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 04-NOV-2026, entry version 192. 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}, PLP GN {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 IN COMPLEXES WITH PYRODOXAL PHOSPHATE; CALCIUM AND RP 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=pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate; 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=pyridoxine 5'-phosphate + H2O = pyridoxine + phosphate; 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=pyridoxamine + phosphate = pyridoxamine 5'-phosphate + H2O; 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=O-phospho-L-seryl-[protein] + H2O = 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 CC 5'-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}. 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; 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_020315.5. [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 PDB; 8S8A; X-ray; 1.50 A; A=1-296. DR PDB; 9EM1; X-ray; 1.50 A; A=1-296. DR AlphaFoldDB; Q96GD0; -. DR SMR; Q96GD0; -. DR BioGRID; 121330; 32. DR FunCoup; Q96GD0; 220. DR IntAct; Q96GD0; 21. 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 SwissPalm; Q96GD0; -. DR BioMuta; PDXP; -. DR DMDM; 44888310; -. DR REPRODUCTION-2DPAGE; IPI00025340; -. DR jPOST; Q96GD0; -. DR MassIVE; Q96GD0; -. DR PaxDb; 9606-ENSP00000215904; -. DR PeptideAtlas; Q96GD0; -. DR ProteomicsDB; 76616; -. DR Pumba; Q96GD0; -. DR Antibodypedia; 34919; 137 antibodies from 27 providers. DR DNASU; 57026; -. DR Ensembl; ENST00000215904.7; ENSP00000215904.6; ENSG00000241360.2. 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 AGR; HGNC:30259; -. DR ClinPGx; PA134882132; -. DR CTD; 57026; -. DR DisGeNET; 57026; -. DR GeneCards; PDXP; -. DR HGNC; HGNC:30259; PDXP. DR HPA; ENSG00000241360; Group enriched (brain, liver). DR MIM; 609246; gene. DR OpenTargets; ENSG00000241360; -. DR VEuPathDB; HostDB:ENSG00000241360; -. DR eggNOG; KOG2882; Eukaryota. DR GeneTree; ENSGT00940000162045; -. DR HOGENOM; CLU_043473_0_1_1; -. DR InParanoid; Q96GD0; -. DR OMA; AACHAWW; -. DR OrthoDB; 413953at2759; -. DR PAN-GO; Q96GD0; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q96GD0; -. DR BRENDA; 3.1.3.74; 2681. DR PathwayCommons; Q96GD0; -. DR SABIO-RK; Q96GD0; -. DR SignaLink; Q96GD0; -. DR SIGNOR; Q96GD0; -. DR Agora; ENSG00000241360; -. DR BioGRID-ORCS; 57026; 10 hits in 1172 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 97 other cell types or tissues. DR ExpressionAtlas; Q96GD0; baseline and differential. 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:0031072; F:heat shock protein binding; IDA:MGI. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; EXP:UniProtKB. 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 5'-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 CDD; cd07510; HAD_Pase_UmpH-like; 1. DR FunFam; 3.40.50.1000:FF:000140; Pyridoxal phosphate phosphatase; 1. DR FunFam; 3.40.50.1000:FF:000163; Pyridoxal phosphate phosphatase; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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 NCBIfam; TIGR01460; HAD-SF-IIA; 1. DR NCBIfam; TIGR01452; PGP_euk; 1. DR PANTHER; PTHR19288; 4-NITROPHENYLPHOSPHATASE-RELATED; 1. DR PANTHER; PTHR19288:SF94; CHRONOPHIN; 1. DR Pfam; PF13344; Hydrolase_6; 1. DR Pfam; PF13242; Hydrolase_like; 1. DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1. DR SFLD; SFLDG01139; C2.A:_Pyridoxal_Phosphate_Phos; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SUPFAM; SSF56784; HAD-like; 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; Proteomics identification; KW Pyridoxal phosphate; 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:8S8A" FT STRAND 20..24 FT /evidence="ECO:0007829|PDB:8S8A" FT TURN 28..30 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 40..49 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 53..58 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 65..74 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 88..99 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:2OYC" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 116..124 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 156..166 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 171..176 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 189..191 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 193..204 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 216..223 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:9EM1" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 233..238 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 245..250 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 253..261 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 264..272 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 276..278 FT /evidence="ECO:0007829|PDB:8S8A" FT STRAND 281..286 FT /evidence="ECO:0007829|PDB:8S8A" FT HELIX 287..293 FT /evidence="ECO:0007829|PDB:8S8A" 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 //