Protein tyrosine phosphatase type IVA 1 precursor

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Q78EG7 (TP4A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. History...

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

Documents (2) |

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:
Protein tyrosine phosphatase type IVA 1
EC=3.1.3.48

Alternative name(s):
Protein-tyrosine phosphatase 4a1
Protein-tyrosine phosphatase of regenerating liver 1
Short name=PRL-1

Gene names

Name:	Ptp4a1
Synonyms:	Prl1

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	173 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	Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. May play a role in the development and maintenance of differentiating epithelial tissues By similarity.
Catalytic activity	Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.
Enzyme regulation	Inhibited by sodium orthovanadate and pentamidine. Ref.1
Subunit structure	Homotrimer. Interacts with ATF5 and tubulin By similarity.
Subcellular location	Cell membrane By similarity. Early endosome By similarity. Endoplasmic reticulum By similarity. Cytoplasm By similarity. Cytoplasm › cytoskeleton › spindle By similarity. Note: And mitotic spindle By similarity. Ref.1
Tissue specificity	Brain (neurons and oligodendrocytes), skeletal muscle, regenerating liver, tumor cell lines. Expressed in enterocytes of the small intestine villi and colonic surface, zymogen cells of the stomach, proximal tubule cells of the kidney, bronchiolar epithelium, but not in esophagus and heart (at protein level). Ref.1 Ref.4 Ref.5
Developmental stage	Expressed in fetal brain. Up-regulated during oligodendroglial differentiation. Expressed in the developing intestine, esophagus, liver, kidney and lung (at protein level). Ref.4 Ref.5 Ref.6
Induction	By hepatectomy, mitogens, and ischemia-reperfusion. Ref.1
Post-translational modification	Farnesylated. Farnesylation is required for membrane targeting By similarity.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cell membrane Cytoplasm Cytoskeleton Endoplasmic reticulum Endosome Membrane
Molecular function	Developmental protein Hydrolase Protein phosphatase
PTM	Disulfide bond Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.1. Source: RGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein tyrosine phosphatase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 170

170

Protein tyrosine phosphatase type IVA 1

PRO_0000094784

Propeptide

171 – 173

Removed in mature form By similarity

PRO_0000396730

Regions

Domain

82 – 148

Tyrosine-protein phosphatase

Region

97 – 132

Interaction with ATF5 By similarity

Region

105 – 110

Phosphate binding By similarity

Sites

Active site

Proton donor By similarity

Active site

104

Phosphocysteine intermediate By similarity

Binding site

110

Substrate By similarity

Amino acid modifications

Modified residue

170

Cysteine methyl ester By similarity

Lipidation

170

S-farnesyl cysteine By similarity

Disulfide bond

49 ↔ 104

By similarity

Experimental info

Mutagenesis

104

C → S: Abolishes enzymatic activity. Ref.1

Sequence conflict

170

C → W in AAL38661. Ref.2

Secondary structure

173

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q78EG7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 702008013D3F3835
Show »

FASTA

173

19,815

        10         20         30         40         50         60 
MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE ATYDTTLVEK 

        70         80         90        100        110        120 
EGIHVLDWPF DDGAPPSNQI VDDWLSLVKI KFREEPGCCI AVHCVAGLGR APVLVALALI 

       130        140        150        160        170 
EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE KYRPKMRLRF KDSNGHRNNC CIQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth." Diamond R.H., Cressman D.E., Laz T.M., Abrams C.S., Taub R. Mol. Cell. Biol. 14:3752-3762(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, ENZYME REGULATION, MUTAGENESIS OF CYS-104. Tissue: Regenerating liver.
[2]	Heneberg P., Draber P. Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Basophil.
[3]	"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]. Tissue: Lung and Placenta.
[4]	"PRL-1, a protein tyrosine phosphatase, is expressed in neurons and oligodendrocytes in the brain and induced in the cerebral cortex following transient forebrain ischemia." Takano S., Fukuyama H., Fukumoto M., Kimura J., Xue J.H., Ohashi H., Fujita J. Brain Res. Mol. Brain Res. 40:105-115(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[5]	"PRL-1 PTPase expression is developmentally regulated with tissue-specific patterns in epithelial tissues." Kong W., Swain G.P., Li S., Diamond R.H. Am. J. Physiol. 279:G613-G621(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[6]	"Analysis of oligodendroglial differentiation using cDNA arrays." Scarlato M., Beesley J., Pleasure D. J. Neurosci. Res. 59:430-435(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[7]	"Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion." Sun J.-P., Wang W.-Q., Yang H., Liu S., Liang F., Fedorov A.A., Almo S.C., Zhang Z.-Y. Biochemistry 44:12009-12021(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-160.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L27843 mRNA. Translation: AAA41935.1.
AY062269 mRNA. Translation: AAL38661.1.
BC081772 mRNA. Translation: AAH81772.1.
BC097307 mRNA. Translation: AAH97307.1.

IPI

IPI00471623.

RefSeq

NP_113767.1. NM_031579.2.
XP_002727244.1. XM_002727198.2.

UniGene

Rn.9459.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X24	X-ray	3.20	A/B	1-160	[»]
1ZCK	X-ray	1.90	A/B/C	7-160	[»]
1ZCL	X-ray	2.90	A/B	1-160	[»]
3RZ2	X-ray	2.80	A/B	1-169	[»]

ProteinModelPortal

Q78EG7.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000016237.

Proteomic databases

PRIDE

Q78EG7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000016237; ENSRNOP00000016237; ENSRNOG00000011771.
ENSRNOT00000073218; ENSRNOP00000067713; ENSRNOG00000046370.

GeneID

100365697.
29463.

KEGG

rno:100365697.
rno:29463.

UCSC

RGD:61970. rat.

Organism-specific databases

CTD

7803.

RGD

61970. Ptp4a1.

Phylogenomic databases

eggNOG

NOG265664.

GeneTree

ENSGT00390000009788.

HOGENOM

HOG000231265.

HOVERGEN

HBG071295.

InParanoid

Q78EG7.

K01104.

OMA

CEATYDA.

OrthoDB

EOG4ZCT5N.

Gene expression databases

Genevestigator

Q78EG7.

GermOnline

ENSRNOG00000011771. Rattus norvegicus.

Family and domain databases

InterPro

IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PROSITE

PS00383. TYR_PHOSPHATASE_1. False negative.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q78EG7.

EvolutionaryTrace

Q78EG7.

NextBio

609264.

Entry information

Entry name

TP4A1_RAT

Accession

Primary (citable) accession number: Q78EG7
Secondary accession number(s): Q4QRA5, Q8VH48

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents