ID A0A0R4IYF8_DANRE Unreviewed; 382 AA.
AC A0A0R4IYF8; A0A8M2B327;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Protein phosphatase 1A {ECO:0000256|ARBA:ARBA00040766};
DE AltName: Full=Protein phosphatase 2C isoform alpha {ECO:0000256|ARBA:ARBA00041227};
GN Name=ppm1aa {ECO:0000313|Ensembl:ENSDARP00000140697,
GN ECO:0000313|RefSeq:XP_005156832.1,
GN ECO:0000313|ZFIN:ZDB-GENE-991102-15};
GN Synonyms=pp2ca2 {ECO:0000313|RefSeq:XP_005156832.1};
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|Ensembl:ENSDARP00000140697};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000140697, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000140697};
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 [2] {ECO:0000313|Ensembl:ENSDARP00000140697}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000140697};
RG Ensembl;
RL Submitted (NOV-2015) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_005156832.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005156832.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC ECO:0000256|RuleBase:RU003465}.
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DR EMBL; BX072537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005156832.1; XM_005156775.4.
DR DNASU; 30704; -.
DR Ensembl; ENSDART00000164590; ENSDARP00000140697; ENSDARG00000032155.
DR Ensembl; ENSDART00000164590.2; ENSDARP00000140697.2; ENSDARG00000032155.12.
DR GeneID; 30704; -.
DR AGR; ZFIN:ZDB-GENE-991102-15; -.
DR CTD; 30704; -.
DR ZFIN; ZDB-GENE-991102-15; ppm1aa.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000000437; Chromosome 13.
DR Bgee; ENSDARG00000032155; Expressed in cardiac ventricle and 25 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0051216; P:cartilage development; IGI:ZFIN.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 1.10.10.430; Phosphatase 2C, C-terminal domain suprefamily; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR012911; PP2C_C.
DR InterPro; IPR036580; PP2C_C_sf.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR47992:SF121; PROTEIN PHOSPHATASE 1A; 1.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF07830; PP2C_C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF81601; Protein serine/threonine phosphatase 2C, C-terminal domain; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0R4IYF8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 23..298
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 382 AA; 41865 MW; CCBCDFE529296133 CRC64;
MGAFLDKPKM EKHNAHGDGN SLRYGLSSMQ GWRVEMEDAH TAVIGLPNSL DLWSFFAVYD
GHAGSQVARY CCEHLLEHIT SNPDFQGGGG GGGPAVEPSV DSVKSGIRTG FLQIDDHMRQ
ISEKKHGGAD RSGSTAVGVM ISPRHIYFIN CGDSRGLLSR GGAVHFFTQD HKPSNPLEKE
RIQNAGGSVM IQRVNGSLAV SRALGDFDYK CVHGKGPTEQ LVSPEPEVCA IERSEAEDEF
IVLACDGIWD VMANEELCDF VRSRLEVTDD LERVCNEIVD TCLYKGSRDN MSVVLVCFVS
APKVSPEAVK REAELDKYLE SRVEEILKRQ GDEGVPDLVH VMRTLASESI PNLPPGGELA
SKRSVIEAVY NKLNPYRNED TT
//
