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Q9D658 (TP4A3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. 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 3

EC=3.1.3.48
Alternative name(s):
Protein-tyrosine phosphatase 4a3
Protein-tyrosine phosphatase of regenerating liver 3
Short name=PRL-3
Gene names
Name:Ptp4a3
Synonyms:Prl3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. May be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II. Ref.2

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Inhibited by sodium orthovanadate and peroxovanadium compounds, and by pentamidine. Ref.2

Subunit structure

Interacts with tubulin By similarity.

Subcellular location

Cell membrane. Early endosome Ref.2 Ref.5.

Tissue specificity

Present in the small intestine, where it is located in the differentiated epithelial cells of the villus but not in the proliferating crypt cells (at protein level). Expressed in heart and skeletal muscle, and at lower levels in lung, spleen and testis. Ref.1 Ref.2

Induction

Down-regulated upon skeletal muscle denervation. Ref.2 Ref.6

Post-translational modification

Farnesylated. Farnesylation is required for membrane targeting. Unfarnesylated forms are shifted into the nucleus.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Membrane
   DiseaseProto-oncogene
   Molecular functionHydrolase
Protein phosphatase
   PTMDisulfide bond
Lipoprotein
Methylation
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentearly endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 170170Protein tyrosine phosphatase type IVA 3
PRO_0000094789
Propeptide171 – 1733Removed in mature form By similarity
PRO_0000396655

Regions

Domain82 – 14867Tyrosine-protein phosphatase

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

Mutagenesis721D → A: Loss of enzymatic activity; reduced migration-promoting activity. Ref.2
Mutagenesis1041C → S: Loss of enzymatic activity; reduced migration-promoting activity. Ref.2
Sequence conflict1011A → L Ref.1
Sequence conflict1011A → L Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9D658 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 262718AA2040F126

FASTA17319,652
        10         20         30         40         50         60 
MARMNRPAPV EVSYRHMRFL ITHNPSNATL STFIEDLKKY GATTVVRVCE VTYDKTPLEK 

        70         80         90        100        110        120 
DGITVVDWPF DDGAPPPGKV VEDWLSLLKA KFYNDPGSCV AVHCVAGLGR APVLVALALI 

       130        140        150        160        170 
ESGMKYEDAI QFIRQKRRGA INSKQLTYLE KYRPKQRLRF KDPHTHKTRC CVM 

« Hide

References

« Hide 'large scale' references
[1]"Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1."
Zeng Q., Hong W., Tan Y.H.
Biochem. Biophys. Res. Commun. 244:421-427(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Phosphatase of regenerating liver-3 promotes motility and metastasis of mouse melanoma cells."
Wu X., Zeng H., Zhang X., Zhao Y., Sha H., Ge X., Zhang M., Gao X., Xu Q.
Am. J. Pathol. 164:2039-2054(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF ASP-72 AND CYS-104, FUNCTION.
Strain: C57BL/6.
Tissue: Heart.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Embryo, Skin and Spleen.
[4]"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].
Strain: C57BL/6.
Tissue: Brain and Eye.
[5]"Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome."
Zeng Q., Si X., Horstmann H., Xu Y., Hong W., Pallen C.J.
J. Biol. Chem. 275:21444-21452(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-170, SUBCELLULAR LOCATION.
[6]"Denervation-induced alterations in gene expression in mouse skeletal muscle."
Magnusson C., Svensson A., Christerson U., Taagerud S.
Eur. J. Neurosci. 21:577-580(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035645 mRNA. Translation: AAC15875.1.
AK003954 mRNA. Translation: BAB23091.1.
AK014601 mRNA. Translation: BAB29456.1.
AK143702 mRNA. Translation: BAE25506.1.
AK172192 mRNA. Translation: BAE42875.1.
BC027445 mRNA. Translation: AAH27445.1.
BC066043 mRNA. Translation: AAH66043.1.
PIRJC5982.
RefSeqNP_001159860.1. NM_001166388.1.
NP_001159861.1. NM_001166389.1.
NP_001159862.1. NM_001166390.1.
NP_033001.2. NM_008975.3.
XP_006520703.1. XM_006520640.1.
XP_006520704.1. XM_006520641.1.
XP_006520705.1. XM_006520642.1.
UniGeneMm.390807.

3D structure databases

ProteinModelPortalQ9D658.
SMRQ9D658. Positions 1-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000060956.

PTM databases

PhosphoSiteQ9D658.

Proteomic databases

PaxDbQ9D658.
PRIDEQ9D658.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053232; ENSMUSP00000060956; ENSMUSG00000059895.
ENSMUST00000163582; ENSMUSP00000131281; ENSMUSG00000059895.
ENSMUST00000165541; ENSMUSP00000132097; ENSMUSG00000059895.
GeneID19245.
KEGGmmu:19245.
UCSCuc007wcj.1. mouse.

Organism-specific databases

CTD11156.
MGIMGI:1277098. Ptp4a3.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00390000009788.
HOGENOMHOG000231265.
HOVERGENHBG071295.
InParanoidQ9D658.
KOK18041.
OMAKAKFCDD.
PhylomeDBQ9D658.
TreeFamTF313384.

Gene expression databases

ArrayExpressQ9D658.
BgeeQ9D658.
CleanExMM_PTP4A3.
GenevestigatorQ9D658.

Family and domain databases

InterProIPR000387. Tyr/Dual-sp_Pase.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PROSITEPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio296066.
PROQ9D658.
SOURCESearch...

Entry information

Entry nameTP4A3_MOUSE
AccessionPrimary (citable) accession number: Q9D658
Secondary accession number(s): O70275, Q3T9Z5, Q9CTC8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 93 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot