PLPP_HUMAN
ID PLPP_HUMAN Reviewed; 296 AA.
AC Q96GD0; Q9UGY2;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Chronophin {ECO:0000303|PubMed:15580268};
DE EC=3.1.3.16 {ECO:0000269|PubMed:15580268};
DE EC=3.1.3.74 {ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:8132548};
DE AltName: Full=Pyridoxal phosphate phosphatase {ECO:0000303|PubMed:14522954};
DE Short=PLP phosphatase {ECO:0000303|PubMed:14522954};
GN Name=PDXP {ECO:0000312|HGNC:HGNC:30259};
GN Synonyms=CIN {ECO:0000303|PubMed:15580268},
GN PLP {ECO:0000303|PubMed:14522954}, PLPP {ECO:0000303|PubMed:14522954};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CIN), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, HOMODIMERIZATION, COFACTOR, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=14522954; DOI=10.1074/jbc.m309619200;
RA Jang Y.M., Kim D.W., Kang T.-C., Won M.H., Baek N.-I., Moon B.J.,
RA Choi S.Y., Kwon O.-S.;
RT "Human pyridoxal phosphatase. Molecular cloning, functional expression, and
RT tissue distribution.";
RL J. Biol. Chem. 278:50040-50046(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CIN).
RC TISSUE=Eye, Lung, and Placenta;
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 PROTEIN SEQUENCE OF 19-35; 100-119 AND 145-158 (ISOFORM CIN), AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 19-30 AND 145-158 (ISOFORM CIN), FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=8132548; DOI=10.1016/s0021-9258(17)37184-3;
RA Gao G.-J., Fonda M.L.;
RT "Identification of an essential cysteine residue in pyridoxal phosphatase
RT from human erythrocytes.";
RL J. Biol. Chem. 269:8234-8239(1994).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-25, AND TISSUE SPECIFICITY.
RX PubMed=15580268; DOI=10.1038/ncb1201;
RA Gohla A., Birkenfeld J., Bokoch G.M.;
RT "Chronophin, a novel HAD-type serine protein phosphatase, regulates
RT cofilin-dependent actin dynamics.";
RL Nat. Cell Biol. 7:21-29(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ALTERNATIVE SPLICING (ISOFORMS CIN; LONG BGIN AND SHORT BGIN), AND TISSUE
RP SPECIFICITY.
RX PubMed=23223568; DOI=10.1091/mbc.e12-07-0565;
RA Huang T.Y., Michael S., Xu T., Sarkeshik A., Moresco J.J., Yates J.R. III,
RA Masliah E., Bokoch G.M., DerMardirossian C.;
RT "A novel Rac1 GAP splice variant relays poly-Ub accumulation signals to
RT mediate Rac1 inactivation.";
RL Mol. Biol. Cell 24:194-209(2013).
RN [9] {ECO:0007744|PDB:2OYC, ECO:0007744|PDB:2P27, ECO:0007744|PDB:2P69}
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 2-296 IN COMPLEXES WITH PYRODOXAL
RP PHOSPHATE; CALCIUM AND MAGNESIUM IONS.
RX PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
RA Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
RA Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
RA Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
RA Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
RA Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
RT "Structural genomics of protein phosphatases.";
RL J. Struct. Funct. Genomics 8:121-140(2007).
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 (PubMed:14522954, PubMed:8132548). Also functions as a protein serine
CC phosphatase that specifically dephosphorylates 'Ser-3' in proteins of
CC the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and
CC DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton
CC reorganization, being required for normal progress through mitosis and
CC normal cytokinesis. Does not dephosphorylate phosphothreonines in
CC LIMK1. Does not dephosphorylate peptides containing phosphotyrosine
CC (PubMed:15580268). {ECO:0000269|PubMed:14522954,
CC ECO:0000269|PubMed:15580268, ECO:0000269|PubMed:8132548}.
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:0000269|PubMed:14522954};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534;
CC Evidence={ECO:0000305|PubMed:14522954};
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:0000269|PubMed:14522954, ECO:0000269|PubMed:8132548};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25113;
CC Evidence={ECO:0000305|PubMed:14522954};
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:0000269|PubMed:14522954};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25137;
CC Evidence={ECO:0000305|PubMed:14522954};
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:0000269|PubMed:15580268};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000269|PubMed:15580268};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:15580268};
CC Note=Divalent metal ions. Mg(2+) is the most effective.
CC {ECO:0000269|PubMed:14522954, ECO:0000269|PubMed:15580268};
CC -!- ACTIVITY REGULATION: Inhibited by NaF, Zn(2+), Ca(2+), Mn(2+) and EDTA.
CC {ECO:0000269|PubMed:15580268}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 uM for pyridoxal 5'-phosphate (at pH 7.4 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:14522954};
CC KM=43.4 uM for pyridoxine 5'-phosphate (at pH 7.4 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:14522954};
CC KM=80.6 uM for pyridoxamine 5'-phosphate (at pH 7.4 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:14522954};
CC Vmax=1.42 umol/min/mg enzyme with pyridoxal 5'-phosphate as substrate
CC {ECO:0000269|PubMed:14522954};
CC Vmax=1.17 umol/min/mg enzyme with pyridoxine 5'-phosphate as
CC substrate {ECO:0000269|PubMed:14522954};
CC Vmax=0.42 umol/min/mg enzyme with pyridoxamine 5'-phosphate as
CC substrate {ECO:0000269|PubMed:14522954};
CC Note=kcat is 1.52 sec(-1) for the dephosphorylation of pyridoxal 5'-
CC phosphate (at pH 7.4 and 37 degrees Celsius). kcat is 1.25 sec(-1)
CC for the dephosphorylation of pyridoxine 5'-phosphate (at pH 7.4 and
CC 37 degrees Celsius). kcat is 0.45 sec(-1) for the dephosphorylation
CC of pyridoxamine 5'-phosphate (at pH 7.4 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:14522954};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14522954}.
CC -!- INTERACTION:
CC Q96GD0; P29066: Arrb1; Xeno; NbExp=2; IntAct=EBI-4303060, EBI-4303019;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15580268}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15580268}. Cell projection,
CC ruffle membrane {ECO:0000269|PubMed:15580268}; Peripheral membrane
CC protein {ECO:0000269|PubMed:15580268}; Cytoplasmic side
CC {ECO:0000269|PubMed:15580268}. Cell projection, lamellipodium membrane
CC {ECO:0000269|PubMed:15580268}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15580268}; Cytoplasmic side
CC {ECO:0000269|PubMed:15580268}. Cell membrane
CC {ECO:0000269|PubMed:15580268}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15580268}; Cytoplasmic side
CC {ECO:0000269|PubMed:15580268}. 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:0000269|PubMed:15580268}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=CIN {ECO:0000303|PubMed:23223568};
CC IsoId=Q96GD0-1; Sequence=Displayed;
CC Name=Long BGIN {ECO:0000303|PubMed:23223568};
CC IsoId=Q6ZT62-1; Sequence=External;
CC Name=Short BGIN {ECO:0000303|PubMed:23223568};
CC IsoId=Q6ZT62-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level)
CC (PubMed:23223568). Highly expressed in all the regions of central nerve
CC system except the spinal cord. Also expressed at high level in liver
CC and testis. In fetus, it is weakly expressed in all organs except brain
CC (PubMed:14522954, PubMed:15580268). {ECO:0000269|PubMed:14522954,
CC ECO:0000269|PubMed:15580268, ECO:0000269|PubMed:23223568}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AY125047; AAM94358.1; -; mRNA.
DR EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000320; AAH00320.1; -; mRNA.
DR EMBL; BC009756; AAH09756.2; -; mRNA.
DR EMBL; BC064922; AAH64922.1; -; mRNA.
DR CCDS; CCDS13953.1; -. [Q96GD0-1]
DR RefSeq; NP_064711.1; NM_020315.4. [Q96GD0-1]
DR PDB; 2CFR; X-ray; 2.40 A; A=1-296.
DR PDB; 2CFS; X-ray; 2.40 A; A=1-296.
DR PDB; 2CFT; X-ray; 1.80 A; A=1-296.
DR PDB; 2OYC; X-ray; 1.72 A; A=2-296.
DR PDB; 2P27; X-ray; 1.90 A; A=2-296.
DR PDB; 2P69; X-ray; 2.25 A; A=2-296.
DR PDB; 5GYN; X-ray; 2.00 A; A=1-296.
DR PDBsum; 2CFR; -.
DR PDBsum; 2CFS; -.
DR PDBsum; 2CFT; -.
DR PDBsum; 2OYC; -.
DR PDBsum; 2P27; -.
DR PDBsum; 2P69; -.
DR PDBsum; 5GYN; -.
DR AlphaFoldDB; Q96GD0; -.
DR SMR; Q96GD0; -.
DR BioGRID; 121330; 25.
DR IntAct; Q96GD0; 5.
DR MINT; Q96GD0; -.
DR STRING; 9606.ENSP00000215904; -.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB00165; Pyridoxine.
DR DrugCentral; Q96GD0; -.
DR DEPOD; PDXP; -.
DR iPTMnet; Q96GD0; -.
DR PhosphoSitePlus; Q96GD0; -.
DR BioMuta; PDXP; -.
DR DMDM; 44888310; -.
DR REPRODUCTION-2DPAGE; IPI00025340; -.
DR UCD-2DPAGE; Q96GD0; -.
DR EPD; Q96GD0; -.
DR jPOST; Q96GD0; -.
DR MassIVE; Q96GD0; -.
DR MaxQB; Q96GD0; -.
DR PaxDb; Q96GD0; -.
DR PeptideAtlas; Q96GD0; -.
DR PRIDE; Q96GD0; -.
DR ProteomicsDB; 76616; -.
DR Antibodypedia; 34919; 109 antibodies from 27 providers.
DR DNASU; 57026; -.
DR Ensembl; ENST00000215904.7; ENSP00000215904.6; ENSG00000241360.2. [Q96GD0-1]
DR GeneID; 57026; -.
DR KEGG; hsa:57026; -.
DR MANE-Select; ENST00000215904.7; ENSP00000215904.6; NM_020315.5; NP_064711.1.
DR UCSC; uc003atm.2; human. [Q96GD0-1]
DR CTD; 57026; -.
DR DisGeNET; 57026; -.
DR GeneCards; PDXP; -.
DR HGNC; HGNC:30259; PDXP.
DR HPA; ENSG00000241360; Tissue enhanced (brain, choroid plexus).
DR MIM; 609246; gene.
DR neXtProt; NX_Q96GD0; -.
DR OpenTargets; ENSG00000241360; -.
DR PharmGKB; PA134882132; -.
DR VEuPathDB; HostDB:ENSG00000241360; -.
DR eggNOG; KOG2882; Eukaryota.
DR GeneTree; ENSGT00940000162045; -.
DR HOGENOM; CLU_043473_0_1_1; -.
DR InParanoid; Q96GD0; -.
DR OMA; MDGVLIH; -.
DR PhylomeDB; Q96GD0; -.
DR TreeFam; TF314344; -.
DR BRENDA; 3.1.3.74; 2681.
DR PathwayCommons; Q96GD0; -.
DR SABIO-RK; Q96GD0; -.
DR SignaLink; Q96GD0; -.
DR SIGNOR; Q96GD0; -.
DR BioGRID-ORCS; 57026; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; PDXP; human.
DR EvolutionaryTrace; Q96GD0; -.
DR GenomeRNAi; 57026; -.
DR Pharos; Q96GD0; Tbio.
DR PRO; PR:Q96GD0; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q96GD0; protein.
DR Bgee; ENSG00000241360; Expressed in right frontal lobe and 95 other tissues.
DR ExpressionAtlas; Q96GD0; baseline and differential.
DR Genevisible; Q96GD0; HS.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA: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:0031072; F:heat shock protein binding; IDA:MGI.
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; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; IDA:UniProtKB.
DR GO; GO:0031247; P:actin rod assembly; IDA:MGI.
DR GO; GO:0071318; P:cellular response to ATP; IDA:MGI.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0032361; P:pyridoxal phosphate catabolic process; IDA:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP: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 3D-structure; Alternative initiation; Alternative splicing; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Hydrolase; Magnesium; Membrane; Metal-binding; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..296
FT /note="Chronophin"
FT /id="PRO_0000068837"
FT ACT_SITE 25
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:15580268,
FT ECO:0000269|PubMed:18058037, ECO:0007744|PDB:2P27"
FT ACT_SITE 27
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15580268,
FT ECO:0000305|PubMed:18058037, ECO:0007744|PDB:2P27"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18058037,
FT ECO:0007744|PDB:2P27"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18058037,
FT ECO:0007744|PDB:2P27"
FT BINDING 58..60
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18058037,
FT ECO:0007744|PDB:2P27"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18058037,
FT ECO:0007744|PDB:2P27"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18058037,
FT ECO:0007744|PDB:2P27"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18058037,
FT ECO:0007744|PDB:2P27"
FT MUTAGEN 25
FT /note="D->N: Abolishes protein phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15580268"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:2OYC"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:2OYC"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2OYC"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:2OYC"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:2OYC"
SQ SEQUENCE 296 AA; 31698 MW; 33466C35A76B458C CRC64;
MARCERLRGA ALRDVLGRAQ GVLFDCDGVL WNGERAVPGA PELLERLARA GKAALFVSNN
SRRARPELAL RFARLGFGGL RAEQLFSSAL CAARLLRQRL PGPPDAPGAV FVLGGEGLRA
ELRAAGLRLA GDPSAGDGAA PRVRAVLVGY DEHFSFAKLR EACAHLRDPE CLLVATDRDP
WHPLSDGSRT PGTGSLAAAV ETASGRQALV VGKPSPYMFE CITENFSIDP ARTLMVGDRL
ETDILFGHRC GMTTVLTLTG VSRLEEAQAY LAAGQHDLVP HYYVESIADL TEGLED
