ABC1_ARATH
ID ABC1_ARATH Reviewed; 623 AA.
AC Q9SBB2; O65576;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein ABC transporter 1, mitochondrial {ECO:0000303|PubMed:9852956};
DE Short=ABC1At {ECO:0000303|PubMed:9852956};
DE Short=AtABC1 {ECO:0000303|PubMed:9852956};
DE EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00159};
GN Name=ABC1 {ECO:0000303|PubMed:9852956}; Synonyms=AtATH10 {ECO:0000305};
GN OrderedLocusNames=At4g01660 {ECO:0000312|Araport:AT4G01660};
GN ORFNames=T15B16.14 {ECO:0000312|EMBL:AAC72875.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=9852956; DOI=10.1016/s0378-1119(98)00417-x;
RA Cardazzo B., Hamel P., Sakamoto W., Wintz H., Dujardin G.;
RT "Isolation of an Arabidopsis thaliana cDNA by complementation of a yeast
RT abc1 deletion mutant deficient in complex III respiratory activity.";
RL Gene 221:117-125(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP INDUCTION BY UV-B.
RX PubMed=16330762; DOI=10.1073/pnas.0507187102;
RA Brown B.A., Cloix C., Jiang G.H., Kaiserli E., Herzyk P.,
RA Kliebenstein D.J., Jenkins G.I.;
RT "A UV-B-specific signaling component orchestrates plant UV protection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18225-18230(2005).
RN [5]
RP INDUCTION BY UV-B.
RX PubMed=16829591; DOI=10.1105/tpc.105.040097;
RA Oravecz A., Baumann A., Mate Z., Brzezinska A., Molinier J., Oakeley E.J.,
RA Adam E., Schaefer E., Nagy F., Ulm R.;
RT "CONSTITUTIVELY PHOTOMORPHOGENIC1 is required for the UV-B response in
RT Arabidopsis.";
RL Plant Cell 18:1975-1990(2006).
CC -!- FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q,
CC also named ubiquinone, an essential lipid-soluble electron transporter
CC for aerobic cellular respiration. {ECO:0000269|PubMed:9852956}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000250|UniProtKB:P27697}.
CC -!- SUBUNIT: Forms homopolymers. Predominantly associated with a complex of
CC about 500 kDa. {ECO:0000250|UniProtKB:P27697}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P27697}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P27697}; Matrix side
CC {ECO:0000250|UniProtKB:P27697}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves, buds and flowers.
CC {ECO:0000269|PubMed:9852956}.
CC -!- INDUCTION: Strongly induced by UV-B. {ECO:0000269|PubMed:16330762,
CC ECO:0000269|PubMed:16829591}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AJ001158; CAA04557.1; -; mRNA.
DR EMBL; AF104919; AAC72875.1; -; Genomic_DNA.
DR EMBL; AL161492; CAB77736.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82058.1; -; Genomic_DNA.
DR PIR; T02007; T02007.
DR PIR; T52128; T52128.
DR RefSeq; NP_192075.1; NM_116396.4.
DR AlphaFoldDB; Q9SBB2; -.
DR SMR; Q9SBB2; -.
DR STRING; 3702.AT4G01660.1; -.
DR iPTMnet; Q9SBB2; -.
DR PaxDb; Q9SBB2; -.
DR PRIDE; Q9SBB2; -.
DR ProteomicsDB; 245111; -.
DR EnsemblPlants; AT4G01660.1; AT4G01660.1; AT4G01660.
DR GeneID; 828127; -.
DR Gramene; AT4G01660.1; AT4G01660.1; AT4G01660.
DR KEGG; ath:AT4G01660; -.
DR Araport; AT4G01660; -.
DR TAIR; locus:2133357; AT4G01660.
DR eggNOG; KOG1234; Eukaryota.
DR HOGENOM; CLU_006533_9_1_1; -.
DR InParanoid; Q9SBB2; -.
DR OMA; QVERVMN; -.
DR OrthoDB; 525494at2759; -.
DR PhylomeDB; Q9SBB2; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:Q9SBB2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SBB2; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0015996; P:chlorophyll catabolic process; IMP:TAIR.
DR GO; GO:0017004; P:cytochrome complex assembly; IGI:TAIR.
DR GO; GO:0010224; P:response to UV-B; IEP:UniProtKB.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IGI:UniProtKB.
DR CDD; cd13970; ABC1_ADCK3; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR034646; ADCK3_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome; Transferase;
KW Ubiquinone biosynthesis.
FT CHAIN 1..623
FT /note="Protein ABC transporter 1, mitochondrial"
FT /id="PRO_0000435657"
FT DOMAIN 295..583
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 152..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 453
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 301..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 94
FT /note="V -> I (in Ref. 1; CAA04557)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="K -> E (in Ref. 1; CAA04557)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="N -> S (in Ref. 1; CAA04557)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="L -> V (in Ref. 1; CAA04557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 68627 MW; 976CFFD6BC2A8C80 CRC64;
MSSWSKSFTR LVNGVSLVAK EIYNQSPELQ RARNGDLEGL ITSSGKKALV AATDLVGLTS
GKLRELSIRR SKEPSVVYFD EGDNKDNVVA TPEVRSVNTK PSEKIVDSKV LRNEFSDEVK
NSNREGEIKV SGVEAGEIIG VRAVESGTVT EASSPSEVVP PVKRRRPRER KVPSTPMARA
YGFFNLGAAL AWGAVKESTY RMVNGTPMTP DNQPALSSLM SKENAERLAL GLCEMRGAAL
KVGQMLSIQD ESLVPAPILN ALEYVRQGAD VMPRSQLNPV LDAELGSNWQ SKLTSFDYEP
LAAASIGQVH RAVTKDGLEV AMKIQYPGVA NSIESDIENV RRLLNYTNLI PKGLFLDRAI
KVAKEELAQE CDYEIEAVSQ KRFRDLLSDT PGFYVPLVVD ETSSKKILTT ELISGIPIDK
VALLDQKTRD YVGRKMLELT LKELFVFRFM QTDPNWGNFL YNEATKTINL IDFGAARDYP
KKFVDDYLRM VMACAEKDSE GVIEMSRRLG FLTGDESDVM LDAHVQAGFI VGLPFAEPGG
YAFRTNNIAS SISNLGATML KHRLSPPPDE AYSLHRKLSG AFLACIKLGA TVPCRDLLLQ
VYNKYQFDDE PQDPVVATSS VSS
