Laforin - Rattus norvegicus (Rat)

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Q91XQ2 (EPM2A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 80. 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

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	327 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript level

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.
Tissue specificity	Widely expressed. Ref.1
Post-translational modification	Polyubiquitinated by NHLRC1/malin By similarity. Phosphorylation on Ser-21 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 – 327

›327

Laforin

PRO_0000094840

Regions

Domain

1 – 120

120

CBM20

Domain

239 – 307

Tyrosine-protein phosphatase

Amino acid modifications

Modified residue

Phosphoserine; by AMPK By similarity

Experimental info

Non-terminal residue

Sequences

Sequence

Length

Mass (Da)

Tools

Q91XQ2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 587A27E42C987A3F
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FASTA

327

36,643

        10         20         30         40         50         60 
FGVVDQPAVA GTRLELLLAG SRPELGRWEP RGAVRLRPAG TAAGAAALAL QEPGLWLAEV 

        70         80         90        100        110        120 
ELAPEEEAAD GAEPGRIDTF WYKFLQREPG GELHWEGNGP HHDRCCTYNE NNLVDGVYCL 

       130        140        150        160        170        180 
PVGHWIEATG HTNEMKHTTD FYFNIAGHQA MHYSRILPNI WLGSCPRQLE HVTIKLKHEL 

       190        200        210        220        230        240 
GITAVMNFQT EWDIIQNSSG CNRYPEPMTP DTMMKLYKEE GLAYIWMPTP DMSTEGRVQM 

       250        260        270        280        290        300 
LPQAVCLLHA LLENGHTVYV HCNAGVGRST AAVCGWLHYV IGWSLRKVQY FIMAKRPAVY 

       310        320 
IDEEALAQAQ QDFFQKFGKV HSSICTL

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References

[1]	"Regional and developmental expression of Epm2a gene and its evolutionary conservation." Ganesh S., Agarwala K.L., Amano K., Suzuki T., Delgado-Escueta A.V., Yamakawa K. Biochem. Biophys. Res. Commun. 283:1046-1053(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: Sprague-Dawley. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF347030 mRNA. Translation: AAK60619.1.
IPI	IPI00763456.
UniGene	Rn.121954.
3D structure databases
ProteinModelPortal	Q91XQ2.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000058646.
Proteomic databases
PRIDE	Q91XQ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	71047. Epm2a.
Phylogenomic databases
eggNOG	NOG243912.
HOGENOM	HOG000285975.
HOVERGEN	HBG051493.
InParanoid	Q91XQ2.
OrthoDB	EOG4PZJ72.
Gene expression databases
ArrayExpress	Q91XQ2.
Genevestigator	Q91XQ2.
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_RAT

Accession

Primary (citable) accession number: Q91XQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	December 1, 2001
Last modified:	April 3, 2013
This is version 80 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents