ID   MITOS_XENTR             Reviewed;         688 AA.
AC   B2GUP8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
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};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2008) 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; BC166360; AAI66360.1; -; mRNA.
DR   RefSeq; NP_001121515.1; NM_001128043.1.
DR   AlphaFoldDB; B2GUP8; -.
DR   SMR; B2GUP8; -.
DR   STRING; 8364.ENSXETP00000026160; -.
DR   PaxDb; B2GUP8; -.
DR   GeneID; 100158634; -.
DR   KEGG; xtr:100158634; -.
DR   CTD; 11194; -.
DR   Xenbase; XB-GENE-1010256; abcb8.
DR   eggNOG; KOG0058; Eukaryota.
DR   InParanoid; B2GUP8; -.
DR   OrthoDB; 684058at2759; -.
DR   Reactome; R-XTR-1369007; Mitochondrial ABC transporters.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000011958; Expressed in testis and 16 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..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..688
FT                   /note="Mitochondrial potassium channel ATP-binding subunit"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000356237"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00441"
FT   DOMAIN          121..409
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          442..679
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         477..484
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   688 AA;  74747 MW;  C013E76EAB7E93C4 CRC64;
     MLFHFLQAGL RQCRPPARLV GLETGLSGAR GPSLPATLAN YSRLRNACRP PWRSPWKPVK
     KGKLLAVLLG PAVLGVGVRA ARCQVELIAP PLIVPQGARP EPEFNWAEFW KLLRPQLIAL
     LTAVLLAFGA ALLNIRIPLM LGELVNVVSR YTREHAGNYL QEVQGPALKL LCLYGAQGLL
     TCGYIVLLSR VGERVAGSMR KSLFFSLLRQ DVAFFDAEKT GLLVNRLTSD VQEFKSSFKQ
     VISQGLRSLT QTVGCFLSLY YISPKLTGLL LVVMPVLVGS GALIGSFLRK LSRRAQEQVA
     RATGLADEAL GNVRTVKAFA MESREMELYS AEVDKSSGQN EVLGVGIAVF QGLSNVVLNC
     IVLGTIFAGG SLMSSKELSA GELMSFLVAS QTVQRSMANM SVLFGQVVRG LSAGGRVFEF
     MSLEPTIPLS GGFKLPVLRG EIHFKDVSFS YPTRPGHEVL RSFDLRIPHG KTVALVGQSG
     GGKSTVAALL ERFYDPTEGA VQLDGVDIRI LDPSWLRGEV IGFINQEPVL FGTTIIENIR
     FGRPDATDAE VHEAAIQANA DSFIRSFPEG YNTMLGERGV TLSGGQKQRV AIARALLKDP
     KILILDEATS ALDTESERAV QVALDRARSG RTVLVIAHRL STISEADFIV VLSKGQVAEF
     GTHQDLLRRG GLYADLIRRQ NQESQEAQ