TP4A2_MOUSE
ID TP4A2_MOUSE Reviewed; 167 AA.
AC O70274; Q3U1K7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein tyrosine phosphatase type IVA 2;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase 4a2;
DE AltName: Full=Protein-tyrosine phosphatase of regenerating liver 2;
DE Short=PRL-2;
DE Flags: Precursor;
GN Name=Ptp4a2; Synonyms=Prl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9514946; DOI=10.1006/bbrc.1998.8291;
RA Zeng Q., Hong W., Tan Y.H.;
RT "Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine
RT phosphatases homologous to PRL-1.";
RL Biochem. Biophys. Res. Commun. 244:421-427(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP ISOPRENYLATION AT CYS-164, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 164-CYS--GLN-167.
RX PubMed=10747914; DOI=10.1074/jbc.m000453200;
RA Zeng Q., Si X., Horstmann H., Xu Y., Hong W., Pallen C.J.;
RT "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1,
RT -2, and -3 with the plasma membrane and the early endosome.";
RL J. Biol. Chem. 275:21444-21452(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protein tyrosine phosphatase which stimulates progression
CC from G1 into S phase during mitosis. Inhibits geranylgeranyl
CC transferase type II activity by blocking the association between
CC RABGGTA and RABGGTB (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC -!- ACTIVITY REGULATION: Inhibited by sodium orthovanadate and pentamidine.
CC {ECO:0000250}.
CC -!- SUBUNIT: In contrast to PTP4A1 and PTP4A3, does not interact with
CC tubulin. Interacts with RABGGTB (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10747914}.
CC Early endosome {ECO:0000269|PubMed:10747914}. Cytoplasm
CC {ECO:0000269|PubMed:10747914}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, and at lower levels
CC in liver, lung, heart, kidney, brain, testis and spleen.
CC {ECO:0000269|PubMed:9514946}.
CC -!- PTM: Farnesylated. Farnesylation is required for membrane targeting and
CC for interaction with RABGGTB (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF035644; AAC15874.1; -; mRNA.
DR EMBL; AK033092; BAC28149.1; -; mRNA.
DR EMBL; AK045093; BAC32217.1; -; mRNA.
DR EMBL; AK155895; BAE33489.1; -; mRNA.
DR EMBL; BC086794; AAH86794.1; -; mRNA.
DR EMBL; BC087551; AAH87551.1; -; mRNA.
DR CCDS; CCDS18704.1; -.
DR PIR; JC5981; JC5981.
DR RefSeq; NP_001158217.1; NM_001164745.1.
DR RefSeq; NP_033000.1; NM_008974.4.
DR RefSeq; XP_017175534.1; XM_017320045.1.
DR PDB; 5K24; X-ray; 3.10 A; A/B=1-163.
DR PDBsum; 5K24; -.
DR AlphaFoldDB; O70274; -.
DR BMRB; O70274; -.
DR SMR; O70274; -.
DR BioGRID; 202474; 1.
DR IntAct; O70274; 1.
DR MINT; O70274; -.
DR STRING; 10090.ENSMUSP00000030578; -.
DR iPTMnet; O70274; -.
DR PhosphoSitePlus; O70274; -.
DR EPD; O70274; -.
DR MaxQB; O70274; -.
DR PaxDb; O70274; -.
DR PeptideAtlas; O70274; -.
DR PRIDE; O70274; -.
DR ProteomicsDB; 258817; -.
DR Antibodypedia; 4406; 214 antibodies from 29 providers.
DR DNASU; 19244; -.
DR Ensembl; ENSMUST00000030578; ENSMUSP00000030578; ENSMUSG00000028788.
DR Ensembl; ENSMUST00000165853; ENSMUSP00000125901; ENSMUSG00000028788.
DR GeneID; 19244; -.
DR KEGG; mmu:19244; -.
DR UCSC; uc008uyf.2; mouse.
DR CTD; 8073; -.
DR MGI; MGI:1277117; Ptp4a2.
DR VEuPathDB; HostDB:ENSMUSG00000028788; -.
DR eggNOG; KOG2836; Eukaryota.
DR GeneTree; ENSGT00940000154383; -.
DR HOGENOM; CLU_099263_2_0_1; -.
DR InParanoid; O70274; -.
DR OMA; IQVHGWT; -.
DR OrthoDB; 1398550at2759; -.
DR PhylomeDB; O70274; -.
DR TreeFam; TF313384; -.
DR Reactome; R-MMU-8873719; RAB geranylgeranylation.
DR BioGRID-ORCS; 19244; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ptp4a2; mouse.
DR PRO; PR:O70274; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O70274; protein.
DR Bgee; ENSMUSG00000028788; Expressed in embryonic post-anal tail and 262 other tissues.
DR Genevisible; O70274; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00102; Y_phosphatase; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Disulfide bond; Endosome;
KW Hydrolase; Lipoprotein; Membrane; Methylation; Prenylation;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..164
FT /note="Protein tyrosine phosphatase type IVA 2"
FT /id="PRO_0000094786"
FT PROPEP 165..167
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396732"
FT DOMAIN 5..158
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 69
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 101
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 102..107
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 164
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 164
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:10747914"
FT DISULFID 46..101
FT /evidence="ECO:0000250"
FT MUTAGEN 164..167
FT /note="Missing: Locates in the nucleus."
FT /evidence="ECO:0000269|PubMed:10747914"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:5K24"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:5K24"
SQ SEQUENCE 167 AA; 19127 MW; E97B88BF87B87943 CRC64;
MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY DKAPVEKEGI
HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH CVAGLGRAPV LVALALIECG
MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR PKMRLRFRDT NGHCCVQ
