MITOS_RAT
ID MITOS_RAT Reviewed; 714 AA.
AC Q5RKI8; Q0QVT4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Mitochondrial potassium channel ATP-binding subunit {ECO:0000305};
DE AltName: Full=ATP-binding cassette sub-family B member 8, mitochondrial {ECO:0000303|PubMed:16390497};
DE Short=ABCB8 {ECO:0000303|PubMed:16390497};
DE AltName: Full=Mitochondrial sulfonylurea-receptor {ECO:0000250|UniProtKB:Q9NUT2};
DE Short=MITOSUR {ECO:0000250|UniProtKB:Q9NUT2};
DE Flags: Precursor;
GN Name=Abcb8 {ECO:0000303|PubMed:16390497};
GN Synonyms=Mitosur {ECO:0000250|UniProtKB:Q9NUT2};
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16390497; DOI=10.1111/j.1365-2605.2005.00616.x;
RA Melaine N., Satie A.-P., Lassurguere J., Desmots S., Jegou B., Samson M.;
RT "Molecular cloning of several rat ABC transporters including a new ABC
RT transporter, Abcb8, and their expression in rat testis.";
RL Int. J. Androl. 29:392-399(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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: 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 -!- TISSUE SPECIFICITY: Strong expression is found in the heart, brain and
CC testis (PubMed:16390497). In the testis, expressed both in the somatic
CC Sertoli cells and peritubular cells and in the germline (spermatogonia
CC and pachytene spermatocytes) (PubMed:16390497). Also expressed in the
CC lung, liver, intestine and kidney (PubMed:16390497).
CC {ECO:0000269|PubMed:16390497}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB71108.1; Type=Frameshift; 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; DQ233644; ABB71108.1; ALT_FRAME; mRNA.
DR EMBL; CH474020; EDL99373.1; -; Genomic_DNA.
DR EMBL; BC085781; AAH85781.1; -; mRNA.
DR RefSeq; NP_001007797.1; NM_001007796.1.
DR AlphaFoldDB; Q5RKI8; -.
DR SMR; Q5RKI8; -.
DR CORUM; Q5RKI8; -.
DR STRING; 10116.ENSRNOP00000012222; -.
DR iPTMnet; Q5RKI8; -.
DR PhosphoSitePlus; Q5RKI8; -.
DR PaxDb; Q5RKI8; -.
DR PRIDE; Q5RKI8; -.
DR Ensembl; ENSRNOT00000012222; ENSRNOP00000012222; ENSRNOG00000008557.
DR GeneID; 362302; -.
DR KEGG; rno:362302; -.
DR CTD; 11194; -.
DR RGD; 1307655; Abcb8.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000159126; -.
DR InParanoid; Q5RKI8; -.
DR OMA; FNTLQMG; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; Q5RKI8; -.
DR TreeFam; TF105196; -.
DR Reactome; R-RNO-1369007; Mitochondrial ABC transporters.
DR PRO; PR:Q5RKI8; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Proteomes; UP000234681; Chromosome 4.
DR Bgee; ENSRNOG00000008557; Expressed in heart and 18 other tissues.
DR ExpressionAtlas; Q5RKI8; baseline and differential.
DR Genevisible; Q5RKI8; RN.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
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 GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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..714
FT /note="Mitochondrial potassium channel ATP-binding subunit"
FT /evidence="ECO:0000255"
FT /id="PRO_0000356235"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 132..419
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 454..691
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 489..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 540
FT /note="P -> T (in Ref. 1; ABB71108)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="S -> C (in Ref. 1; ABB71108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 77770 MW; A77B4362C41C9C5C CRC64;
MLVHLFRVGI RGGPVPRWSL QSLRFQTFSA ARSSDDQFSS CLLRAVAQLR SQLRAHLPRS
PPASHRSTSA WCWVGGTLVV PAVLWQHPRF CLIALCEAKG SPPAQPTRAR ELRFKWKLFW
HFLHPHLLAL GLAIVLALGA ALVNVQIPLL LGQLVEIVAK YTREHVGSFV SESRRLSIQL
LLLYGVQGLL TFGYLVLLSH MGERMAMDMR KALFSSLLRQ DIAFFDAKKT GQLVSRLTTD
VQEFKSSFKL VISQGLRSST QVIGSLMTLS ILSPRLTLML AVVTPALMGV GTLMGSGLRK
LSRQCQEQIA RATGVADEAL GSVRTVRAFA MEKREEERYQ AELESCCCKA EELGRGIALF
QGLSNIAFNC MVLGTLFIGG SLVAGQQLKG GDLMSFLVAS QTVQRSMASL SVLFGQVVRG
LSAGARVFEY MSLSPVIPLT GGYSIPSKDL RGSITFQNVS FSYPCRPGFN VLKNFTLKLP
PGKIVALVGQ SGGGKTTVAS LLERFYDPTA GVVTLDGHDL RTLDPSWLRG QVIGFISQEP
VLFATTIMEN IRFGKLDASD EEVYTAARKA NAHEFISSFP DGYSTVVGER GTTLSGGQKQ
RLAIARALIK RPTVLILDEA TSALDAESER IVQEALDRAS AGRTVLVIAH RLSTVRAAHS
IIVMANGQVC EAGTHEELLQ KGGLYAELIR RQALDASLPS APPAEKPEDH RSCQ
