MITOS_PONAB
ID MITOS_PONAB Reviewed; 718 AA.
AC Q5RFQ9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
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; Synonyms=MITOSUR {ECO:0000250|UniProtKB:Q9NUT2};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- ACTIVITY REGULATION: Channel activity inhibited by ATP via
CC ABCB8/MITOSUR subunit. {ECO:0000250|UniProtKB:Q9NUT2}.
CC -!- SUBUNIT: The mitochondrial potassium channel (mitoK(ATP)) is composed
CC of 4 subunits of CCDC51/MITOK and 4 subunits of ABCB8/MITOSUR.
CC Physically interacts with PAAT. Interacts with Neuropilin-1 (NRP1) in
CC mitochondria. {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; CR857093; CAH89398.1; -; mRNA.
DR RefSeq; NP_001124589.1; NM_001131117.1.
DR AlphaFoldDB; Q5RFQ9; -.
DR SMR; Q5RFQ9; -.
DR STRING; 9601.ENSPPYP00000020386; -.
DR GeneID; 100171425; -.
DR KEGG; pon:100171425; -.
DR CTD; 11194; -.
DR eggNOG; KOG0058; Eukaryota.
DR InParanoid; Q5RFQ9; -.
DR OrthoDB; 684058at2759; -.
DR Proteomes; UP000001595; Unplaced.
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..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..718
FT /note="Mitochondrial potassium channel ATP-binding subunit"
FT /evidence="ECO:0000255"
FT /id="PRO_0000356234"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 133..420
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 455..692
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 697..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 490..497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 718 AA; 78186 MW; 4DB86585C1F1EA95 CRC64;
MLVHLFRVGI RGGPFPGRLL PPLRFQTFSA VRYSDGYRSS SLFWAVAHLR SQLWAHLPRA
PLAPRWSPSA WCWVGGALLG PMVLSKHPHL CLVALCEAEE ATPASSTPHV VGSRFNWKLF
WQFLRPHLLV LGVAVVLALG AALVNVQIPL LLGQLVEIVA KYTRDHVGSF MTESQNLSTH
LLILYGVQGL LTFGYLVLLS HVGERMAVDM RRALFSSLLR QDIAFFDANK TGQLVSRLTT
DVQEFKSSFK LVISQGLRSC TQVAGCLVSL SMLSTRLTLL LMLATPALMG VGTLMGSGLR
KLSRQCQEQI ARAMGVADEA LGNVRTVRAF AMEQREEERY GAELEACRCR AEELGRGIAL
SQGLSNIAFN CMVLGTLFIG GSLVAGQQLT GGDLMSFLVA SQTVQRSMAN LSVLFGQVVR
GLSAGARVFE YMALNPCIPL SGGCCVPKEQ LRGSVTFQNV CFSYPCRPGF EVLKDFTLTL
PPGKIVALVG QSGGGKTTVA SLLERFYDPT AGVVMLDGRD LRTLDPSWLR GQVVGFISQE
PVLFGTTIME NIRFGKLEAS DEEVYAAARE ANAHEFITSF PEGYNTIVGE RGTTLSGGQK
QRLAIARALI KQPTVLILDE ATSALDAESE RVVQEALDRA SAGRTVLVIA HRLSTVRGAH
RIVVMADGRV WEAGTHEELL KKGGLYAELI RRQALDAPRT AAPLPKKPEG PRNHQHKS
