GENTAUR Molecular Products.

 PLPP_RAT                Reviewed;         309 AA.
 Q8VD52;
 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
 10-JAN-2006, sequence version 2.
 20-JUN-2018, entry version 106.
 RecName: Full=Pyridoxal phosphate phosphatase;
          Short=PLP phosphatase;
          EC=3.1.3.3 {ECO:0000250|UniProtKB:Q96GD0};
          EC=3.1.3.74 {ECO:0000250|UniProtKB:Q96GD0};
 AltName: Full=Chronophin;
 AltName: Full=Reg I-binding protein 1;
 Name=Pdxp; Synonyms=Cin, Plp, Plpp, Rbp1;
 Rattus norvegicus (Rat).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
 Muroidea; Muridae; Murinae; Rattus.
 NCBI_TaxID=10116;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=Brown Norway;
 PubMed=15057822; DOI=10.1038/nature02426;
 Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
 Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
 Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
 Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
 Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
 Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
 Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
 Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
 Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
 Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
 Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
 Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
 Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
 Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
 Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
 D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
 Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
 Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
 Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
 Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
 Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
 Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
 Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
 Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
 Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
 Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
 Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
 Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
 Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
 Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
 Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
 Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
 Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
 Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
 Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
 Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
 Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
 Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
 Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
 Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
 Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
 Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
 Collins F.S.;
 "Genome sequence of the Brown Norway rat yields insights into
 mammalian evolution.";
 Nature 428:493-521(2004).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] OF 106-309.
 STRAIN=Wistar; TISSUE=Pancreas;
 Wu H., Zenilman M.E.;
 "Isolation of cDNA clone from rat pancreas cDNA library by two hybrid
 system, clone 13.";
 Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
 [3]
 PROTEIN SEQUENCE OF 129-138; 141-154; 186-202 AND 236-245, AND
 IDENTIFICATION BY MASS SPECTROMETRY.
 STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
 Lubec G., Chen W.-Q.;
 Submitted (APR-2007) to UniProtKB.
 -!- FUNCTION: Protein serine phosphatase that dephosphorylates 'Ser-3'
     in cofilin and probably also dephosphorylates phospho-serine
     residues in DSTN. Regulates cofilin-dependent actin cytoskeleton
     reorganization. Required for normal progress through mitosis and
     normal cytokinesis. Does not dephosphorylate phospho-threonines in
     LIMK1. Does not dephosphorylate peptides containing phospho-
     tyrosine. Pyridoxal phosphate (PLP) phosphatase, which also
     catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP)
     and pyridoxamine 5'-phosphate (PMP), with order of substrate
     preference PLP > PNP > PMP. {ECO:0000250|UniProtKB:Q96GD0}.
 -!- CATALYTIC ACTIVITY: Pyridoxal 5'-phosphate + H(2)O = pyridoxal +
     phosphate. {ECO:0000250|UniProtKB:Q96GD0}.
 -!- CATALYTIC ACTIVITY: O-phospho-L(or D)-serine + H(2)O = L(or D)-
     serine + phosphate. {ECO:0000250|UniProtKB:Q96GD0}.
 -!- COFACTOR:
     Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
       Evidence={ECO:0000250|UniProtKB:Q96GD0};
     Note=Divalent metal ions. Mg(2+) is the most effective.
     {ECO:0000250|UniProtKB:Q96GD0};
 -!- SUBUNIT: Homodimer (By similarity). Interacts with REG1.
     {ECO:0000250|UniProtKB:Q96GD0}.
 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
     {ECO:0000250|UniProtKB:Q96GD0}. Cytoplasm, cytoskeleton
     {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, ruffle membrane
     {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
     {ECO:0000250, ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
     {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, lamellipodium
     membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane
     protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
     {ECO:0000250|UniProtKB:Q96GD0}. Cell membrane
     {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
     {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
     {ECO:0000250|UniProtKB:Q96GD0}. Note=Colocalizes with the actin
     cytoskeleton in membrane ruffles and lamellipodia. Diffusely
     distributed throughout the cytosol during pro-metaphase and
     metaphase. Detected at the dynamic cell poles during telophase.
     Detected at the cleavage furrow and contractile ring during
     cytokinesis. Transiently detected at the plasma membrane in late
     stages of cytokinesis. Detected at the midbody.
     {ECO:0000250|UniProtKB:Q96GD0}.
 -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
     {ECO:0000305}.
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 EMBL; AABR03056024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AF318578; AAL37168.1; -; mRNA.
 UniGene; Rn.222285; -.
 ProteinModelPortal; Q8VD52; -.
 SMR; Q8VD52; -.
 STRING; 10116.ENSRNOP00000064092; -.
 PaxDb; Q8VD52; -.
 PRIDE; Q8VD52; -.
 UCSC; RGD:1586212; rat.
 RGD; 1586212; Pdxp.
 eggNOG; KOG2882; Eukaryota.
 eggNOG; COG0647; LUCA.
 HOGENOM; HOG000068104; -.
 HOVERGEN; HBG049429; -.
 InParanoid; Q8VD52; -.
 PhylomeDB; Q8VD52; -.
 PRO; PR:Q8VD52; -.
 Proteomes; UP000002494; Unplaced.
 GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO; GO:0005829; C:cytosol; ISS:UniProtKB.
 GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
 GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO; GO:0019838; F:growth factor binding; IPI:RGD.
 GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
 GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IBA:GO_Central.
 GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
 GO; GO:0004647; F:phosphoserine phosphatase activity; IEA:UniProtKB-EC.
 GO; GO:0033883; F:pyridoxal phosphatase activity; ISS:UniProtKB.
 GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISS:UniProtKB.
 GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
 GO; GO:0032361; P:pyridoxal phosphate catabolic process; ISS:UniProtKB.
 GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
 GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
 Gene3D; 3.40.50.1000; -; 3.
 InterPro; IPR036412; HAD-like_sf.
 InterPro; IPR006357; HAD-SF_hydro_IIA.
 InterPro; IPR023214; HAD_sf.
 InterPro; IPR006349; PGP_euk.
 Pfam; PF13344; Hydrolase_6; 1.
 PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
 SUPFAM; SSF56784; SSF56784; 1.
 TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
 TIGRFAMs; TIGR01452; PGP_euk; 1.
 1: Evidence at protein level;
 Cell membrane; Cell projection; Complete proteome; Cytoplasm;
 Cytoskeleton; Direct protein sequencing; Hydrolase; Magnesium;
 Membrane; Metal-binding; Pyridoxal phosphate; Reference proteome.
 CHAIN         1    309       Pyridoxal phosphate phosphatase.
                              /FTId=PRO_0000068839.
 REGION       58     62       Substrate binding. {ECO:0000250}.
 ACT_SITE     25     25       Nucleophile. {ECO:0000250}.
 ACT_SITE     27     27       Proton donor. {ECO:0000250}.
 METAL        25     25       Magnesium. {ECO:0000250}.
 METAL        27     27       Magnesium; via carbonyl oxygen.
                              {ECO:0000250}.
 METAL       234    234       Magnesium. {ECO:0000250}.
 BINDING     178    178       Substrate. {ECO:0000250}.
 BINDING     209    209       Substrate. {ECO:0000250}.
 CONFLICT    106    108       APG -> GTR (in Ref. 2). {ECO:0000305}.
 SEQUENCE   309 AA;  33115 MW;  E609DAA5250151C4 CRC64;
 MARCERLRGA ALRDVLGQAQ GVLFDCDGVL WNGERIVPGA PELLQRLAQA GKATLFVSNN
 SRRARPELAL RFARLGFTGL RAEELFSSAV CAARLLRQRL PGPPDAPGAV FVLGGEGLRA
 ELRAAGLRLA GDPGDDPRVR AVLVGYDEHF SFAKLTEACA HLRDPDCLLV ATDRDPWHPL
 TDGSRTPGTG SLAAAVETAS GRQALVVGKP SPYMFQCITE DFSVDPARML MVGDRLETDI
 LFGHRCGMTT VLTLTGVSSL EEAQAYLAAG QHDLVPHYYV ESIADLMEGL GGLSPPPQFP
 DPVDGGYRP

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