Laforin - Canis familiaris (Dog)

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Q1M199 (EPM2A_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 53. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Laforin
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
Lafora PTPase
Short name=LAFPTPase

Gene names

Name:

EPM2A

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Dual specificity protein phosphatase. May be involved in the control of glycogen metabolism, particularly in monitoring for and preventing the formation of poorly branched glycogen molecules (polyglucosans). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Forms a complex with NHLRC1/malin and HSP70 and this complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS) By similarity.
Catalytic activity	Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate. A phosphoprotein + H₂O = a protein + phosphate.
Subunit structure	Interacts with itself; interacts also with PPP1R3C, HIRIP5 and EPM2AIP1. Binds polyglucosans and glycogen. Interacts with NHLRC1/malin (via the NHL repeats). Forms a complex with NHLRC1/malin and HSP70 By similarity.
Subcellular location	Cytoplasm By similarity. Endoplasmic reticulum By similarity. Note: Under glycogenolytic conditions localizes to the nucleus By similarity.
Post-translational modification	Polyubiquitinated by NHLRC1/malin By similarity. Phosphorylation on Ser-25 by AMPK affects the phosphatase activity of the enzyme and its ability to homodimerize and interact with NHLRC1, PPP1R3C or PRKAA2 By similarity.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Contains 1 CBM20 (carbohydrate binding type-20) domain. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glycogen metabolism
Cellular component	Cytoplasm Endoplasmic reticulum
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycogen metabolic process Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome starch binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 331

331

Laforin

PRO_0000289592

Regions

Domain

1 – 124

124

CBM20

Domain

243 – 311

Tyrosine-protein phosphatase

Amino acid modifications

Modified residue

Phosphoserine; by AMPK By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q1M199 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 788A905A6D82835B
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FASTA

331

36,900

        10         20         30         40         50         60 
MRFRFGVVVP PAGAGAAPEL LVVGSRPELG RWEPRGAVRL RPAGSAAGGG ARALQEPGLW 

        70         80         90        100        110        120 
LGEVELAPGE AARDGAEPAR VDTFWYKFLK REPGGALSWE GNGPHHDRCC TYNENNLVDG 

       130        140        150        160        170        180 
VYCLPIGHWI EATGHTNEMK HTTDFYFNIA GHQAMHYSRI LPNIWLGSCP RQVEHITIKL 

       190        200        210        220        230        240 
KHELGITAVM NFQTEWDIVQ NSSGCNRYPE PMTPDTMIKL YKEEGLVYIW MPTPDMSTEG 

       250        260        270        280        290        300 
RVQMLPQAVC LLHALLENGH TVYVHCNAGV GRSTAAVCGW LQYVMGWNLR KVQYFLMAKR 

       310        320        330 
PAVYIDEDAL ARAEEDFFQK FGKVRSSVCS V

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References

[1]

"Expanded repeat in canine epilepsy."
Lohi H., Young E.J., Fitzmaurice S.N., Rusbridge C., Chan E.M., Vervoort M., Turnbull J., Zhao X.C., Ianzano L., Paterson A.D., Sutter N.B., Ostrander E.A., Andre C., Shelton G.D., Ackerley C.A., Scherer S.W., Minassian B.A.
Science 307:81-81(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY560906 Genomic DNA. Translation: ABE98181.1.
3D structure databases
ProteinModelPortal	Q1M199.
ModBase	Search...
Protein-protein interaction databases
STRING	9615.ENSCAFP00000000457.
Protein family/group databases
CAZy	CBM20. Carbohydrate-Binding Module Family 20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG243912.
HOGENOM	HOG000285975.
HOVERGEN	HBG051493.
InParanoid	Q1M199.
Family and domain databases
Gene3D	2.60.40.10. 1 hit.
InterPro	IPR013784. Carb-bd-like_fold. IPR002044. CBM_fam20. IPR000340. Dual-sp_phosphatase_cat-dom. IPR020422. Dual-sp_phosphatase_subgr_cat. IPR024950. DUSP. IPR013783. Ig-like_fold. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00686. CBM_20. 1 hit. PF00782. DSPc. 1 hit. [Graphical view]
SMART	SM01065. CBM_2. 1 hit. [Graphical view]
SUPFAM	SSF49452. CBD_4. 1 hit.
PROSITE	PS51166. CBM20. 1 hit. PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EPM2A_CANFA

Accession

Primary (citable) accession number: Q1M199

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 30, 2006
Last modified:	April 3, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents