ACFR4_ARATH
ID ACFR4_ARATH Reviewed; 236 AA.
AC Q9C540;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable transmembrane ascorbate ferrireductase 4;
DE EC=7.2.1.3 {ECO:0000250|UniProtKB:Q8L856};
DE AltName: Full=Artb561-4;
DE AltName: Full=Cytochrome b-561D;
DE AltName: Full=Protein b561A.tha6;
GN Name=CYB561D; OrderedLocusNames=At1g26100; ORFNames=F14G11.7, F28B23.22;
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 Sparla F., Preger V., Trost P.;
RT "Molecular cloning of cytochrome b-561D from Arabidopsis thaliana.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 [5]
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 [6]
RP IDENTIFICATION, AND NOMENCLATURE.
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 [7]
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 [8]
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).
CC -!- FUNCTION: Two-heme-containing cytochrome. May catalyze ascorbate-
CC dependent trans-membrane ferric-chelate reduction (By similarity).
CC {ECO:0000250}.
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:0000250|UniProtKB:Q8L856};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q9SWS1};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:Q9SWS1};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9SWS1}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8L856}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q8L856}.
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DR EMBL; AY114120; AAM63528.1; -; mRNA.
DR EMBL; AC079829; AAG50673.1; -; Genomic_DNA.
DR EMBL; AC084221; AAG50524.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30648.1; -; Genomic_DNA.
DR EMBL; BT024618; ABD43016.1; -; mRNA.
DR PIR; A86387; A86387.
DR RefSeq; NP_173935.1; NM_102375.3.
DR AlphaFoldDB; Q9C540; -.
DR SMR; Q9C540; -.
DR STRING; 3702.AT1G26100.1; -.
DR PaxDb; Q9C540; -.
DR PRIDE; Q9C540; -.
DR ProteomicsDB; 244524; -.
DR EnsemblPlants; AT1G26100.1; AT1G26100.1; AT1G26100.
DR GeneID; 839151; -.
DR Gramene; AT1G26100.1; AT1G26100.1; AT1G26100.
DR KEGG; ath:AT1G26100; -.
DR Araport; AT1G26100; -.
DR TAIR; locus:2011425; AT1G26100.
DR eggNOG; KOG1619; Eukaryota.
DR HOGENOM; CLU_069712_0_1_1; -.
DR InParanoid; Q9C540; -.
DR OMA; IFGIWTR; -.
DR OrthoDB; 1503869at2759; -.
DR PhylomeDB; Q9C540; -.
DR PRO; PR:Q9C540; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C540; baseline and differential.
DR Genevisible; Q9C540; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..236
FT /note="Probable transmembrane ascorbate ferrireductase 4"
FT /id="PRO_0000412910"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT DOMAIN 14..210
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 44
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 77
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 110
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 149
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"
SQ SEQUENCE 236 AA; 26307 MW; 55E1ABBC4DEFF05F CRC64;
MGSVDPSRLS LVLFARLSGL VVAVSVLYWA LFLPNLGLSY STLHPLLMVI GFILVSGEAI
LIHRWLPGSR KTKKAVHLWL QGMALASAVF GIWTKFHYQR GVFANFYSLH SWMGLLSVSL
FAAQWVTGFM SFWHRGEVRT TRTTFLPWHV FLGLYTYGLA IATAETGLLE KLTFLQTKRN
VPRRGSESMT VNGLGLGLAL LGCIVITAAI LPKYQSHSRD EKLVYSSQDR PKCLSS
