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Pyridoxal phosphate phosphatase (PLP phosphatase) (EC 3.1.3.3) (EC 3.1.3.74) (Chronophin) (Reg I-binding protein 1)

 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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