ACFR2_ARATH
ID ACFR2_ARATH Reviewed; 230 AA.
AC Q9SWS1; Q42137;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transmembrane ascorbate ferrireductase 2;
DE EC=7.2.1.3 {ECO:0000305|PubMed:24449903};
DE AltName: Full=Cytochrome b561-1;
DE Short=Artb561-2;
DE Short=AtCytb561;
DE AltName: Full=Protein b561A.tha4;
GN Name=CYB561B; Synonyms=ACYB-1, CYB-1, CYB561B2, CYBASC2, CYTB561;
GN OrderedLocusNames=At5g38630; ORFNames=MBB18.18;
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 [GENOMIC DNA].
RA Asard H., Terol-Alcayde J., Preger V., Del Favero J., Verelst W.,
RA Sparla F., Perez-Alonso M., Trost P.;
RT "Arabidopsis thaliana sequence analysis confirms the presence of cyt b-561
RT in plants: Evidence for a novel protein family.";
RL Plant Physiol. Biochem. 38:905-912(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-75.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RA Desprez T., Amselem J., Chiapello H., Caboche M., Hofte H.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [9]
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 [10]
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 [11]
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH ASCORBATE;
RP MONODEHYDROASCORBATE AND HEME, COFACTOR, SUBUNIT, MUTAGENESIS OF LYS-81;
RP PHE-105; HIS-106 AND ARG-150, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RX PubMed=24449903; DOI=10.1073/pnas.1323931111;
RA Lu P., Ma D., Yan C., Gong X., Du M., Shi Y.;
RT "Structure and mechanism of a eukaryotic transmembrane ascorbate-dependent
RT oxidoreductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:1813-1818(2014).
CC -!- FUNCTION: Two-heme-containing cytochrome (PubMed:24449903). Catalyzes
CC ascorbate-dependent transmembrane ferric-chelate reduction (Probable).
CC {ECO:0000269|PubMed:24449903, ECO:0000305|PubMed:24449903}.
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:0000305|PubMed:24449903};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:24449903};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000269|PubMed:24449903};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24449903}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:24449903}; Multi-
CC pass membrane protein {ECO:0000305|PubMed:24449903}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, leaves and flowers.
CC Expressed in the L1 layer of the shoot apex, in the epidermis of leaf
CC primordia and young leaves and in vascular bundles. In the
CC differentiation zone of the root, detected in the pericycle and in the
CC epidermis, but not in the cortex. Strongly expressed in the cortical
CC region of the root tip, in the meristematic tissue and in the epidermal
CC cell layer of lateral roots, but not in the root caps. Highly expressed
CC in unfertilized ovules. In mature embryos, expressed in the epidermis,
CC cotyledon 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}.
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DR EMBL; AF132115; AAD45585.1; -; Genomic_DNA.
DR EMBL; AB049627; BAB21521.1; -; mRNA.
DR EMBL; AB005231; BAB10153.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94343.1; -; Genomic_DNA.
DR EMBL; BT024611; ABD43009.1; -; mRNA.
DR EMBL; AY085028; AAM61586.1; -; mRNA.
DR EMBL; AK117270; BAC41943.1; -; mRNA.
DR EMBL; Z26702; CAA81401.1; -; mRNA.
DR RefSeq; NP_198679.1; NM_123224.3.
DR PDB; 4O6Y; X-ray; 1.70 A; A/B=1-230.
DR PDB; 4O79; X-ray; 2.00 A; A/B=1-230.
DR PDB; 4O7G; X-ray; 2.21 A; A/B=1-230.
DR PDBsum; 4O6Y; -.
DR PDBsum; 4O79; -.
DR PDBsum; 4O7G; -.
DR AlphaFoldDB; Q9SWS1; -.
DR SMR; Q9SWS1; -.
DR STRING; 3702.AT5G38630.1; -.
DR PaxDb; Q9SWS1; -.
DR PRIDE; Q9SWS1; -.
DR ProteomicsDB; 244342; -.
DR EnsemblPlants; AT5G38630.1; AT5G38630.1; AT5G38630.
DR GeneID; 833853; -.
DR Gramene; AT5G38630.1; AT5G38630.1; AT5G38630.
DR KEGG; ath:AT5G38630; -.
DR Araport; AT5G38630; -.
DR TAIR; locus:2159858; AT5G38630.
DR eggNOG; KOG1619; Eukaryota.
DR HOGENOM; CLU_069712_0_1_1; -.
DR InParanoid; Q9SWS1; -.
DR OMA; SAEFNWH; -.
DR OrthoDB; 1503869at2759; -.
DR PhylomeDB; Q9SWS1; -.
DR BRENDA; 7.2.1.3; 399.
DR PRO; PR:Q9SWS1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SWS1; baseline and differential.
DR Genevisible; Q9SWS1; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IDA:TAIR.
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 3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..230
FT /note="Transmembrane ascorbate ferrireductase 2"
FT /id="PRO_0000412908"
FT TRANSMEM 5..25
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT DOMAIN 14..218
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 51
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:0000269|PubMed:24449903"
FT BINDING 77
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:24449903"
FT BINDING 81
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:24449903"
FT BINDING 84
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:0000269|PubMed:24449903"
FT BINDING 105
FT /ligand="monodehydro-L-ascorbate radical"
FT /ligand_id="ChEBI:CHEBI:59513"
FT /evidence="ECO:0000269|PubMed:24449903"
FT BINDING 106
FT /ligand="monodehydro-L-ascorbate radical"
FT /ligand_id="ChEBI:CHEBI:59513"
FT /evidence="ECO:0000269|PubMed:24449903"
FT BINDING 115
FT /ligand="monodehydro-L-ascorbate radical"
FT /ligand_id="ChEBI:CHEBI:59513"
FT /evidence="ECO:0000269|PubMed:24449903"
FT BINDING 118
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:0000269|PubMed:24449903"
FT BINDING 140
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:24449903"
FT BINDING 150
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:24449903"
FT BINDING 151
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000269|PubMed:24449903"
FT BINDING 157
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:0000269|PubMed:24449903"
FT BINDING 182
FT /ligand="monodehydro-L-ascorbate radical"
FT /ligand_id="ChEBI:CHEBI:59513"
FT /evidence="ECO:0000269|PubMed:24449903"
FT BINDING 186
FT /ligand="monodehydro-L-ascorbate radical"
FT /ligand_id="ChEBI:CHEBI:59513"
FT /evidence="ECO:0000269|PubMed:24449903"
FT MUTAGEN 81
FT /note="K->A: Abrogates electron transfer; when associated
FT with W-105/E-106/A-150."
FT /evidence="ECO:0000269|PubMed:24449903"
FT MUTAGEN 105
FT /note="F->W: Abrogates electron transfer; when associated
FT with A-81/E-106/A-150."
FT /evidence="ECO:0000269|PubMed:24449903"
FT MUTAGEN 106
FT /note="H->E: Abrogates electron transfer; when associated
FT with A-81/W-105/A-150."
FT /evidence="ECO:0000269|PubMed:24449903"
FT MUTAGEN 150
FT /note="R->A: Abrogates electron transfer; when associated
FT with A-81/W-105/E-106."
FT /evidence="ECO:0000269|PubMed:24449903"
FT HELIX 11..31
FT /evidence="ECO:0007829|PDB:4O6Y"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:4O6Y"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:4O6Y"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:4O6Y"
FT HELIX 77..109
FT /evidence="ECO:0007829|PDB:4O6Y"
FT HELIX 117..140
FT /evidence="ECO:0007829|PDB:4O6Y"
FT HELIX 147..185
FT /evidence="ECO:0007829|PDB:4O6Y"
FT HELIX 194..218
FT /evidence="ECO:0007829|PDB:4O6Y"
SQ SEQUENCE 230 AA; 25289 MW; 544F69F682C9D259 CRC64;
MAVPVLGGFP IFMVVRVLGF IIAALVLTWT VHYRGGLALS SDNKDHIFNV HPVMMVIGLI
LFNGEAMLAY KSVQGTKNLK KLVHLTLQLT AFILSLIGVW AALKFHIDKG IENFYSLHSW
LGLACLFLFA FQWAAGFVTY WYPGGSRNSR ASLMPWHVFL GISIYALALV TATTGILEKV
TFLQVNQVIT RYSTEAMLVN TMGVLILILG GFVILGVVTP VSGKDQVLTQ
