Q9D658 (TP4A3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Ptp4a3
Synonyms:	Prl3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cell membrane Endosome Membrane
Disease	Proto-oncogene
Molecular function	Hydrolase Protein phosphatase
PTM	Disulfide bond Lipoprotein Methylation Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 170	170	Protein tyrosine phosphatase type IVA 3		PRO_0000094789
	Propeptide	171 – 173	3	Removed in mature form By similarity		PRO_0000396655
Regions
	Domain	82 – 148	67	Tyrosine-protein phosphatase
Sites
	Active site	72	1	Proton donor By similarity
	Active site	104	1	Phosphocysteine intermediate By similarity
	Binding site	110	1	Substrate By similarity
Amino acid modifications
	Modified residue	170	1	Cysteine methyl ester By similarity
	Lipidation	170	1	S-farnesyl cysteine By similarity
	Disulfide bond	49 ↔ 104		By similarity
Experimental info
	Mutagenesis	72	1	D → A: Loss of enzymatic activity; reduced migration-promoting activity. Ref.2
	Mutagenesis	104	1	C → S: Loss of enzymatic activity; reduced migration-promoting activity. Ref.2
	Sequence conflict	101	1	A → L Ref.1
	Sequence conflict	101	1	A → L Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9D658 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 262718AA2040F126	FASTA	173	19,652
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00387241.
PIR	JC5982.
RefSeq	NP_001159860.1. NM_001166388.1. NP_001159861.1. NM_001166389.1. NP_001159862.1. NM_001166390.1. NP_033001.2. NM_008975.3.
UniGene	Mm.390807.
3D structure databases
ProteinModelPortal	Q9D658.
SMR	Q9D658. Positions 1-169.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000060956.
PTM databases
PhosphoSite	Q9D658.
Proteomic databases
PaxDb	Q9D658.
PRIDE	Q9D658.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000053232; ENSMUSP00000060956; ENSMUSG00000059895. ENSMUST00000163582; ENSMUSP00000131281; ENSMUSG00000059895. ENSMUST00000165541; ENSMUSP00000132097; ENSMUSG00000059895.
GeneID	19245.
KEGG	mmu:19245.
UCSC	uc007wcj.1. mouse.
Organism-specific databases
CTD	11156.
MGI	MGI:1277098. Ptp4a3.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00390000009788.
HOGENOM	HOG000231265.
HOVERGEN	HBG071295.
InParanoid	Q9D658.
KO	K01104.
OMA	KAKFCDD.
OrthoDB	EOG415GFJ.
Gene expression databases
ArrayExpress	Q9D658.
Bgee	Q9D658.
CleanEx	MM_PTP4A3.
Genevestigator	Q9D658.
GermOnline	ENSMUSG00000059895. Mus musculus.
Family and domain databases
InterPro	IPR000387. Tyr/Dual-sp_Pase. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view]
Pfam	PF00102. Y_phosphatase. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. False negative. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	296066.
SOURCE	Search...

Entry information

Entry name

TP4A3_MOUSE

Accession

Primary (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 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program