.7 Ref.9 Ref.19 Ref.21 Ref.22

Developmental stage

In stage E9.5-E15.5, widely expressed in the surface ectoderm and later in the germinal layer of the skin, the olfactory and otic placode and their derivatives and the lining of the oral cavity. In stages E14.5-17.5 expressed in ducts connected to epidermis, and in developing epidermal openings. Highly expressed in the early stages of the developing kidney, in the metanephric mesenchymal aggregates, prefusion skeletal muscle, cardiac myoblasts, and in visceral and vascular smooth muscle. Ref.1 Ref.6 Ref.12 Ref.14

Induction

Expression decreased by hypoxia. Up-regulated by EWS-FLI1 transcription factor in tumor-derived cells. Up-regulated by IL13 overexpression in the lung via STAT6 and EGR1. Elevated expression induced by coxsackievirus B3 infection in immunodeficient mice. Overexpressed in the renal fibrosis. Expression in the lung is significantly increased after bleomycin treatment. Down-regulated by retinoic acid and gonadotropin. Ref.8 Ref.11 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21

Post-translational modification

Proteolytic removal of the N-terminal CUB domain releasing the core domain is necessary for unmasking the receptor-binding epitopes of the core domain. Cleavage after basic residues in the hinge region (region connecting the CUB and growth factor domains) gives rise to the receptor-binding form. Cleaved by PLAT and PLG By similarity.

Sumoylated by SUMO1. Ref.20

N-glycosylated By similarity.

Involvement in disease

Involved in the development of myocarditis and subsequent fibrosis in the experimental model of coxsackievirus B3-induced chronic myocarditis. Ref.16

Disruption phenotype

Perinatal lethality. Mice have feeding and respiratory difficulties due to a complete cleft of the secondary palate. However, they have reduction of renal fibrogenesis. Mice lacking both PDGFA and PDGFC develop a cleft face, subepidermal blistering, deficiency of renal cortex mesenchyme, spina bifida and skeletal and vascular defects. Ref.15 Ref.22

Sequence similarities

Belongs to the PDGF/VEGF growth factor family.

Contains 1 CUB domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Secreted
   DomainSignal
   Molecular functionDevelopmental protein
Growth factor
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of transmembrane receptor protein tyrosine kinase activity

Inferred from direct assay Ref.6. Source: MGI

cellular response to amino acid stimulus

Inferred from direct assay PubMed 20548288. Source: MGI

organ morphogenesis

Inferred from mutant phenotype Ref.15. Source: MGI

platelet-derived growth factor receptor signaling pathway

Inferred from direct assay Ref.14. Source: MGI

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell proliferation

Inferred from direct assay Ref.6PubMed 15234987. Source: MGI

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 11940581. Source: MGI

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from direct assay Ref.6. Source: MGI

extracellular space

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionplatelet-derived growth factor receptor binding

Inferred from direct assay Ref.6Ref.14. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 345323Platelet-derived growth factor C, latent form
PRO_0000343873
Chain? – 345Platelet-derived growth factor C, receptor-binding formPRO_0000343874

Regions

Domain46 – 163118CUB

Sites

Site225 – 2262Cleavage By similarity
Site231 – 2322Cleavage By similarity
Site234 – 2352Cleavage By similarity

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation551N-linked (GlcNAc...) Potential
Disulfide bond104 ↔ 124 By similarity
Disulfide bond250 ↔ 294 By similarity
Disulfide bond274Interchain (with C-286) By similarity
Disulfide bond280 ↔ 335 By similarity
Disulfide bond286Interchain (with C-274) By similarity
Disulfide bond287 ↔ 337 By similarity

Experimental info

Sequence conflict861I → T in AAF91483. Ref.1
Sequence conflict1031I → L in AAH37696. Ref.5
Sequence conflict1271G → E in AAF91483. Ref.1
Sequence conflict2301G → V in AAF91483. Ref.1
Sequence conflict2691I → R in AAF91483. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8CI19 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 3A58A1F701B84EA2

FASTA34538,741
        10         20         30         40         50         60 
MLLLGLLLLT SALAGQRTGT RAESNLSSKL QLSSDKEQNG VQDPRHERVV TISGNGSIHS 

        70         80         90        100        110        120 
PKFPHTYPRN MVLVWRLVAV DENVRIQLTF DERFGLEDPE DDICKYDFVE VEEPSDGSVL 

       130        140        150        160        170        180 
GRWCGSGTVP GKQTSKGNHI RIRFVSDEYF PSEPGFCIHY SIIMPQVTET TSPSVLPPSS 

       190        200        210        220        230        240 
LSLDLLNNAV TAFSTLEELI RYLEPDRWQV DLDSLYKPTW QLLGKAFLYG KKSKVVNLNL 

       250        260        270        280        290        300 
LKEEVKLYSC TPRNFSVSIR EELKRTDTIF WPGCLLVKRC GGNCACCLHN CNECQCVPRK 

       310        320        330        340 
VTKKYHEVLQ LRPKTGVKGL HKSLTDVALE HHEECDCVCR GNAGG 

« Hide

References

« Hide 'large scale' references
[1]"The mouse Pdgfc gene: dynamic expression in embryonic tissues during organogenesis."
Ding H., Wu X., Kim I., Tam P.P., Koh G.Y., Nagy A.
Mech. Dev. 96:209-213(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
Strain: Swiss Webster / NIH.
[2]"cDNA cloning of fallotein from mouse ovary."
Tsai Y.-J., Lee R.K.-K., Chen Y.-H., Lin S.-P., Cheng W.T.-K.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[3]"Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha receptor."
Gao Z., Hart C., Piddington C., Sheppard P., Shoemaker K., Gilbertson D., West J., O'Hara P.J.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[4]"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.
Tissue: Cecum, Cerebellum and Head.
[5]"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: Czech II and FVB/N.
Tissue: Mammary tumor.
[6]"PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor."
Li X., Ponten A., Aase K., Karlsson L., Abramsson A., Uutela M., Backstrom G., Hellstrom M., Bostrom H., Li H., Soriano P., Betsholtz C., Heldin C.H., Alitalo K., Ostman A., Eriksson U.
Nat. Cell Biol. 2:302-309(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE.
[7]"Platelet-derived growth factor C (PDGF-C), a novel growth factor that binds to PDGF alpha and beta receptor."
Gilbertson D.G., Duff M.E., West J.W., Kelly J.D., Sheppard P.O., Hofstrand P.D., Gao Z., Shoemaker K., Bukowski T.R., Moore M., Feldhaus A.L., Humes J.M., Palmer T.E., Hart C.E.
J. Biol. Chem. 276:27406-27414(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
[8]"PDGF-C is an EWS/FLI induced transforming growth factor in Ewing family tumors."
Zwerner J.P., May W.A.
Oncogene 20:626-633(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[9]"Expression analysis of PDGF-C in adult and developing mouse tissues."
Aase K., Abramsson A., Karlsson L., Betsholtz C., Eriksson U.
Mech. Dev. 110:187-191(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Transgenic overexpression of platelet-derived growth factor-C in the mouse heart induces cardiac fibrosis, hypertrophy, and dilated cardiomyopathy."
Ponten A., Li X., Thoren P., Aase K., Sjoblom T., Ostman A., Eriksson U.
Am. J. Pathol. 163:673-682(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Modulation of PDGF-C and PDGF-D expression during bleomycin-induced lung fibrosis."
Zhuo Y., Zhang J., Laboy M., Lasky J.A.
Am. J. Physiol. 286:L182-L188(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY BLEOMYCIN.
[12]"PDGF C is a selective alpha platelet-derived growth factor receptor agonist that is highly expressed in platelet alpha granules and vascular smooth muscle."
Fang L., Yan Y., Komuves L.G., Yonkovich S., Sullivan C.M., Stringer B., Galbraith S., Lokker N.A., Hwang S.S., Nurden P., Phillips D.R., Giese N.A.
Arterioscler. Thromb. Vasc. Biol. 24:787-792(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[13]"PDGF signaling in cells and mice."
Tallquist M., Kazlauskas A.
Cytokine Growth Factor Rev. 15:205-213(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[14]"Tissue plasminogen activator is a potent activator of PDGF-CC."
Fredriksson L., Li H., Fieber C., Li X., Eriksson U.
EMBO J. 23:3793-3802(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, ACTIVATION BY PROTEOLYTIC CLEAVAGE.
[15]"A specific requirement for PDGF-C in palate formation and PDGFR-alpha signaling."
Ding H., Wu X., Bostrom H., Kim I., Wong N., Tsoi B., O'Rourke M., Koh G.Y., Soriano P., Betsholtz C., Hart T.C., Marazita M.L., Field L.L., Tam P.P., Nagy A.
Nat. Genet. 36:1111-1116(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[16]"Linkage between elevated PDGF-C expression and myocardial fibrogenesis in coxsackievirus B3-induced chronic myocarditis."
Yang D., Qiu D.
Eur. Heart J. 26:642-643(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY COXSACKIEVIRUS B3 INFECTION, DISEASE.
[17]"Structural requirements for activation of latent platelet-derived growth factor CC by tissue plasminogen activator."
Fredriksson L., Ehnman M., Fieber C., Eriksson U.
J. Biol. Chem. 280:26856-26862(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[18]"PDGF-C controls proliferation and is down-regulated by retinoic acid in mouse embryonic palatal mesenchymal cells."
Han J., Xiao Y., Lin J., Li Y.
Birth Defects Res. B Dev. Reprod. Toxicol. 77:438-444(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY RETINOIC ACID.
[19]"Aberrant expression of PDGF ligands and receptors in the tumor prone ovary of follitropin receptor knockout (FORKO) mouse."
Chen X., Aravindakshan J., Yang Y., Tiwari-Pandey R., Sairam M.R.
Carcinogenesis 27:903-915(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION BY GONADOTROPIN.
[20]"Nuclear localisation of endogenous SUMO-1-modified PDGF-C in human thyroid tissue and cell lines."
Reigstad L.J., Martinez A., Varhaug J.E., Lillehaug J.R.
Exp. Cell Res. 312:782-795(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, SUMOYLATION.
[21]"Opposing actions of Stat1 and Stat6 on IL-13-induced up-regulation of early growth response-1 and platelet-derived growth factor ligands in pulmonary fibroblasts."
Ingram J.L., Antao-Menezes A., Mangum J.B., Lyght O., Lee P.J., Elias J.A., Bonner J.C.
J. Immunol. 177:4141-4148(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION BY IL13.
[22]"PDGF-C is a proinflammatory cytokine that mediates renal interstitial fibrosis."
Eitner F., Bucher E., van Roeyen C., Kunter U., Rong S., Seikrit C., Villa L., Boor P., Fredriksson L., Backstrom G., Eriksson U., Ostman A., Floege J., Ostendorf T.
J. Am. Soc. Nephrol. 19:281-289(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF286725 mRNA. Translation: AAF91483.1.
AF117608 mRNA. Translation: AAF22516.1.
AF266467 mRNA. Translation: AAK58566.1.
AK033734 mRNA. Translation: BAC28455.1.
AK042767 mRNA. Translation: BAC31358.1.
AK052947 mRNA. Translation: BAC35216.1.
BC006027 mRNA. Translation: AAH06027.1.
BC037696 mRNA. Translation: AAH37696.1.
CCDSCCDS17425.1.
RefSeqNP_064355.1. NM_019971.2.
UniGeneMm.331089.

3D structure databases

ProteinModelPortalQ8CI19.
SMRQ8CI19. Positions 53-198.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8CI19.

Proteomic databases

PRIDEQ8CI19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029652; ENSMUSP00000029652; ENSMUSG00000028019.
GeneID54635.
KEGGmmu:54635.
UCSCuc008poi.1. mouse.

Organism-specific databases

CTD56034.
MGIMGI:1859631. Pdgfc.

Phylogenomic databases

eggNOGNOG74970.
GeneTreeENSGT00390000005171.
HOGENOMHOG000261610.
HOVERGENHBG057324.
InParanoidQ8CI19.
KOK05450.
OMADCVCRGN.
OrthoDBEOG7VB2FN.
PhylomeDBQ8CI19.
TreeFamTF332130.

Gene expression databases

ArrayExpressQ8CI19.
BgeeQ8CI19.
GenevestigatorQ8CI19.

Family and domain databases

Gene3D2.10.90.10. 1 hit.
2.60.120.290. 1 hit.
InterProIPR000859. CUB_dom.
IPR029034. Cystine-knot_cytokine.
IPR000072. PDGF/VEGF_dom.
[Graphical view]
PfamPF00431. CUB. 1 hit.
PF00341. PDGF. 1 hit.
[Graphical view]
SMARTSM00042. CUB. 1 hit.
SM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMSSF49854. SSF49854. 1 hit.
SSF57501. SSF57501. 1 hit.
PROSITEPS01180. CUB. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDGFC. mouse.
NextBio311464.
PROQ8CI19.
SOURCESearch...

Entry information

Entry namePDGFC_MOUSE
AccessionPrimary (citable) accession number: Q8CI19
Secondary accession number(s): Q99JM4, Q9JHV8, Q9QY71
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 87 of the entry and version 2 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

MGD cross-references

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