NameProtein tyrosine phosphatase type IVA 3
Synonyms
  • 3.1.3.48
  • PRL-3
  • PRL-R
  • PRL3
  • Protein-tyrosine phosphatase 4a3
  • Protein-tyrosine phosphatase of regenerating liver 3
Gene NamePTP4A3
OrganismHuman
Amino acid sequence
>lcl|BSEQ0008991|Protein tyrosine phosphatase type IVA 3
MARMNRPAPVEVSYKHMRFLITHNPTNATLSTFIEDLKKYGATTVVRVCEVTYDKTPLEK
DGITVVDWPFDDGAPPPGKVVEDWLSLVKAKFCEAPGSCVAVHCVAGLGRAPVLVALALI
ESGMKYEDAIQFIRQKRRGAINSKQLTYLEKYRPKQRLRFKDPHTHKTRCCVM
Number of residues173
Molecular Weight19534.69
Theoretical pINot Available
GO Classification
Functions
  • protein tyrosine/serine/threonine phosphatase activity
  • prenylated protein tyrosine phosphatase activity
Processes
  • Notch signaling pathway
  • endothelial cell migration
  • peptidyl-tyrosine dephosphorylation
  • positive regulation of vascular permeability
  • regulation of vascular endothelial growth factor signaling pathway
Components
  • cytoplasm
  • nucleus
  • plasma membrane
  • early endosome
General FunctionProtein tyrosine/serine/threonine phosphatase activity
Specific FunctionProtein 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.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDO75365
UniProtKB Entry NameTP4A3_HUMAN
Cellular LocationCell membrane
Gene sequence
>lcl|BSEQ0013552|Protein tyrosine phosphatase type IVA 3 (PTP4A3)
ATGGCTCGGATGAACCGCCCGGCCCCGGTGGAGGTGAGCTACAAACACATGCGCTTCCTC
ATCACCCACAACCCCACCAACGCCACGCTCAGCACCTTCATTGAGGACCTGAAGAAGTAC
GGGGCTACCACTGTGGTGCGTGTGTGTGAAGTGACCTATGACAAAACGCCGCTGGAGAAG
GATGGCATCACCGTTGTGGACTGGCCGTTTGACGATGGGGCGCCCCCGCCCGGCAAGGTA
GTGGAAGACTGGCTGAGCCTGGTGAAGGCCAAGTTCTGTGAGGCCCCCGGCAGCTGCGTG
GCTGTGCACTGCGTGGCGGGCCTGGGCCGGAAGCGCCGCGGAGCCATCAACAGCAAGCAG
CTCACCTACCTGGAGAAATACCGGCCCAAACAGAGGCTGCGGTTCAAAGACCCACACACG
CACAAGACCCGGTGCTGCGTTATGTAG
GenBank Gene IDNot Available
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:9636
Chromosome Location8
LocusNot Available
References
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  2. Dayton MA, Knobloch TJ: Multiple phosphotyrosine phosphatase mRNAs are expressed in the human lung fibroblast cell line WI-38. Recept Signal Transduct. 1997;7(4):241-56. 9633825
  3. Matter WF, Estridge T, Zhang C, Belagaje R, Stancato L, Dixon J, Johnson B, Bloem L, Pickard T, Donaghue M, Acton S, Jeyaseelan R, Kadambi V, Vlahos CJ: Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling. Biochem Biophys Res Commun. 2001 May 25;283(5):1061-8. 11355880
  4. Saha S, Bardelli A, Buckhaults P, Velculescu VE, Rago C, St Croix B, Romans KE, Choti MA, Lengauer C, Kinzler KW, Vogelstein B: A phosphatase associated with metastasis of colorectal cancer. Science. 2001 Nov 9;294(5545):1343-6. Epub 2001 Oct 11. 11598267
  5. Wang J, Kirby CE, Herbst R: The tyrosine phosphatase PRL-1 localizes to the endoplasmic reticulum and the mitotic spindle and is required for normal mitosis. J Biol Chem. 2002 Nov 29;277(48):46659-68. Epub 2002 Sep 13. 12235145
  6. Pathak MK, Dhawan D, Lindner DJ, Borden EC, Farver C, Yi T: Pentamidine is an inhibitor of PRL phosphatases with anticancer activity. Mol Cancer Ther. 2002 Dec;1(14):1255-64. 12516958
  7. Zeng Q, Dong JM, Guo K, Li J, Tan HX, Koh V, Pallen CJ, Manser E, Hong W: PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. Cancer Res. 2003 Jun 1;63(11):2716-22. 12782572
  8. Kim KA, Song JS, Jee J, Sheen MR, Lee C, Lee TG, Ro S, Cho JM, Lee W, Yamazaki T, Jeon YH, Cheong C: Structure of human PRL-3, the phosphatase associated with cancer metastasis. FEBS Lett. 2004 May 7;565(1-3):181-7. 15135076
  9. Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I: Structural insights into molecular function of the metastasis-associated phosphatase PRL-3. J Biol Chem. 2004 Mar 19;279(12):11882-9. Epub 2004 Jan 1. 14704153