MITOK_HUMAN
ID MITOK_HUMAN Reviewed; 411 AA.
AC Q96ER9; Q9HA01;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Mitochondrial potassium channel {ECO:0000303|PubMed:31435016};
DE Short=MITOK {ECO:0000303|PubMed:31435016};
DE AltName: Full=Coiled-coil domain-containing protein 51 {ECO:0000305};
DE Flags: Precursor;
GN Name=CCDC51 {ECO:0000312|HGNC:HGNC:25714};
GN Synonyms=MITOK {ECO:0000303|PubMed:31435016};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT, AND ACTIVITY
RP REGULATION.
RX PubMed=31435016; DOI=10.1038/s41586-019-1498-3;
RA Paggio A., Checchetto V., Campo A., Menabo R., Di Marco G., Di Lisa F.,
RA Szabo I., Rizzuto R., De Stefani D.;
RT "Identification of an ATP-sensitive potassium channel in mitochondria.";
RL Nature 572:609-613(2019).
CC -!- FUNCTION: Mitochondrial potassium channel located in the mitochondrial
CC inner membrane (PubMed:31435016). Together with ABCB8/MITOSUR, forms a
CC protein complex localized in the mitochondria that mediates ATP-
CC dependent potassium currents across the inner membrane (that is,
CC mitoK(ATP) channel) (PubMed:31435016). May contribute to the
CC homeostatic control of cellular metabolism under stress conditions by
CC regulating the mitochondrial matrix volume (PubMed:31435016).
CC {ECO:0000269|PubMed:31435016}.
CC -!- ACTIVITY REGULATION: Channel activity inhibited by ATP via
CC ABCB8/MITOSUR subunit. {ECO:0000269|PubMed:31435016}.
CC -!- SUBUNIT: The mitochondrial potassium channel (mitoK(ATP)) is composed
CC of 4 subunits of CCDC51/MITOK and 4 subunits of ABCB8/MITOSUR.
CC {ECO:0000305|PubMed:31435016}.
CC -!- INTERACTION:
CC Q96ER9; Q9NUT2: ABCB8; NbExp=2; IntAct=EBI-11926384, EBI-722515;
CC Q96ER9; P57086: SCAND1; NbExp=3; IntAct=EBI-11926384, EBI-745846;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:31435016}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:31435016}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96ER9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96ER9-2; Sequence=VSP_025800;
CC -!- TISSUE SPECIFICITY: Isoform 1: Widely expressed (PubMed:31435016).
CC Isoform 2: Expression is barely detectable (PubMed:31435016).
CC {ECO:0000269|PubMed:31435016}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11993.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK022498; BAB14060.1; -; mRNA.
DR EMBL; BC011993; AAH11993.1; ALT_INIT; mRNA.
DR CCDS; CCDS2766.2; -. [Q96ER9-1]
DR CCDS; CCDS58830.1; -. [Q96ER9-2]
DR RefSeq; NP_001243893.1; NM_001256964.1. [Q96ER9-1]
DR RefSeq; NP_001243894.1; NM_001256965.2. [Q96ER9-2]
DR RefSeq; NP_001243895.1; NM_001256966.2. [Q96ER9-2]
DR RefSeq; NP_001243896.1; NM_001256967.2. [Q96ER9-2]
DR RefSeq; NP_001243897.1; NM_001256968.2. [Q96ER9-2]
DR RefSeq; NP_001243898.1; NM_001256969.2. [Q96ER9-2]
DR RefSeq; NP_078937.3; NM_024661.4. [Q96ER9-1]
DR AlphaFoldDB; Q96ER9; -.
DR SMR; Q96ER9; -.
DR BioGRID; 122831; 77.
DR ComplexPortal; CPX-6083; MITOK-MITOSUR mitochondrial potassium channel complex.
DR IntAct; Q96ER9; 38.
DR STRING; 9606.ENSP00000379047; -.
DR DrugBank; DB01236; Sevoflurane.
DR iPTMnet; Q96ER9; -.
DR PhosphoSitePlus; Q96ER9; -.
DR SwissPalm; Q96ER9; -.
DR BioMuta; CCDC51; -.
DR DMDM; 152032342; -.
DR EPD; Q96ER9; -.
DR jPOST; Q96ER9; -.
DR MassIVE; Q96ER9; -.
DR MaxQB; Q96ER9; -.
DR PaxDb; Q96ER9; -.
DR PeptideAtlas; Q96ER9; -.
DR PRIDE; Q96ER9; -.
DR ProteomicsDB; 76443; -. [Q96ER9-1]
DR ProteomicsDB; 76444; -. [Q96ER9-2]
DR Antibodypedia; 2566; 126 antibodies from 18 providers.
DR DNASU; 79714; -.
DR Ensembl; ENST00000395694.7; ENSP00000379047.2; ENSG00000164051.14. [Q96ER9-1]
DR Ensembl; ENST00000412398.6; ENSP00000401194.2; ENSG00000164051.14. [Q96ER9-2]
DR Ensembl; ENST00000442740.1; ENSP00000392898.1; ENSG00000164051.14. [Q96ER9-2]
DR Ensembl; ENST00000447018.5; ENSP00000412300.1; ENSG00000164051.14. [Q96ER9-2]
DR GeneID; 79714; -.
DR KEGG; hsa:79714; -.
DR MANE-Select; ENST00000395694.7; ENSP00000379047.2; NM_001256964.2; NP_001243893.1.
DR UCSC; uc003ctd.3; human. [Q96ER9-1]
DR CTD; 79714; -.
DR DisGeNET; 79714; -.
DR GeneCards; CCDC51; -.
DR HGNC; HGNC:25714; CCDC51.
DR HPA; ENSG00000164051; Low tissue specificity.
DR MIM; 618585; gene.
DR neXtProt; NX_Q96ER9; -.
DR OpenTargets; ENSG00000164051; -.
DR PharmGKB; PA142672167; -.
DR VEuPathDB; HostDB:ENSG00000164051; -.
DR eggNOG; ENOG502QWCS; Eukaryota.
DR GeneTree; ENSGT00390000001709; -.
DR HOGENOM; CLU_060968_0_0_1; -.
DR InParanoid; Q96ER9; -.
DR OMA; STATTWW; -.
DR OrthoDB; 1459041at2759; -.
DR PhylomeDB; Q96ER9; -.
DR TreeFam; TF318449; -.
DR PathwayCommons; Q96ER9; -.
DR SignaLink; Q96ER9; -.
DR BioGRID-ORCS; 79714; 83 hits in 1084 CRISPR screens.
DR ChiTaRS; CCDC51; human.
DR GenomeRNAi; 79714; -.
DR Pharos; Q96ER9; Tdark.
DR PRO; PR:Q96ER9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96ER9; protein.
DR Bgee; ENSG00000164051; Expressed in pigmented layer of retina and 169 other tissues.
DR ExpressionAtlas; Q96ER9; baseline and differential.
DR Genevisible; Q96ER9; HS.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0062157; C:mitochondrial ATP-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0062156; F:mitochondrial ATP-gated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0006884; P:cell volume homeostasis; IDA:ComplexPortal.
DR GO; GO:0140141; P:mitochondrial potassium ion transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR InterPro; IPR037660; CCDC51.
DR PANTHER; PTHR28624; PTHR28624; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Ion channel; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..411
FT /note="Mitochondrial potassium channel"
FT /evidence="ECO:0000255"
FT /id="PRO_0000288868"
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..386
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q3URS9"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..411
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:Q3URS9"
FT REGION 274..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 111..173
FT /evidence="ECO:0000255"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..109
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025800"
FT VARIANT 360
FT /note="F -> S (in dbSNP:rs7618609)"
FT /id="VAR_032515"
SQ SEQUENCE 411 AA; 45811 MW; D99F1D8AF9EB8C04 CRC64;
MMGRSPGFAM QHIVGVPHVL VRRGLLGRDL FMTRTLCSPG PSQPGEKRPE EVALGLHHRL
PALGRALGHS IQQRATSTAK TWWDRYEEFV GLNEVREAQG KVTEAEKVFM VARGLVREAR
EDLEVHQAKL KEVRDRLDRV SREDSQYLEL ATLEHRMLQE EKRLRTAYLR AEDSEREKFS
LFSAAVRESH EKERTRAERT KNWSLIGSVL GALIGVAGST YVNRVRLQEL KALLLEAQKG
PVSLQEAIRE QASSYSRQQR DLHNLMVDLR GLVHAAGPGQ DSGSQAGSPP TRDRDVDVLS
AALKEQLSHS RQVHSCLEGL REQLDGLEKT CSQMAGVVQL VKSAAHPGLV EPADGAMPSF
LLEQGSMILA LSDTEQRLEA QVNRNTIYST LVTCVTFVAT LPVLYMLFKA S
