ID   PPM1H_DANRE             Reviewed;         516 AA.
AC   Q05AL2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Protein phosphatase 1H;
DE            EC=3.1.3.16;
GN   Name=ppm1h; ORFNames=zgc:153678;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULR3}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9ULR3}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; BC124421; AAI24422.1; -; mRNA.
DR   RefSeq; NP_001070923.1; NM_001077455.1.
DR   AlphaFoldDB; Q05AL2; -.
DR   SMR; Q05AL2; -.
DR   STRING; 7955.ENSDARP00000087709; -.
DR   PaxDb; 7955-ENSDARP00000087709; -.
DR   GeneID; 768291; -.
DR   KEGG; dre:768291; -.
DR   AGR; ZFIN:ZDB-GENE-061027-190; -.
DR   CTD; 57460; -.
DR   ZFIN; ZDB-GENE-061027-190; ppm1h.
DR   eggNOG; KOG1323; Eukaryota.
DR   InParanoid; Q05AL2; -.
DR   OrthoDB; 1450097at2759; -.
DR   PhylomeDB; Q05AL2; -.
DR   PRO; PR:Q05AL2; -.
DR   Proteomes; UP000000437; Chromosome 25.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004741; F:[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF287; PROTEIN PHOSPHATASE 1H; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT   CHAIN           1..516
FT                   /note="Protein phosphatase 1H"
FT                   /id="PRO_0000286606"
FT   DOMAIN          106..506
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          102..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  56561 MW;  E13BF19741EFA0BD CRC64;
     MMTRVRSAVS SIIGGIMASG TGAHDSHPDL PLRFPYSRPD FLALSPDEVE CSADHISRPI
     LILKEMKLPW ATGYAEVINA GKSALNEDQA CCEVVELRKR PADPSSVSYT PSRRRSSLPS
     GDVLDTIHNP EVKELDFHYW ALFDGHGGSG AAVFAAKFLH LHIEEQLQEV LEILQDPGLQ
     PPTCLGEESP NPQLHASASG SQRGLSRAAS LRGAAGAPGS PNTMAPRFFM EKKIKQESLV
     VGAIENAFKE MDAHIARERC AYSISGGCTA LAVMFLLGKL YVANAGDSRA LIVRAGELIT
     MSSSFTPESE RQRLQFLAHL QPSLLGSDFT HLEFPRRVTK REIGKRMLYR DFTMNGWAYK
     TVQEEDLKFP LIYGEGKKAR VLATIGITRG LGDHDLKVHD SDIAIKPFLS CSPEVQVYNL
     CQFEHGADDV LILATDGLWD VLSNQEVADA VSGFLGNCDP DDQHRYTMAA QDLVMKARGI
     LKDRGWRIAG DRLGSGDDIS VFIIPLMYGT QQPQPS
//