B561K_ARATH
ID B561K_ARATH Reviewed; 369 AA.
AC Q0WRW8; Q9SSF3;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cytochrome b561 and DOMON domain-containing protein At3g07570;
DE AltName: Full=Protein b561A.tha11;
DE Flags: Precursor;
GN OrderedLocusNames=At3g07570; ORFNames=MLP3.2;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF13075.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009176; AAF13075.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74567.1; -; Genomic_DNA.
DR EMBL; AK228175; BAF00131.1; -; mRNA.
DR RefSeq; NP_566313.2; NM_111636.3.
DR AlphaFoldDB; Q0WRW8; -.
DR SMR; Q0WRW8; -.
DR BioGRID; 5283; 3.
DR STRING; 3702.AT3G07570.1; -.
DR TCDB; 5.B.2.2.2; the eukaryotic cytochrome b561 (cytb561) family.
DR PaxDb; Q0WRW8; -.
DR PRIDE; Q0WRW8; -.
DR ProteomicsDB; 241193; -.
DR EnsemblPlants; AT3G07570.1; AT3G07570.1; AT3G07570.
DR GeneID; 819948; -.
DR Gramene; AT3G07570.1; AT3G07570.1; AT3G07570.
DR KEGG; ath:AT3G07570; -.
DR Araport; AT3G07570; -.
DR TAIR; locus:2091097; AT3G07570.
DR eggNOG; KOG4293; Eukaryota.
DR HOGENOM; CLU_036675_0_2_1; -.
DR InParanoid; Q0WRW8; -.
DR OMA; DKQSKYR; -.
DR OrthoDB; 599276at2759; -.
DR PRO; PR:Q0WRW8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WRW8; baseline and differential.
DR Genevisible; Q0WRW8; 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; cd09631; DOMON_DOH; 1.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR InterPro; IPR045266; DOH_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR017214; UCP037471.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR PIRSF; PIRSF037471; UCP037471; 1.
DR SMART; SM00665; B561; 1.
DR SMART; SM00664; DoH; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..369
FT /note="Cytochrome b561 and DOMON domain-containing protein
FT At3g07570"
FT /id="PRO_0000430479"
FT TRANSMEM 212..232
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT DOMAIN 55..167
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 174..369
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT BINDING 213
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 246
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 279
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 315
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 369 AA; 40444 MW; BA1E1A1CF28C2C70 CRC64;
MKLYSVSIII FVLIALSTIV NAQQAATDSC NSTLPLNDLT FNTSLLQCTE AWTPQNFILR
YARTAENTWS FILSAPDSSA FIGIGFSTNG QMIGSSAIVG WIPSDGGSGT VKPYLLGGKS
PGEVNPDQGD LTIVNGSLKI ESVSSRLYMR FQLTATLPRQ SLLYAVGPAG FFPSSPDFRL
REHRFVTTTT INYNTGSQSV VKVSPHSKLK KTHGLMNMFG WGILIIVGAI VARHMKQWDP
TWFYAHIALQ TTGFLLGLTG VICGLVLENR LKANNVSKHK GLGITILVMG VLQMLALLAR
PDKQSKYRKY WNWYHHNIGR LLIILAISNI FYGIHLAKAG TSWNGGYGFA VAVLALTAIG
LEVRKFLKK
