Protein phosphatase 1K, mitochondrial (EC 3.1.3.16) (PP2C domain-containing protein phosphatase 1K) (PP2C-like mitochondrial protein) (PP2C-type mitochondrial phosphoprotein phosphatase) (PTMP) (Protein phosphatase 2C isoform kappa) (PP2C-kappa)
1_MSTAA 6_ LITLV 11_ RSGGN 16_ QVRRR 21_ VLLSS 26_ RLLQD 31_ DRRVT 36_ PTCHS 41_ STSEP 46_ RCSRF 51_ DPDGS 56_ GSPAT 61_ WDNFG 66_ IWDNR 71_ IDEPI 76_ LLPPS 81_ IKYGK 86_ PIPKI 91_ SLENV 96_ GCASQ 101_ IGKRK 106_ ENEDR 111_ FDFAQ 116_ LTDEV 121_ LYFAV 126_ YDGHG 131_ GPAAA 136_ DFCHT 141_ HMEKC 146_ IMDLL 151_ PKEKN 156_ LETLL 161_ TLAFL 166_ EIDKA 171_ FSSHA 176_ RLSAD 181_ ATLLT 186_ SGTTA 191_ TVALL 196_ RDGIE 201_ LVVAS 206_ VGDSR 211_ AILCR 216_ KGKPM 221_ KLTID 226_ HTPER 231_ KDEKE 236_ RIKKC 241_ GGFVA 246_ WNSLG 251_ QPHVN 256_ GRLAM 261_ TRSIG 266_ DLDLK 271_ TSGVI 276_ AEPET 281_ KRIKL 286_ HHADD 291_ SFLVL 296_ TTDGI 301_ NFMVN 306_ SQEIC 311_ DFVNQ 316_ CHDPN 321_ EAAHA 326_ VTEQA 331_ IQYGT 336_ EDNST 341_ AVVVP 346_ FGAWG 351_ KYKNS 356_ EINFS 361_ FSRSF 366_ASSGR
1: Serine/threonine-protein phosphatase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with BCKDK, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). At high levels of branched-chain ketoacids, dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Tightly associates with the E2 component of BCKDH complex and dephosphorylates BCKDHA on Ser-337 (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). Regulates the reversible phosphorylation of ACLY in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. At fasting state, appears to dephosphorylate ACLY on Ser-455 and inactivate it. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and gluconeogenesis, respectively (PubMed:29779826). Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity (PubMed:29779826). Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death (PubMed:17374715)