B561O_ARATH
ID B561O_ARATH Reviewed; 394 AA.
AC Q9SV71; Q8L9T0;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cytochrome b561 and DOMON domain-containing protein At4g12980;
DE AltName: Full=Protein b561A.tha15;
DE Flags: Precursor;
GN OrderedLocusNames=At4g12980; ORFNames=F25G13.70;
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;
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 [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;
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 [4]
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 [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; AL079349; CAB45497.1; -; Genomic_DNA.
DR EMBL; AL161535; CAB78340.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83210.1; -; Genomic_DNA.
DR EMBL; BT003827; AAO41879.1; -; mRNA.
DR EMBL; BT005128; AAO50661.1; -; mRNA.
DR EMBL; AY088240; AAM65781.1; -; mRNA.
DR PIR; T10200; T10200.
DR RefSeq; NP_193034.1; NM_117367.3.
DR AlphaFoldDB; Q9SV71; -.
DR BioGRID; 12207; 2.
DR IntAct; Q9SV71; 2.
DR STRING; 3702.AT4G12980.1; -.
DR PaxDb; Q9SV71; -.
DR PRIDE; Q9SV71; -.
DR ProteomicsDB; 241196; -.
DR EnsemblPlants; AT4G12980.1; AT4G12980.1; AT4G12980.
DR GeneID; 826910; -.
DR Gramene; AT4G12980.1; AT4G12980.1; AT4G12980.
DR KEGG; ath:AT4G12980; -.
DR Araport; AT4G12980; -.
DR TAIR; locus:2123271; AT4G12980.
DR eggNOG; KOG4293; Eukaryota.
DR HOGENOM; CLU_036675_1_1_1; -.
DR InParanoid; Q9SV71; -.
DR OMA; WAINPKS; -.
DR OrthoDB; 599276at2759; -.
DR PhylomeDB; Q9SV71; -.
DR PRO; PR:Q9SV71; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SV71; baseline and differential.
DR Genevisible; Q9SV71; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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..394
FT /note="Cytochrome b561 and DOMON domain-containing protein
FT At4g12980"
FT /id="PRO_0000430482"
FT TRANSMEM 220..240
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT DOMAIN 49..169
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 184..381
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 221
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 257
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 290
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 326
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 CONFLICT 266
FT /note="V -> A (in Ref. 4; AAM65781)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="C -> S (in Ref. 4; AAM65781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 42229 MW; 9D1A51E8BA329FD4 CRC64;
MDSSYLRISL SFLFWALLLS PAVSQSSSCS SQTFSGVKSY PHCLDLPDLK AILHYSYDAS
NTTLAVVFSA PPSKPGGWIA WAINPKSTGM AGSQALVASK DPSTGVASVT TLNIVSYSSL
VPSKLSFDVW DVKAEEAAND GGALRIFAKV KVPADLAASG KVNQVWQVGP GVSNGRIQAH
DFSGPNLNSV GSLDLTGTTP GVPVSGGGGA GNSRIHKRNI HGILNAVSWG LLFPIGAMIA
RYMRIFESAD PAWFYLHVSC QFSAYVIGVA GWATGLKLGS ESKGIQYNTH RNIGICLFSI
ATLQMFAMLL RPRKDHKFRF VWNIYHHGVG YSILILGIIN VFKGLSILNP KHTYKTAYIA
VIGTLGGITL LLEVVTWVIV LKRKSAKSTK PLKA
