ID   MITOK_RAT               Reviewed;         410 AA.
AC   Q5PPN7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Mitochondrial potassium channel {ECO:0000250|UniProtKB:Q3URS9};
DE            Short=MITOK {ECO:0000250|UniProtKB:Q3URS9};
DE   AltName: Full=Coiled-coil domain-containing protein 51;
DE   Flags: Precursor;
GN   Name=Ccdc51 {ECO:0000250|UniProtKB:Q3URS9};
GN   Synonyms=Mitok {ECO:0000250|UniProtKB:Q3URS9};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mitochondrial potassium channel located in the mitochondrial
CC       inner membrane. Together with ABCB8/MITOSUR, forms a protein complex
CC       localized in the mitochondria that mediates ATP-dependent potassium
CC       currents across the inner membrane (that is, mitoK(ATP) channel). May
CC       contribute to the homeostatic control of cellular metabolism under
CC       stress conditions by regulating the mitochondrial matrix volume.
CC       {ECO:0000250|UniProtKB:Q3URS9}.
CC   -!- ACTIVITY REGULATION: Channel activity inhibited by ATP via
CC       ABCB8/MITOSUR subunit. {ECO:0000250|UniProtKB:Q96ER9}.
CC   -!- SUBUNIT: The mitochondrial potassium channel (mitoK(ATP)) forms a
CC       heteromultimer. {ECO:0000250|UniProtKB:Q3URS9}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q3URS9}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH87581.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC087581; AAH87581.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001014120.1; NM_001014098.1.
DR   RefSeq; XP_006243853.1; XM_006243791.2.
DR   RefSeq; XP_006243854.1; XM_006243792.3.
DR   AlphaFoldDB; Q5PPN7; -.
DR   SMR; Q5PPN7; -.
DR   STRING; 10116.ENSRNOP00000028075; -.
DR   iPTMnet; Q5PPN7; -.
DR   PhosphoSitePlus; Q5PPN7; -.
DR   PaxDb; Q5PPN7; -.
DR   PRIDE; Q5PPN7; -.
DR   GeneID; 316008; -.
DR   KEGG; rno:316008; -.
DR   UCSC; RGD:1311466; rat.
DR   CTD; 79714; -.
DR   RGD; 1311466; Ccdc51.
DR   eggNOG; ENOG502QWCS; Eukaryota.
DR   HOGENOM; CLU_060968_0_0_1; -.
DR   InParanoid; Q5PPN7; -.
DR   PhylomeDB; Q5PPN7; -.
DR   TreeFam; TF318449; -.
DR   PRO; PR:Q5PPN7; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; Q5PPN7; RN.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0062157; C:mitochondrial ATP-gated potassium channel complex; ISS:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR   GO; GO:0034705; C:potassium channel complex; ISO:RGD.
DR   GO; GO:0062156; F:mitochondrial ATP-gated potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0006884; P:cell volume homeostasis; ISO:RGD.
DR   GO; GO:0140141; P:mitochondrial potassium ion transmembrane transport; ISO:RGD.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR   InterPro; IPR037660; CCDC51.
DR   PANTHER; PTHR28624; PTHR28624; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Ion channel; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transit peptide; Transmembrane;
KW   Transmembrane helix; Transport.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..410
FT                   /note="Mitochondrial potassium channel"
FT                   /evidence="ECO:0000250|UniProtKB:Q3URS9"
FT                   /id="PRO_0000288870"
FT   TOPO_DOM        36..201
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q3URS9"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..385
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q3URS9"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        407..410
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:Q3URS9"
FT   REGION          276..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          116..143
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   410 AA;  45813 MW;  280EDB699DFE29C2 CRC64;
     MTGCSPVFTM QQVVGVSHRL VWRTFRGTDL LMTRTLCSPG PSRPGEKRPE AAALGLYHRL
     PELGRTLSHT IRNQAASTAK AWWDRYEEFV GLNEVREAQG NVTEAEKVFM VARGLVREAR
     EDLEAQQTKL KEVRDRLDRV SREDNQYLEL ATLEHRMLQE EKRLRIAYLR AEDSEREKFS
     LFSAAVRESH EKERTRAERT KNWSLIGSVL GALIGVAGST YVNRVRLQEL KALLLEAQKG
     PVSLQEAIRE QASSYSLQQK DLQNLMVDLR GLVHVGQDQG SGSPTGPSSP RGKDIDGLSA
     AMKEQLNHSR QVYSCLEGLR EQLDSLEKTC SQMAGVVRLA KVPAHPGMVE PLDGALPSSL
     LEHGSTMLAL SEMEQRLEAQ ANRNAISSTL VTCVTFMATL PLLYMLFKTS