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B561I_ARATH
ID   B561I_ARATH             Reviewed;         398 AA.
AC   Q9M363;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Cytochrome b561 and DOMON domain-containing protein At3g61750;
DE   AltName: Full=Protein b561A.tha9;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g61750; ORFNames=F15G16.140, F21F14.14;
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   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   [4]
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   [5]
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   [6]
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; AL132959; CAB71105.1; -; Genomic_DNA.
DR   EMBL; AL138642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002686; AEE80252.1; -; Genomic_DNA.
DR   PIR; T47967; T47967.
DR   RefSeq; NP_191734.1; NM_116040.2.
DR   AlphaFoldDB; Q9M363; -.
DR   SMR; Q9M363; -.
DR   BioGRID; 10662; 14.
DR   IntAct; Q9M363; 14.
DR   STRING; 3702.AT3G61750.1; -.
DR   PaxDb; Q9M363; -.
DR   PRIDE; Q9M363; -.
DR   ProteomicsDB; 241191; -.
DR   EnsemblPlants; AT3G61750.1; AT3G61750.1; AT3G61750.
DR   GeneID; 825348; -.
DR   Gramene; AT3G61750.1; AT3G61750.1; AT3G61750.
DR   KEGG; ath:AT3G61750; -.
DR   Araport; AT3G61750; -.
DR   TAIR; locus:2076770; AT3G61750.
DR   eggNOG; KOG4293; Eukaryota.
DR   HOGENOM; CLU_036675_0_1_1; -.
DR   InParanoid; Q9M363; -.
DR   OMA; DGMMLNS; -.
DR   OrthoDB; 599276at2759; -.
DR   PhylomeDB; Q9M363; -.
DR   PRO; PR:Q9M363; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M363; baseline and differential.
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   Pfam; PF03188; Cytochrom_B561; 1.
DR   SMART; SM00665; B561; 1.
DR   SMART; SM00664; DoH; 1.
DR   PROSITE; PS50939; CYTOCHROME_B561; 1.
DR   PROSITE; PS50836; DOMON; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..398
FT                   /note="Cytochrome b561 and DOMON domain-containing protein
FT                   At3g61750"
FT                   /id="PRO_0000430477"
FT   TRANSMEM        222..242
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          64..177
FT                   /note="DOMON"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT   DOMAIN          184..377
FT                   /note="Cytochrome b561"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT   BINDING         220
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         253
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         285
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         321
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   398 AA;  44466 MW;  3715E3D14941623B CRC64;
     MKTLVGFYIL CFLIGQDLPF LAADDVNVIN DSTQNLCFAN RLSDFLPPPY SNISDNMPCT
     PLWNTFVLRY SENRDNVMTI IVSALYTTGW VGIGFSKEGR MVGSSAMIGW ISKKGHAKIK
     QYYLQGTERD QVVPDQGELQ LQKVPPVVAL HGAMIYLAFQ VKFAVRVPRR AVILAFSTAY
     PSKLGRLTKH DDKTTVIVDF SKASGATSIK TTTSTEKTKH GVMAILGWGF LLPVGAILAR
     YLRHKDPLWY YLHIGFQFTG FIFGLAAVIL GIQLYNRIQP DIPAHRGIGI FLLVLSTLQV
     LAFFARPQKE TKMRRYWNWY HHWIGRISLF FGAVNIVLGI RMADNGGDGW KIGYGFVLSV
     TLLAFVVLEI FRIRGTIGSP SSRSPPSFET HPSSSTSV
 
 
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