B561J_ARATH
ID B561J_ARATH Reviewed; 395 AA.
AC Q9FGK4;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cytochrome b561 and DOMON domain-containing protein At5g47530;
DE AltName: Full=Protein b561A.tha10;
DE Flags: Precursor;
GN OrderedLocusNames=At5g47530; ORFNames=MNJ7.12;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DOMAIN, AND FUNCTION.
RX PubMed=15022831; DOI=10.1078/0176-1617-01064;
RA Verelst W., Asard H.;
RT "Analysis of an Arabidopsis thaliana protein family, structurally related
RT to cytochromes b561 and potentially involved in catecholamine biochemistry
RT in plants.";
RL J. Plant Physiol. 161:175-181(2004).
RN [6]
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 [7]
RP DOMAIN.
RX PubMed=19386804; DOI=10.1104/pp.109.139170;
RA Preger V., Tango N., Marchand C., Lemaire S.D., Carbonera D.,
RA Di Valentin M., Costa A., Pupillo P., Trost P.;
RT "Auxin-responsive genes AIR12 code for a new family of plasma membrane b-
RT type cytochromes specific to flowering plants.";
RL Plant Physiol. 150:606-620(2009).
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: May act as a catecholamine-responsive trans-membrane electron
CC transporter. {ECO:0000269|PubMed:15022831}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: DOMON domain could bind catecholamines and thereby could
CC regulate the cytochrome b561 domain function (PubMed:15022831). DOMON
CC domain could bind one heme b (PubMed:19386804).
CC {ECO:0000269|PubMed:15022831, ECO:0000269|PubMed:19386804}.
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DR EMBL; AB025628; BAB09079.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95529.1; -; Genomic_DNA.
DR EMBL; BT012551; AAS99695.1; -; mRNA.
DR EMBL; AK176454; BAD44217.1; -; mRNA.
DR RefSeq; NP_199564.1; NM_124126.3.
DR AlphaFoldDB; Q9FGK4; -.
DR BioGRID; 20051; 47.
DR IntAct; Q9FGK4; 46.
DR STRING; 3702.AT5G47530.1; -.
DR PaxDb; Q9FGK4; -.
DR ProteomicsDB; 241192; -.
DR EnsemblPlants; AT5G47530.1; AT5G47530.1; AT5G47530.
DR GeneID; 834803; -.
DR Gramene; AT5G47530.1; AT5G47530.1; AT5G47530.
DR KEGG; ath:AT5G47530; -.
DR Araport; AT5G47530; -.
DR TAIR; locus:2168948; AT5G47530.
DR eggNOG; KOG4293; Eukaryota.
DR HOGENOM; CLU_036675_1_0_1; -.
DR InParanoid; Q9FGK4; -.
DR OMA; EAYTWFL; -.
DR OrthoDB; 599276at2759; -.
DR PhylomeDB; Q9FGK4; -.
DR PRO; PR:Q9FGK4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGK4; baseline and differential.
DR Genevisible; Q9FGK4; 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 CDD; cd09629; DOMON_CIL1_like; 1.
DR InterPro; IPR045265; AIR12_DOMON.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR017214; UCP037471.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR Pfam; PF04526; DUF568; 1.
DR PIRSF; PIRSF037471; UCP037471; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
DR PROSITE; PS50836; DOMON; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..395
FT /note="Cytochrome b561 and DOMON domain-containing protein
FT At5g47530"
FT /id="PRO_0000430478"
FT TRANSMEM 210..230
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT DOMAIN 47..162
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 176..371
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 211
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 247
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 280
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 316
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 395 AA; 42998 MW; B04ED689DD72DAFC CRC64;
MAISSNLLLC LSLFIFIITK SALAQKCSNY KFSTNRLFES CNDLPVLDSF LHYTYDSSSG
NLQIAYRHTK LTPGKWVAWA VNPTSTGMVG AQAIVAYPQS DGTVRAYTSP ISSYQTSLLE
AELSFNVSQL SATYQNNEMV IYAILNLPLA NGGIINTVWQ DGSLSGNNPL PHPTSGNNVR
SVSTLNLVSG ASGSTSTGAG GASKLRKRNI HGILNGVSWG IMMPIGAIIA RYLKVSKSAD
PAWFYLHVFC QSSAYIIGVA GWATGLKLGN ESAGIQFTFH RAVGIALFCL ATIQVFAMFL
RPKPEHKYRV YWNIYHHTVG YSVIILAVVN VFKGLDILSP EKQWRNAYTA IIVVLGIVAV
VLEGFTWYVV IKRGKAEASA KTSQRVGNDG RSLYV
