PPM1K_BOVIN
ID PPM1K_BOVIN Reviewed; 372 AA.
AC Q2PC20; Q17R15; Q2PC19;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein phosphatase 1K, mitochondrial;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2C isoform kappa;
DE Short=PP2C-kappa;
DE Flags: Precursor;
GN Name=PPM1K;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Holstein;
RA Seroussi E.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulates the mitochondrial permeability transition pore and
CC is essential for cellular survival and development. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2PC20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2PC20-2; Sequence=VSP_023155;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AJ871967; CAI44748.1; -; mRNA.
DR EMBL; AJ871968; CAI44749.1; -; mRNA.
DR EMBL; BC118079; AAI18080.1; -; mRNA.
DR RefSeq; NP_001039939.1; NM_001046474.2.
DR RefSeq; XP_005207855.1; XM_005207798.3. [Q2PC20-1]
DR AlphaFoldDB; Q2PC20; -.
DR SMR; Q2PC20; -.
DR STRING; 9913.ENSBTAP00000007563; -.
DR PaxDb; Q2PC20; -.
DR PRIDE; Q2PC20; -.
DR Ensembl; ENSBTAT00000007563; ENSBTAP00000007563; ENSBTAG00000005754. [Q2PC20-1]
DR GeneID; 540329; -.
DR KEGG; bta:540329; -.
DR CTD; 152926; -.
DR VEuPathDB; HostDB:ENSBTAG00000005754; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000156633; -.
DR HOGENOM; CLU_013173_1_3_1; -.
DR InParanoid; Q2PC20; -.
DR OMA; MKGADNC; -.
DR OrthoDB; 1044139at2759; -.
DR TreeFam; TF354344; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000005754; Expressed in cardiac ventricle and 109 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Mitochondrion; Phosphoprotein; Protein phosphatase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..372
FT /note="Protein phosphatase 1K, mitochondrial"
FT /id="PRO_0000278207"
FT DOMAIN 94..346
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXN7"
FT VAR_SEQ 106..153
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023155"
FT CONFLICT 365
FT /note="F -> I (in Ref. 2; AAI18080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41151 MW; 5A8536B6E2F78090 CRC64;
MSTAALLTLV RSGGNQVRRR VLLRARGLQD DRWVMPTCHS STSEPKWSRF DPDGSGRPAT
WDNFGIWDNR LEEPILLPPS IKYGKPIPKV SLQNVGSASQ IGKRKENEDR FGFAQLTNEV
LYFAVYDGHG GPAAADFCHT HMEKCILDLL PKEENLETVL TLAFLEIDKT FARHAHLSAD
ATLLTSGTTA TVALLRDGIE LVIASVGDSR AILCRKGKPM KLTIDHTPER KDEKERIKKC
GGFVAWNSLG QPHVNGRLAM TRSLGDLDLK TSGVIAEPET KRIKLHHADD SFLVLTTDGI
NFMVNSQEIC DFVNQCHDPN EAAHAVTEQA IQYGTEDNTT AVVVPFGAWG KYKNSEITFS
FSRSFASSGR WA
