PLPP_RAT
ID PLPP_RAT Reviewed; 309 AA.
AC Q8VD52;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Chronophin {ECO:0000250|UniProtKB:Q96GD0};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q3ZBF9};
DE EC=3.1.3.74 {ECO:0000250|UniProtKB:Q96GD0};
DE AltName: Full=Pyridoxal phosphate phosphatase {ECO:0000250|UniProtKB:Q96GD0};
DE Short=PLP phosphatase {ECO:0000250|UniProtKB:Q96GD0};
DE AltName: Full=Reg I-binding protein 1 {ECO:0000303|Ref.2};
GN Name=Pdxp {ECO:0000312|RGD:1586212};
GN Synonyms=Cin, Plp, Plpp, Rbp1 {ECO:0000303|Ref.2};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-309.
RC STRAIN=Wistar; TISSUE=Pancreas;
RA Wu H., Zenilman M.E.;
RT "Isolation of cDNA clone from rat pancreas cDNA library by two hybrid
RT system, clone 13.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 129-138; 141-154; 186-202 AND 236-245, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: Functions as a pyridoxal phosphate (PLP) phosphatase, which
CC also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP)
CC and pyridoxamine 5'-phosphate (PMP), with order of substrate preference
CC PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism.
CC Also functions as a protein serine phosphatase that specifically
CC dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor
CC (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-
CC dependent actin cytoskeleton reorganization, being required for normal
CC progress through mitosis and normal cytokinesis. Does not
CC dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate
CC peptides containing phosphotyrosine. {ECO:0000250|UniProtKB:Q96GD0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal;
CC Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxine 5'-phosphate = phosphate + pyridoxine;
CC Xref=Rhea:RHEA:25112, ChEBI:CHEBI:15377, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58589; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25113;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + pyridoxamine = H2O + pyridoxamine 5'-phosphate;
CC Xref=Rhea:RHEA:25135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57761, ChEBI:CHEBI:58451; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25137;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC Note=Divalent metal ions. Mg(2+) is the most effective.
CC {ECO:0000250|UniProtKB:Q96GD0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96GD0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96GD0}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
CC {ECO:0000250, ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, lamellipodium membrane
CC {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GD0}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GD0}. Note=Colocalizes with the actin
CC cytoskeleton in membrane ruffles and lamellipodia. Diffusely
CC distributed throughout the cytosol during pro-metaphase and metaphase.
CC Detected at the dynamic cell poles during telophase. Detected at the
CC cleavage furrow and contractile ring during cytokinesis. Transiently
CC detected at the plasma membrane in late stages of cytokinesis. Detected
CC at the midbody. {ECO:0000250|UniProtKB:Q96GD0}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
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; AABR03056024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF318578; AAL37168.1; -; mRNA.
DR AlphaFoldDB; Q8VD52; -.
DR SMR; Q8VD52; -.
DR STRING; 10116.ENSRNOP00000064092; -.
DR jPOST; Q8VD52; -.
DR PaxDb; Q8VD52; -.
DR PRIDE; Q8VD52; -.
DR UCSC; RGD:1586212; rat.
DR RGD; 1586212; Pdxp.
DR eggNOG; KOG2882; Eukaryota.
DR InParanoid; Q8VD52; -.
DR PhylomeDB; Q8VD52; -.
DR PRO; PR:Q8VD52; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043136; F:glycerol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0019838; F:growth factor binding; IPI:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; ISS:UniProtKB.
DR GO; GO:0031247; P:actin rod assembly; ISO:RGD.
DR GO; GO:0071318; P:cellular response to ATP; ISO:RGD.
DR GO; GO:0016311; P:dephosphorylation; ISO:RGD.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0032361; P:pyridoxal phosphate catabolic process; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006349; PGP_euk.
DR Pfam; PF13344; Hydrolase_6; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR TIGRFAMs; TIGR01452; PGP_euk; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Hydrolase; Magnesium; Membrane; Metal-binding;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..309
FT /note="Chronophin"
FT /id="PRO_0000068839"
FT ACT_SITE 25
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT ACT_SITE 27
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 58..60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT CONFLICT 106..108
FT /note="APG -> GTR (in Ref. 2; AAL37168)"
FT /evidence="ECO:0000305"
SQ 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
