ACFR1_ARATH
ID ACFR1_ARATH Reviewed; 239 AA.
AC Q8L856; O65605; Q8LE60; Q9CAZ1; Q9M0K3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transmembrane ascorbate ferrireductase 1;
DE EC=7.2.1.3 {ECO:0000269|PubMed:14730083, ECO:0000269|PubMed:17376442};
DE AltName: Full=Cytochrome b561;
DE Short=Artb561-1;
DE Short=AtCytb561;
DE AltName: Full=Protein b561A.tha5;
DE AltName: Full=Tonoplast Cyt-b561;
DE Short=TCytb;
GN Name=CYB561A; Synonyms=ACYB-2, CYB561B1, CYBASC1;
GN OrderedLocusNames=At4g25570; ORFNames=M7J2.60;
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].
RA Asada A., Kusakawa T., Orii H., Watanabe K., Tsubaki M.;
RT "Molecular cloning of cytochrome b561 from Arabidopsis thaliana.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11732342; DOI=10.1007/bf01289417;
RA Asard H., Kapila J., Verelst W., Berczi A.;
RT "Higher-plant plasma membrane cytochrome b561: a protein in search of a
RT function.";
RL Protoplasma 217:77-93(2001).
RN [7]
RP TOPOLOGY.
RX PubMed=12768339; DOI=10.1007/s00709-002-0065-0;
RA Bashtovyy D., Berczi A., Asard H., Pali T.;
RT "Structure prediction for the di-heme cytochrome b561 protein family.";
RL Protoplasma 221:31-40(2003).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15032866; DOI=10.1111/j.0031-9317.2004.0235.x;
RA Verelst W., Kapila J., De Almeida Engler J., Stone J.M., Caubergs R.,
RA Asard H.;
RT "Tissue-specific expression and developmental regulation of cytochrome b561
RT genes in Arabidopsis thaliana and Raphanus sativus.";
RL Physiol. Plantarum 120:312-318(2004).
RN [9]
RP SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=14730083; DOI=10.1104/pp.103.032359;
RA Griesen D., Su D., Berczi A., Asard H.;
RT "Localization of an ascorbate-reducible cytochrome b561 in the plant
RT tonoplast.";
RL Plant Physiol. 134:726-734(2004).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16169296; DOI=10.1016/j.bbapap.2005.08.015;
RA Tsubaki M., Takeuchi F., Nakanishi N.;
RT "Cytochrome b561 protein family: expanding roles and versatile
RT transmembrane electron transfer abilities as predicted by a new
RT classification system and protein sequence motif analyses.";
RL Biochim. Biophys. Acta 1753:174-190(2005).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17376442; DOI=10.1016/j.febslet.2007.03.006;
RA Berczi A., Su D., Asard H.;
RT "An Arabidopsis cytochrome b561 with trans-membrane ferrireductase
RT capability.";
RL FEBS Lett. 581:1505-1508(2007).
RN [12]
RP COFACTOR, TOPOLOGY, AND MUTAGENESIS OF HIS-83 AND HIS-156.
RX PubMed=21236254; DOI=10.1016/j.febslet.2011.01.006;
RA Desmet F., Berczi A., Zimanyi L., Asard H., Van Doorslaer S.;
RT "Axial ligation of the high-potential heme center in an Arabidopsis
RT cytochrome b561.";
RL FEBS Lett. 585:545-548(2011).
RN [13]
RP REVIEW.
RX PubMed=23249217; DOI=10.1089/ars.2012.5065;
RA Asard H., Barbaro R., Trost P., Berczi A.;
RT "Cytochromes b561: ascorbate-mediated trans-membrane electron transport.";
RL Antioxid. Redox Signal. 19:1026-1035(2013).
RN [14]
RP FUNCTION.
RX PubMed=22526465; DOI=10.1007/s00249-012-0812-x;
RA Berczi A., Zimanyi L., Asard H.;
RT "Dihydrolipoic acid reduces cytochrome b561 proteins.";
RL Eur. Biophys. J. 42:159-168(2013).
CC -!- FUNCTION: Two-heme-containing cytochrome. Catalyzes ascorbate-dependent
CC trans-membrane ferric-chelate reduction. Able to use dihydrolipoic acid
CC (DHLA) as an alternative substrate to ascorbate.
CC {ECO:0000269|PubMed:14730083, ECO:0000269|PubMed:17376442,
CC ECO:0000269|PubMed:22526465}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(3+)(out) + L-ascorbate(in) = Fe(2+)(out) + H(+) +
CC monodehydro-L-ascorbate radical(in); Xref=Rhea:RHEA:30403,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:59513; EC=7.2.1.3;
CC Evidence={ECO:0000269|PubMed:14730083, ECO:0000269|PubMed:17376442};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:21236254};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000269|PubMed:21236254};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9SWS1}.
CC -!- INTERACTION:
CC Q8L856; Q9SIN1: TTL3; NbExp=2; IntAct=EBI-2295096, EBI-2292882;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14730083};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14730083}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings and leaves. Lower
CC expression in flowers. Expressed in the L1 layer of the shoot apex, in
CC the epidermis of leaf primordia and young leaves and in vascular
CC bundles. In the differentiation zone of the root, detected in the
CC pericycle and in the epidermis, but not in the cortex. Strongly
CC expressed in the lateral part of the root cap and in the epidermis of
CC the root tip, but not in the meristematic tissue. Not expressed in
CC lateral roots. In mature embryos, expressed in the epidermis, cotyledon
CC tips and root tips. {ECO:0000269|PubMed:15032866}.
CC -!- DEVELOPMENTAL STAGE: Strong reduction in expression levels in flowers
CC following fertilization. {ECO:0000269|PubMed:15032866}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18169.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81367.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB049628; BAB21522.1; -; mRNA.
DR EMBL; AL022197; CAA18169.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81367.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85078.1; -; Genomic_DNA.
DR EMBL; AY120730; AAM53288.1; -; mRNA.
DR EMBL; BT002176; AAN72187.1; -; mRNA.
DR EMBL; AY085603; AAM62824.1; -; mRNA.
DR PIR; E85295; E85295.
DR PIR; T05790; T05790.
DR RefSeq; NP_001328918.1; NM_001341751.1.
DR RefSeq; NP_567723.1; NM_118689.4.
DR AlphaFoldDB; Q8L856; -.
DR SMR; Q8L856; -.
DR BioGRID; 13949; 6.
DR IntAct; Q8L856; 4.
DR STRING; 3702.AT4G25570.1; -.
DR PaxDb; Q8L856; -.
DR PRIDE; Q8L856; -.
DR ProteomicsDB; 244357; -.
DR EnsemblPlants; AT4G25570.1; AT4G25570.1; AT4G25570.
DR GeneID; 828662; -.
DR Gramene; AT4G25570.1; AT4G25570.1; AT4G25570.
DR KEGG; ath:AT4G25570; -.
DR Araport; AT4G25570; -.
DR TAIR; locus:2131859; AT4G25570.
DR eggNOG; KOG1619; Eukaryota.
DR HOGENOM; CLU_069712_0_1_1; -.
DR InParanoid; Q8L856; -.
DR OrthoDB; 1503869at2759; -.
DR PhylomeDB; Q8L856; -.
DR BRENDA; 7.2.1.3; 399.
DR PRO; PR:Q8L856; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L856; baseline and differential.
DR Genevisible; Q8L856; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; IEA:UniProtKB-EC.
DR InterPro; IPR043205; CYB561/CYBRD1-like.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR10106; PTHR10106; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 1: Evidence at protein level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Vacuole.
FT CHAIN 1..239
FT /note="Transmembrane ascorbate ferrireductase 1"
FT /id="PRO_0000412907"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..45
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..119
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..193
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 13..216
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT REGION 217..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9SWS1"
FT BINDING 83
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9SWS1"
FT BINDING 117
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9SWS1"
FT BINDING 156
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q9SWS1"
FT MUTAGEN 83
FT /note="H->A: Disrupts high-potential heme; when associated
FT with A-156."
FT /evidence="ECO:0000269|PubMed:21236254"
FT MUTAGEN 83
FT /note="H->L: Disrupts high-potential heme; when associated
FT with L-156."
FT /evidence="ECO:0000269|PubMed:21236254"
FT MUTAGEN 156
FT /note="H->A: Disrupts high-potential heme; when associated
FT with A-83."
FT /evidence="ECO:0000269|PubMed:21236254"
FT MUTAGEN 156
FT /note="H->L: Disrupts high-potential heme; when associated
FT with L-83."
FT /evidence="ECO:0000269|PubMed:21236254"
FT CONFLICT 25..26
FT /note="Missing (in Ref. 1; BAB21522)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="N -> K (in Ref. 2; CAB81367)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..220
FT /note="Missing (in Ref. 5; AAM62824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 25865 MW; 889543868B994A13 CRC64;
MAVRINAMAV TFVAHALAVI AAIMVLVWSI SYRGGLAWEA TNKNLIFNLH PVLMLIGFII
LGGEAIISYK SLPLEKPVKK LIHLILHAIA LALGIFGICA AFKNHNESHI PNLYSLHSWI
GIGVISLYGF QWVYSFIVFF FPGGSTNLKS GLLPWHAMLG LFVYILAVGN AALGFLEKLT
FLENGGLDKY GSEAFLINFT AIITILFGAF VVLTASAESP SPSPSVSNDD SVDFSYSAI
