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Q78EG7 (TP4A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. 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:
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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Cytoplasmcytoskeletonspindle 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 170170Protein tyrosine phosphatase type IVA 1
PRO_0000094784
Propeptide171 – 1733Removed in mature form By similarity
PRO_0000396730

Regions

Domain82 – 14867Tyrosine-protein phosphatase
Region97 – 13236Interaction with ATF5 By similarity
Region105 – 1106Phosphate binding By similarity

Sites

Active site721Proton donor By similarity
Active site1041Phosphocysteine intermediate By similarity
Binding site1101Substrate By similarity

Amino acid modifications

Modified residue1701Cysteine methyl ester By similarity
Lipidation1701S-farnesyl cysteine By similarity
Disulfide bond49 ↔ 104 By similarity

Experimental info

Mutagenesis1041C → S: Abolishes enzymatic activity. Ref.1
Sequence conflict1701C → W in AAL38661. Ref.2

Secondary structure

.............................. 173
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q78EG7 [UniParc].

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

FASTA17319,815
        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' 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.
RefSeqNP_113767.1. NM_031579.2.
XP_002727244.1. XM_002727198.3.
XP_006244732.1. XM_006244670.1.
XP_006244733.1. XM_006244671.1.
XP_006244747.1. XM_006244685.1.
UniGeneRn.9459.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X24X-ray3.20A/B1-160[»]
1ZCKX-ray1.90A/B/C7-160[»]
1ZCLX-ray2.90A/B1-160[»]
3RZ2X-ray2.80A/B1-169[»]
ProteinModelPortalQ78EG7.
SMRQ78EG7. Positions 9-160.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000016237.

Chemistry

BindingDBQ78EG7.

Proteomic databases

PRIDEQ78EG7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000016237; ENSRNOP00000016237; ENSRNOG00000011771.
ENSRNOT00000073218; ENSRNOP00000067713; ENSRNOG00000046370.
GeneID100365697.
102547074.
29463.
KEGGrno:100365697.
rno:102547074.
rno:29463.
UCSCRGD:61970. rat.

Organism-specific databases

CTD7803.
RGD61970. Ptp4a1.

Phylogenomic databases

eggNOGNOG265664.
GeneTreeENSGT00390000009788.
HOGENOMHOG000231265.
HOVERGENHBG071295.
InParanoidQ78EG7.
KOK18041.
OMADKSIAVH.
OrthoDBEOG7C8GJD.
PhylomeDBQ78EG7.
TreeFamTF313384.

Gene expression databases

GenevestigatorQ78EG7.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ78EG7.
NextBio609264.
PROQ78EG7.

Entry information

Entry nameTP4A1_RAT
AccessionPrimary (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: June 11, 2014
This is version 95 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references