ABCB7_RAT
ID ABCB7_RAT Reviewed; 752 AA.
AC Q704E8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Iron-sulfur clusters transporter ABCB7, mitochondrial {ECO:0000305};
DE AltName: Full=ATP-binding cassette sub-family B member 7, mitochondrial;
DE AltName: Full=ATP-binding cassette transporter 7;
DE Short=ABC transporter 7 protein;
DE Flags: Precursor;
GN Name=Abcb7 {ECO:0000250|UniProtKB:Q61102};
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].
RC STRAIN=Wistar;
RA Jakimenko A., Petry F., Hirsch-Ernst K.I.;
RT "Characterization of Abcb7 in rat hepatocytes.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; TYR-340 AND THR-342, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP FUNCTION, AND INTERACTION WITH COX4I1 AND ATP5F1A.
RX PubMed=31511561; DOI=10.1038/s41598-019-49666-0;
RA Kumar V., Kumar A., Sanawar R., Jaleel A., Santhosh Kumar T.R.,
RA Kartha C.C.;
RT "Chronic Pressure Overload Results in Deficiency of Mitochondrial Membrane
RT Transporter ABCB7 Which Contributes to Iron Overload, Mitochondrial
RT Dysfunction, Metabolic Shift and Worsens Cardiac Function.";
RL Sci. Rep. 9:13170-13170(2019).
CC -!- FUNCTION: Exports glutathione-coordinated iron-sulfur clusters such as
CC [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-
CC dependent manner allowing the assembly of the cytosolic iron-sulfur
CC (Fe/S) cluster-containing proteins and participates in iron homeostasis
CC (By similarity). Moreover, through a functional complex formed of
CC ABCB7, FECH and ABCB10, also plays a role in the cellular iron
CC homeostasis, mitochondrial function and heme biosynthesis (By
CC similarity). In cardiomyocytes, regulates cellular iron homeostasis and
CC cellular reactive oxygen species (ROS) levels through its interaction
CC with COX4I1 (PubMed:31511561). May also play a role in hematopoiesis
CC (By similarity). {ECO:0000250|UniProtKB:O75027,
CC ECO:0000250|UniProtKB:Q61102, ECO:0000269|PubMed:31511561}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(glutathione)4[2Fe(III)-2S] cluster(in) + ATP + H2O =
CC (glutathione)4[2Fe(III)-2S] cluster(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:67028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167627,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O75027};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67029;
CC Evidence={ECO:0000250|UniProtKB:O75027};
CC -!- SUBUNIT: Homodimer or heterodimer. Interacts with C10orf88/PAAT. Forms
CC a complex with ABCB10 and FECH, where a dimeric FECH bridges ABCB7 and
CC ABCB10 homodimers; this complex may be required for cellular iron
CC homeostasis, mitochondrial function and heme biosynthesis (By
CC similarity). Interacts with FECH (By similarity). Interacts with
CC ATP5F1A (PubMed:31511561). Interacts with COX4I1; this interaction
CC allows the regulation of cellular iron homeostasis and cellular
CC reactive oxygen species (ROS) levels in cardiomyocytes
CC (PubMed:31511561). {ECO:0000250|UniProtKB:O75027,
CC ECO:0000269|PubMed:31511561}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P40416}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Heavy Metal importer (TC 3.A.1.210) subfamily. {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; AJ621255; CAF18435.1; -; mRNA.
DR RefSeq; NP_997683.1; NM_212518.1.
DR AlphaFoldDB; Q704E8; -.
DR SMR; Q704E8; -.
DR BioGRID; 257169; 1.
DR STRING; 10116.ENSRNOP00000003739; -.
DR iPTMnet; Q704E8; -.
DR PhosphoSitePlus; Q704E8; -.
DR jPOST; Q704E8; -.
DR PaxDb; Q704E8; -.
DR PRIDE; Q704E8; -.
DR GeneID; 302395; -.
DR KEGG; rno:302395; -.
DR UCSC; RGD:1303086; rat.
DR CTD; 22; -.
DR RGD; 1303086; Abcb7.
DR eggNOG; KOG0057; Eukaryota.
DR InParanoid; Q704E8; -.
DR OrthoDB; 248727at2759; -.
DR PhylomeDB; Q704E8; -.
DR Reactome; R-RNO-1369007; Mitochondrial ABC transporters.
DR PRO; PR:Q704E8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0140481; F:ABC-type iron-sulfur cluster transporter activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IDA:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0034755; P:iron ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; ISS:UniProtKB.
DR GO; GO:0140466; P:iron-sulfur cluster export from the mitochondrion; ISS:UniProtKB.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR GO; GO:0070455; P:positive regulation of heme biosynthetic process; ISS:UniProtKB.
DR GO; GO:1903331; P:positive regulation of iron-sulfur cluster assembly; 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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..752
FT /note="Iron-sulfur clusters transporter ABCB7,
FT mitochondrial"
FT /id="PRO_0000000250"
FT TOPO_DOM 23..140
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 162..185
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 207..259
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 281..290
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 312..382
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 404..409
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 431..752
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT DOMAIN 140..436
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 472..706
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 315..319
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 378..381
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P40416"
FT BINDING 428
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q2G506"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NP58"
FT BINDING 505..516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 216
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75027"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75027"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 340
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61102"
SQ SEQUENCE 752 AA; 82558 MW; 83AB45A9ACA4F8AB CRC64;
MALLAIHSWR WAAAAVAFEK HKHSAVLTRS LVSICGSGLR WSSYQSGASG SARLSQTTES
LRNSTQQRWE KNNSRQLLDA SKVLQAWPLI EKRTCWHGHA GGGLHTDPKE GLKDVDTRKI
IKAMLSYVWP KDRPDLRARV AISLGFLGGA KAMNIVVPFM FKYAVDSLNQ MSGNMLNLSD
APNTVATMAT AVLIGYGVSR AGAAFFNEVR NAVFGKVAQN SIRRIAKNVF LHLHNLDLGF
HLSRQTGALS KAIDRGTRGI SFVLSALVFN LLPIVFEMTL VSSVLYYKCG AQFALVTLGT
LGAYTAFTVA VTRWRTRFRI EMNKADNDAG NAAIDSLLNY ETVKYFNNEK YEAQRYDGFL
KTYETASLKS TSTLAMLNFG QSAIFSVGLT AIMVLASQGI VAGALTVGDL VMVNGLLFQL
SLPLNFLGTV YRETRQALID MNTLFTLLKV DTRIKDKAMA SPLQITPQTA TVAFDNVHFE
YIEGQKVLSG VSFEVPAGKK VAIVGGSGSG KSTIVRLLFR FYEPQKGSIY LAGQNIQDVS
LESLRRAVGV VPQDAVLFHN TIYYNLLYGN INASPEEVYA VAKLAGLHDA ILRMPHGYDT
QVGERGLKLS GGEKQRVAIA RAILKDPPVI LYDEATSSLD SITEETILGA MRDVVKHRTS
IFIAHRLSTV VDADEIIVLS QGKVAERGTH YGLLANSSSI YSEMWHTQST RIQNHDNLGW
DAKKESLSKE EERKKLQEEI VNSVKGCGNC SC
