MITOS_DANRE
ID MITOS_DANRE Reviewed; 714 AA.
AC Q56A55; F1QTQ6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Mitochondrial potassium channel ATP-binding subunit {ECO:0000305};
DE AltName: Full=ATP-binding cassette sub-family B member 8, mitochondrial {ECO:0000250|UniProtKB:Q9NUT2};
DE Short=ABCB8 {ECO:0000250|UniProtKB:Q9NUT2};
DE AltName: Full=Mitochondrial sulfonylurea-receptor {ECO:0000250|UniProtKB:Q9NUT2};
DE Short=MITOSUR {ECO:0000250|UniProtKB:Q9NUT2};
DE Flags: Precursor;
GN Name=abcb8 {ECO:0000250|UniProtKB:Q9NUT2};
GN Synonyms=mitosur {ECO:0000250|UniProtKB:Q9NUT2}; ORFNames=zgc:113037;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-binding subunit of the mitochondrial potassium channel
CC located in the mitochondrial inner membrane. Together with
CC CCDC51/MITOK, forms a protein complex localized in the mitochondria
CC that mediates ATP-dependent potassium currents across the inner
CC membrane (that is, mitoK(ATP) channel) (By similarity). Plays a role in
CC mitochondrial iron transport. Required for maintenance of normal
CC cardiac function, possibly by influencing mitochondrial iron export and
CC regulating the maturation of cytosolic iron sulfur cluster-containing
CC enzymes (By similarity). {ECO:0000250|UniProtKB:Q9CXJ4,
CC ECO:0000250|UniProtKB:Q9NUT2}.
CC -!- SUBUNIT: Component of the mitochondrial potassium channel (mitoK(ATP)).
CC {ECO:0000250|UniProtKB:Q9NUT2}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9NUT2}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
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DR EMBL; CU019563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092161; AAH92161.1; -; mRNA.
DR RefSeq; NP_001017544.1; NM_001017544.1.
DR AlphaFoldDB; Q56A55; -.
DR SMR; Q56A55; -.
DR STRING; 7955.ENSDARP00000073658; -.
DR PaxDb; Q56A55; -.
DR Ensembl; ENSDART00000079202; ENSDARP00000073658; ENSDARG00000056672.
DR GeneID; 548340; -.
DR KEGG; dre:548340; -.
DR CTD; 11194; -.
DR ZFIN; ZDB-GENE-050410-6; abcb8.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000159126; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; Q56A55; -.
DR OMA; FNTLQMG; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; Q56A55; -.
DR TreeFam; TF105196; -.
DR Reactome; R-DRE-1369007; Mitochondrial ABC transporters.
DR PRO; PR:Q56A55; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000056672; Expressed in early embryo and 27 other tissues.
DR GO; GO:0062157; C:mitochondrial ATP-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Potassium;
KW Potassium transport; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..714
FT /note="Mitochondrial potassium channel ATP-binding subunit"
FT /evidence="ECO:0000255"
FT /id="PRO_0000356236"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 148..435
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 470..707
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 505..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 63
FT /note="V -> I (in Ref. 2; AAH92161)"
SQ SEQUENCE 714 AA; 77322 MW; 406E6842FA8B2690 CRC64;
MFHFARCSRL TRGTVTSDRL LSSHKTRDFL FQHLNRRGNH SAPWSSSQIP STQLTVGVPV
LRVWRQAQKL LRLTSRQQPR PPSIALKFIL GPAALTVTAR LLGPSAHCEA DVNNNKVPLE
VQVKEKIPEF SWAVLWEFVR PQLFALMGAI LLAFGAAALN IQIPLMLGDL VNVVARHMRE
QAGHYMRDIQ APAVKLLGLY ALQGLLTSGY IILLSRVGER VAADMRTTLF TSLLRQDIAF
FDANKTGQLV NRLTSDIQEF KSSFKLVISQ GLRSATQTVG CFVSLYFISP KLTGLTVVVL
PCLVGAGALI GSFLRKLSRK AQEQVAKATG VADEALGNVR TVRAFAMEDR ELEMYAAEVQ
KSAAMNETLG TGIAVFQGLS NIVLNCIVLG TIFAGGSLMA RDDLSPGDLM SFLVASQTVQ
RSLASISILF GQMVRGMSAG ARVFEYLALD PSVPLTGGGR IPLDSLMGRV DFMNISFSYP
TRPGNQILKH FSLTLPPCKT VAIVGESGGG KSTVAALLER FYDPSSGVVM LDGLDIRTLD
PSWLRGHVIG FISQEPVLFG TSVMENIRFG KPSATDAEVV SAAKQANAHN FITGFADGYN
TVVGERGVTL SGGQKQRIAI ARALVKNPSI LILDEATSAL DAESERVVQE ALDRATTGRT
VLIIAHRLST IQAADLICVM SNGRIVEAGT HLELLSKGGL YAELIKRQRS NGHK
