ID Q1JPZ8_DANRE Unreviewed; 327 AA. AC Q1JPZ8; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 02-OCT-2024, entry version 123. DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273}; DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273}; GN Name=ppp1cb {ECO:0000313|EMBL:AAI16540.1, GN ECO:0000313|RefSeq:NP_001004527.2, GN ECO:0000313|ZFIN:ZDB-GENE-030616-609}; GN Synonyms=ik:tdsubc_2f2 {ECO:0000313|RefSeq:NP_001004527.2}, GN si:zc214p16.4 {ECO:0000313|RefSeq:NP_001004527.2}, wu:fa09h01 GN {ECO:0000313|RefSeq:NP_001004527.2}, wu:fa11e06 GN {ECO:0000313|RefSeq:NP_001004527.2}, xx:tdsubc_2f2 GN {ECO:0000313|RefSeq:NP_001004527.2}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI16540.1}; RN [1] {ECO:0000313|RefSeq:NP_001004527.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=16109975; RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R., RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.; RT "The zebrafish gene map defines ancestral vertebrate chromosomes."; RL Genome Res. 15:1307-1314(2005). RN [2] {ECO:0000313|EMBL:AAI16540.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin {ECO:0000313|EMBL:AAI16540.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|RefSeq:NP_001004527.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=18776143; RA Huang H., Ruan H., Aw M.Y., Hussain A., Guo L., Gao C., Qian F., Leung T., RA Song H., Kimelman D., Wen Z., Peng J.; RT "Mypt1-mediated spatial positioning of Bmp2-producing cells is essential RT for liver organogenesis."; RL Development 135:3209-3218(2008). RN [4] {ECO:0000313|RefSeq:NP_001004527.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=19515695; RA Weiser D.C., Row R.H., Kimelman D.; RT "Rho-regulated myosin phosphatase establishes the level of protrusive RT activity required for cell movements during zebrafish gastrulation."; RL Development 136:2375-2384(2009). RN [5] {ECO:0000313|RefSeq:NP_001004527.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=22205629; RA Levi L., Ziv T., Admon A., Levavi-Sivan B., Lubzens E.; RT "Insight into molecular pathways of retinal metabolism, associated with RT vitellogenesis in zebrafish."; RL Am. J. Physiol. Endocrinol. Metab. 302:E626-E644(2012). RN [6] {ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [7] {ECO:0000313|RefSeq:NP_001004527.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=24040418; RA Jayashankar V., Nguyen M.J., Carr B.W., Zheng D.C., Rosales J.B., RA Rosales J.B., Weiser D.C.; RT "Protein phosphatase 1 beta paralogs encode the zebrafish myosin RT phosphatase catalytic subunit."; RL PLoS ONE 8:e75766-e75766(2013). RN [8] {ECO:0000313|RefSeq:NP_001004527.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=26469318; RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M., RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D., RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E., RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M., RA Reith W., Hertzano R.; RT "RFX transcription factors are essential for hearing in mice."; RL Nat. Commun. 6:8549-8549(2015). RN [9] {ECO:0000313|RefSeq:NP_001004527.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=28252024; RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A., RA Choudhary J.S., Emes R.D., Grant S.G.; RT "Evolution of complexity in the zebrafish synapse proteome."; RL Nat. Commun. 8:14613-14613(2017). RN [10] {ECO:0000313|RefSeq:NP_001004527.2} RP IDENTIFICATION. RG RefSeq; RL Submitted (JUN-2024) to UniProtKB. 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:0000256|ARBA:ARBA00001512}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000256|ARBA:ARBA00001482, CC ECO:0000256|RuleBase:RU004273}; CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily. CC {ECO:0000256|ARBA:ARBA00005333}. 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; BC116539; AAI16540.1; -; mRNA. DR RefSeq; NP_001004527.2; NM_001004527.3. DR GeneID; 100003223; -. DR KEGG; dre:100003223; -. DR AGR; ZFIN:ZDB-GENE-030616-609; -. DR CTD; 5500; -. DR ZFIN; ZDB-GENE-030616-609; ppp1cb. DR OrthoDB; 19833at2759; -. DR Proteomes; UP000000437; Chromosome 17. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ZFIN. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central. DR GO; GO:0060028; P:convergent extension involved in axis elongation; IMP:ZFIN. DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW. DR GO; GO:0001889; P:liver development; IMP:ZFIN. DR GO; GO:0042752; P:regulation of circadian rhythm; IBA:GO_Central. DR CDD; cd07414; MPP_PP1_PPKL; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR050341; PP1_catalytic_subunit. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR InterPro; IPR031675; STPPase_N. DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF449; SERINE_THREONINE-PROTEIN PHOSPHATASE; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF16891; STPPase_N; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306}; KW Cell division {ECO:0000256|ARBA:ARBA00022618}; KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273}; KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q1JPZ8}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}. FT DOMAIN 120..125 FT /note="Serine/threonine specific protein phosphatases" FT /evidence="ECO:0000259|PROSITE:PS00125" FT REGION 305..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 327 AA; 37142 MW; 334480C886E5A195 CRC64; MAEGELNVDS LISRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANNLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIIDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDESLMC SFQILKPSEK KAKYQYSGVN SGRPVTPPRT AQAPKKR //