O70274 (TP4A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein tyrosine phosphatase type IVA 2
EC=3.1.3.48

Alternative name(s):
Protein-tyrosine phosphatase 4a2
Protein-tyrosine phosphatase of regenerating liver 2
Short name=PRL-2

Gene names

Name:	Ptp4a2
Synonyms:	Prl2

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	167 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. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB By similarity.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Enzyme regulation	Inhibited by sodium orthovanadate and pentamidine By similarity.
Subunit structure	In contrast to PTP4A1 and PTP4A3, does not interact with tubulin. Interacts with RABGGTB By similarity.
Subcellular location	Cell membrane. Early endosome. Cytoplasm Ref.4.
Tissue specificity	Expressed in skeletal muscle, and at lower levels in liver, lung, heart, kidney, brain, testis and spleen. Ref.1
Post-translational modification	Farnesylated. Farnesylation is required for membrane targeting and for interaction with RABGGTB By similarity.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Endosome Membrane
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 – 164	164	Protein tyrosine phosphatase type IVA 2		PRO_0000094786
	Propeptide	165 – 167	3	Removed in mature form Probable		PRO_0000396732
Regions
	Domain	79 – 145	67	Tyrosine-protein phosphatase
	Region	102 – 107	6	Phosphate binding By similarity
Sites
	Active site	69	1	Proton donor By similarity
	Active site	101	1	Phosphocysteine intermediate By similarity
	Binding site	107	1	Substrate By similarity
Amino acid modifications
	Modified residue	164	1	Cysteine methyl ester Probable
	Lipidation	164	1	S-farnesyl cysteine Ref.4
	Disulfide bond	46 ↔ 101		By similarity
Experimental info
	Mutagenesis	164 – 167	4	Missing: Locates in the nucleus. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O70274 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: E97B88BF87B87943	FASTA	167	19,127
	10 20 30 40 50 60 MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY DKAPVEKEGI 70 80 90 100 110 120 HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH CVAGLGRAPV LVALALIECG 130 140 150 160 MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR PKMRLRFRDT NGHCCVQ

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]	"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. Tissue: Testis.
[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]. Strain: C57BL/6. Tissue: Brain and Embryo.
[4]	"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-164, SUBCELLULAR LOCATION, MUTAGENESIS OF 164-CYS--GLN-167.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF035644 mRNA. Translation: AAC15874.1. AK033092 mRNA. Translation: BAC28149.1. AK045093 mRNA. Translation: BAC32217.1. AK155895 mRNA. Translation: BAE33489.1. BC086794 mRNA. Translation: AAH86794.1. BC087551 mRNA. Translation: AAH87551.1.
IPI	IPI00116529.
PIR	JC5981.
RefSeq	NP_001158217.1. NM_001164745.1. NP_033000.1. NM_008974.4.
UniGene	Mm.193688.
3D structure databases
ProteinModelPortal	O70274.
ModBase	Search...
PTM databases
PhosphoSite	O70274.
Proteomic databases
PaxDb	O70274.
PRIDE	O70274.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030578; ENSMUSP00000030578; ENSMUSG00000028788. ENSMUST00000165853; ENSMUSP00000125901; ENSMUSG00000028788.
GeneID	19244.
KEGG	mmu:19244.
Organism-specific databases
CTD	8073.
MGI	MGI:1277117. Ptp4a2.
Phylogenomic databases
eggNOG	NOG316886.
GeneTree	ENSGT00390000009788.
HOGENOM	HOG000231265.
HOVERGEN	HBG071295.
InParanoid	O70274.
KO	K01104.
OMA	LANMNRP.
OrthoDB	EOG4ZCT5N.
Gene expression databases
ArrayExpress	O70274.
Bgee	O70274.
CleanEx	MM_PTP4A2.
Genevestigator	O70274.
GermOnline	ENSMUSG00000028788. 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
BindingDB	O70274.
ChiTaRS	PTP4A2. mouse.
NextBio	296062.
SOURCE	Search...

Entry information

Entry name

TP4A2_MOUSE

Accession

Primary (citable) accession number: O70274
Secondary accession number(s): Q3U1K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program