ID F7HI43_CALJA Unreviewed; 372 AA.
AC F7HI43;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Protein phosphatase Mn(2+)-dependent 1K {ECO:0000256|ARBA:ARBA00044138};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.52 {ECO:0000256|ARBA:ARBA00044043};
DE AltName: Full=Branched-chain alpha-ketoacid dehydrogenase phosphatase {ECO:0000256|ARBA:ARBA00044323};
DE AltName: Full=Protein phosphatase 2C family member {ECO:0000256|ARBA:ARBA00044233};
GN Name=PPM1K {ECO:0000313|EMBL:JAB03058.1,
GN ECO:0000313|Ensembl:ENSCJAP00000011859.2};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000011859.2, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000011859.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB03058.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB03058.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB21963.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB40752.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000011859.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[3-methyl-2-oxobutanoate
CC dehydrogenase] = L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] +
CC phosphate; Xref=Rhea:RHEA:77247, Rhea:RHEA-COMP:13695, Rhea:RHEA-
CC COMP:13696, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.52;
CC Evidence={ECO:0000256|ARBA:ARBA00043761};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77248;
CC Evidence={ECO:0000256|ARBA:ARBA00043761};
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:ARBA00036558};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000256|ARBA:ARBA00036558};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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DR EMBL; GAMT01008803; JAB03058.1; -; mRNA.
DR EMBL; GAMS01001173; JAB21963.1; -; mRNA.
DR EMBL; GAMQ01001099; JAB40752.1; -; mRNA.
DR RefSeq; XP_002745650.1; XM_002745604.3.
DR STRING; 9483.ENSCJAP00000011859; -.
DR Ensembl; ENSCJAT00000012507.4; ENSCJAP00000011859.2; ENSCJAG00000006428.5.
DR GeneID; 100410897; -.
DR KEGG; cjc:100410897; -.
DR CTD; 152926; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000156633; -.
DR HOGENOM; CLU_013173_1_3_1; -.
DR OrthoDB; 202023at2759; -.
DR TreeFam; TF354344; -.
DR Proteomes; UP000008225; Chromosome 3.
DR Bgee; ENSCJAG00000006428; Expressed in heart and 6 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
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:SF226; PROTEIN PHOSPHATASE 1K, MITOCHONDRIAL; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 94..346
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 33..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 41070 MW; 65A51CA93540D7F5 CRC64;
MSTAALITLV RSGGNQLRRR VLLSSRLLQD DRQVTPTCNS STSEPRCSRF DPDGSGRPAT
WDNFGIWDNR IDEPILLPPS IKYGKPIPKI SLENVGCASQ IGKRKENEDR FDFAQLTDEV
LYFAVYDGHG GPAAADFCHT HMEKCIRDLL PKEKNLETVL TLAFLEIDKA FSSHTRLSAD
ATLLTSGTTA TVALLRDGIE LVVASVGDSR AILCRKGKPM KLTIDHTPER KDEKERIKKC
GGFVAWNSLG QPHVNGRLAM TRSIGDLDLK TSGVIAEPET KRIKLHHADD SFLVLTTDGI
NFMVNSQEIC DFVNQCHDPN EAAHAVTEQA IQYGTEDNST AVVVPFGAWG KYKNSEINFS
FSRSFASSGR WA
//
