Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein tyrosine phosphatase type IVA 1

Gene

Ptp4a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

Inhibited by sodium orthovanadate and pentamidine.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei72 – 721Proton donorBy similarity
Active sitei104 – 1041Phosphocysteine intermediateBy similarity
Binding sitei110 – 1101SubstrateBy similarity

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: RGD

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. multicellular organismal development Source: UniProtKB-KW
  3. peptidyl-tyrosine dephosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
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 namesi
Name:Ptp4a1
Synonyms:Prl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi61970. Ptp4a1.

Subcellular locationi

Cell membrane By similarity. Early endosome By similarity. Endoplasmic reticulum By similarity. Cytoplasm By similarity. Cytoplasmcytoskeletonspindle By similarity
Note: And mitotic spindle.By similarity

GO - Cellular componenti

  1. early endosome Source: UniProtKB-SubCell
  2. endoplasmic reticulum Source: UniProtKB-SubCell
  3. nucleus Source: RGD
  4. plasma membrane Source: UniProtKB-SubCell
  5. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi104 – 1041C → S: Abolishes enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Protein tyrosine phosphatase type IVA 1PRO_0000094784Add
BLAST
Propeptidei171 – 1733Removed in mature formBy similarityPRO_0000396730

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 104By similarity
Modified residuei170 – 1701Cysteine methyl esterBy similarity
Lipidationi170 – 1701S-farnesyl cysteineBy similarity

Post-translational modificationi

Farnesylated. Farnesylation is required for membrane targeting (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

PRIDEiQ78EG7.

Expressioni

Tissue specificityi

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).3 Publications

Developmental stagei

Expressed in fetal brain. Up-regulated during oligodendroglial differentiation. Expressed in the developing intestine, esophagus, liver, kidney and lung (at protein level).3 Publications

Inductioni

By hepatectomy, mitogens, and ischemia-reperfusion.1 Publication

Gene expression databases

GenevestigatoriQ78EG7.

Interactioni

Subunit structurei

Homotrimer. Interacts with ATF5 and tubulin (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016237.

Structurei

Secondary structure

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Beta strandi18 – 214Combined sources
Turni27 – 293Combined sources
Helixi30 – 3910Combined sources
Beta strandi42 – 476Combined sources
Helixi56 – 605Combined sources
Beta strandi64 – 674Combined sources
Beta strandi72 – 743Combined sources
Helixi78 – 9417Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi105 – 1084Combined sources
Turni109 – 1113Combined sources
Helixi112 – 12110Combined sources
Helixi126 – 1349Combined sources
Beta strandi137 – 1393Combined sources
Helixi143 – 1519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X24X-ray3.20A/B1-160[»]
1ZCKX-ray1.90A/B/C7-160[»]
1ZCLX-ray2.90A/B1-160[»]
3RZ2X-ray2.80A/B1-169[»]
ProteinModelPortaliQ78EG7.
SMRiQ78EG7. Positions 9-160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ78EG7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 14867Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 13236Interaction with ATF5By similarityAdd
BLAST
Regioni105 – 1106Phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG265664.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiQ78EG7.
KOiK18041.
OMAiNGHRNTC.
OrthoDBiEOG7C8GJD.
PhylomeDBiQ78EG7.
TreeFamiTF313384.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q78EG7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARMNRPAPV EVTYKNMRFL ITHNPTNATL NKFIEELKKY GVTTIVRVCE
60 70 80 90 100
ATYDTTLVEK EGIHVLDWPF DDGAPPSNQI VDDWLSLVKI KFREEPGCCI
110 120 130 140 150
AVHCVAGLGR APVLVALALI EGGMKYEDAV QFIRQKRRGA FNSKQLLYLE
160 170
KYRPKMRLRF KDSNGHRNNC CIQ
Length:173
Mass (Da):19,815
Last modified:July 5, 2004 - v1
Checksum:i702008013D3F3835
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti170 – 1701C → W in AAL38661. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27843 mRNA. Translation: AAA41935.1.
AY062269 mRNA. Translation: AAL38661.1.
BC081772 mRNA. Translation: AAH81772.1.
BC097307 mRNA. Translation: AAH97307.1.
RefSeqiNP_113767.1. NM_031579.2.
XP_002727244.1. XM_002727198.4.
XP_006244732.1. XM_006244670.2.
XP_006244733.1. XM_006244671.2.
XP_008765001.1. XM_008766779.1.
UniGeneiRn.9459.

Genome annotation databases

EnsembliENSRNOT00000016237; ENSRNOP00000016237; ENSRNOG00000011771.
ENSRNOT00000073218; ENSRNOP00000067713; ENSRNOG00000046370.
GeneIDi100365697.
103693189.
29463.
KEGGirno:100365697.
rno:29463.
UCSCiRGD:61970. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27843 mRNA. Translation: AAA41935.1.
AY062269 mRNA. Translation: AAL38661.1.
BC081772 mRNA. Translation: AAH81772.1.
BC097307 mRNA. Translation: AAH97307.1.
RefSeqiNP_113767.1. NM_031579.2.
XP_002727244.1. XM_002727198.4.
XP_006244732.1. XM_006244670.2.
XP_006244733.1. XM_006244671.2.
XP_008765001.1. XM_008766779.1.
UniGeneiRn.9459.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X24X-ray3.20A/B1-160[»]
1ZCKX-ray1.90A/B/C7-160[»]
1ZCLX-ray2.90A/B1-160[»]
3RZ2X-ray2.80A/B1-169[»]
ProteinModelPortaliQ78EG7.
SMRiQ78EG7. Positions 9-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016237.

Chemistry

BindingDBiQ78EG7.

Proteomic databases

PRIDEiQ78EG7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016237; ENSRNOP00000016237; ENSRNOG00000011771.
ENSRNOT00000073218; ENSRNOP00000067713; ENSRNOG00000046370.
GeneIDi100365697.
103693189.
29463.
KEGGirno:100365697.
rno:29463.
UCSCiRGD:61970. rat.

Organism-specific databases

CTDi7803.
RGDi61970. Ptp4a1.

Phylogenomic databases

eggNOGiNOG265664.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiQ78EG7.
KOiK18041.
OMAiNGHRNTC.
OrthoDBiEOG7C8GJD.
PhylomeDBiQ78EG7.
TreeFamiTF313384.

Miscellaneous databases

EvolutionaryTraceiQ78EG7.
NextBioi609264.
PROiQ78EG7.

Gene expression databases

GenevestigatoriQ78EG7.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiTP4A1_RAT
AccessioniPrimary (citable) accession number: Q78EG7
Secondary accession number(s): Q4QRA5, Q8VH48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2004
Last modified: January 7, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.