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Q78EG7

- TP4A1_RAT

UniProt

Q78EG7 - TP4A1_RAT

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Protein

Protein tyrosine phosphatase type IVA 1

Gene

Ptp4a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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
  4. positive regulation of cell migration Source: Ensembl
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. cytoplasmic side of plasma membrane Source: Ensembl
  2. cytoskeleton Source: UniProtKB-KW
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. endosome Source: UniProtKB-KW
  5. extracellular vesicular exosome Source: Ensembl
  6. nucleus Source: RGD
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.
OMAiDKSIAVH.
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:102547074.
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 .
RefSeqi NP_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.
UniGenei Rn.9459.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q78EG7.
SMRi Q78EG7. Positions 9-160.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000016237.

Chemistry

BindingDBi Q78EG7.

Proteomic databases

PRIDEi Q78EG7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000016237 ; ENSRNOP00000016237 ; ENSRNOG00000011771 .
ENSRNOT00000073218 ; ENSRNOP00000067713 ; ENSRNOG00000046370 .
GeneIDi 100365697.
103693189.
29463.
KEGGi rno:100365697.
rno:102547074.
rno:29463.
UCSCi RGD:61970. rat.

Organism-specific databases

CTDi 7803.
RGDi 61970. Ptp4a1.

Phylogenomic databases

eggNOGi NOG265664.
GeneTreei ENSGT00390000009788.
HOGENOMi HOG000231265.
HOVERGENi HBG071295.
InParanoidi Q78EG7.
KOi K18041.
OMAi DKSIAVH.
OrthoDBi EOG7C8GJD.
PhylomeDBi Q78EG7.
TreeFami TF313384.

Miscellaneous databases

EvolutionaryTracei Q78EG7.
NextBioi 609264.
PROi Q78EG7.

Gene expression databases

Genevestigatori Q78EG7.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 98 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