PPM1H_DANRE
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 03-AUG-2022, entry version 81.
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; Q05AL2; -.
DR GeneID; 768291; -.
DR KEGG; dre:768291; -.
DR CTD; 57460; -.
DR ZFIN; ZDB-GENE-061027-190; ppm1h.
DR eggNOG; KOG1323; Eukaryota.
DR InParanoid; Q05AL2; -.
DR OrthoDB; 601888at2759; -.
DR PhylomeDB; Q05AL2; -.
DR PRO; PR:Q05AL2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 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