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Protein

Protein tyrosine phosphatase type IVA 3

Gene

Ptp4a3

Organism
Mus musculus (Mouse)
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. 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.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

Inhibited by sodium orthovanadate and peroxovanadium compounds, and by 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

GO - Biological processi

  • endothelial cell migration Source: MGI
  • Notch signaling pathway Source: MGI
  • positive regulation of vascular permeability Source: MGI
  • regulation of vascular endothelial growth factor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ptp4a3
Synonyms:Prl3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1277098. Ptp4a3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi72 – 721D → A: Loss of enzymatic activity; reduced migration-promoting activity. 1 Publication
Mutagenesisi104 – 1041C → S: Loss of enzymatic activity; reduced migration-promoting activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 170170Protein tyrosine phosphatase type IVA 3PRO_0000094789Add
BLAST
Propeptidei171 – 1733Removed in mature formBy similarityPRO_0000396655

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. Unfarnesylated forms are shifted into the nucleus.

Keywords - PTMi

Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ9D658.
PaxDbiQ9D658.
PRIDEiQ9D658.

PTM databases

PhosphoSiteiQ9D658.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

Down-regulated upon skeletal muscle denervation.1 Publication

Gene expression databases

BgeeiQ9D658.
CleanExiMM_PTP4A3.
ExpressionAtlasiQ9D658. baseline and differential.
GenevisibleiQ9D658. MM.

Interactioni

Subunit structurei

Interacts with tubulin.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000060956.

Structurei

3D structure databases

ProteinModelPortaliQ9D658.
SMRiQ9D658. Positions 1-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiQ9D658.
KOiK18041.
OMAiKAKFCDD.
PhylomeDBiQ9D658.
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.

Q9D658-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARMNRPAPV EVSYRHMRFL ITHNPSNATL STFIEDLKKY GATTVVRVCE
60 70 80 90 100
VTYDKTPLEK DGITVVDWPF DDGAPPPGKV VEDWLSLLKA KFYNDPGSCV
110 120 130 140 150
AVHCVAGLGR APVLVALALI ESGMKYEDAI QFIRQKRRGA INSKQLTYLE
160 170
KYRPKQRLRF KDPHTHKTRC CVM
Length:173
Mass (Da):19,652
Last modified:June 1, 2001 - v1
Checksum:i262718AA2040F126
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti101 – 1011A → L (PubMed:9514946).Curated
Sequence conflicti101 – 1011A → L (PubMed:15161639).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27519.1.
PIRiJC5982.
RefSeqiNP_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_006520640.2.
XP_006520705.1. XM_006520642.1.
UniGeneiMm.390807.

Genome annotation databases

EnsembliENSMUST00000053232; ENSMUSP00000060956; ENSMUSG00000059895.
ENSMUST00000163582; ENSMUSP00000131281; ENSMUSG00000059895.
ENSMUST00000165541; ENSMUSP00000132097; ENSMUSG00000059895.
GeneIDi19245.
KEGGimmu:19245.
UCSCiuc007wcj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27519.1.
PIRiJC5982.
RefSeqiNP_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_006520640.2.
XP_006520705.1. XM_006520642.1.
UniGeneiMm.390807.

3D structure databases

ProteinModelPortaliQ9D658.
SMRiQ9D658. Positions 1-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000060956.

PTM databases

PhosphoSiteiQ9D658.

Proteomic databases

MaxQBiQ9D658.
PaxDbiQ9D658.
PRIDEiQ9D658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053232; ENSMUSP00000060956; ENSMUSG00000059895.
ENSMUST00000163582; ENSMUSP00000131281; ENSMUSG00000059895.
ENSMUST00000165541; ENSMUSP00000132097; ENSMUSG00000059895.
GeneIDi19245.
KEGGimmu:19245.
UCSCiuc007wcj.1. mouse.

Organism-specific databases

CTDi11156.
MGIiMGI:1277098. Ptp4a3.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00390000009788.
HOGENOMiHOG000231265.
HOVERGENiHBG071295.
InParanoidiQ9D658.
KOiK18041.
OMAiKAKFCDD.
PhylomeDBiQ9D658.
TreeFamiTF313384.

Miscellaneous databases

NextBioi296066.
PROiQ9D658.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D658.
CleanExiMM_PTP4A3.
ExpressionAtlasiQ9D658. baseline and differential.
GenevisibleiQ9D658. MM.

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. "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.
    , 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.

Entry informationi

Entry nameiTP4A3_MOUSE
AccessioniPrimary (citable) accession number: Q9D658
Secondary accession number(s): O70275, Q3T9Z5, Q9CTC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 100 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

Complete proteome, Reference proteome

Documents

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