B561H_ARATH
ID B561H_ARATH Reviewed; 466 AA.
AC Q9LYS9;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytochrome b561 and DOMON domain-containing protein At3g59070;
DE AltName: Full=Protein b561A.tha8;
DE Flags: Precursor;
GN OrderedLocusNames=At3g59070; ORFNames=F17J16_120;
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; AL163527; CAB86935.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79872.1; -; Genomic_DNA.
DR PIR; T47789; T47789.
DR RefSeq; NP_191466.1; NM_115769.1.
DR AlphaFoldDB; Q9LYS9; -.
DR PaxDb; Q9LYS9; -.
DR PRIDE; Q9LYS9; -.
DR EnsemblPlants; AT3G59070.1; AT3G59070.1; AT3G59070.
DR GeneID; 825076; -.
DR Gramene; AT3G59070.1; AT3G59070.1; AT3G59070.
DR KEGG; ath:AT3G59070; -.
DR Araport; AT3G59070; -.
DR TAIR; locus:2077690; AT3G59070.
DR eggNOG; KOG4293; Eukaryota.
DR HOGENOM; CLU_036675_1_0_1; -.
DR InParanoid; Q9LYS9; -.
DR OMA; ICCIAAF; -.
DR OrthoDB; 599276at2759; -.
DR PhylomeDB; Q9LYS9; -.
DR PRO; PR:Q9LYS9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYS9; baseline and differential.
DR Genevisible; Q9LYS9; 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 Pfam; PF03188; Cytochrom_B561; 1.
DR Pfam; PF04526; DUF568; 1.
DR SMART; SM00665; B561; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..466
FT /note="Cytochrome b561 and DOMON domain-containing protein
FT At3g59070"
FT /id="PRO_0000430476"
FT TRANSMEM 219..239
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 327..347
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT DOMAIN 57..172
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 179..380
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 256
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 289
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 325
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 466 AA; 52008 MW; 1503BAC1B29C3385 CRC64;
MSLSSRATLV VLCCLFMLIP SFTTAATEQG LHARSRCESY SFNNGKSFRS CTDLLVLNSY
LHFNYAQETG VLEIAYHHSN LESSSWISWA INPTSKGMVG AQALVAYRNS TSGVMRAYTS
SINSYSPMLQ ESPLSLRVTQ VSAEYSNGEM MIFATLVLPP NTTVVNHLWQ DGPLKEGDRL
GMHAMSGDNL KSMASLDLLS GQVTTTKSVN RNMLLVKQIH AIVNALSWGI LMPIGVMAAR
YMKNYEVLDP TWFYIHVVCQ TTGYFSGLIG GLGTAIYMAR HTGMRTTLHT VIGLLLFALG
FLQILSLKAR PNKDHKYRKY WNWYHHTMGY IVIVLSIYNI YKGLSILQPG SIWKIAYTTI
ICCIAAFAVV MEILQFKKRW ARLFFKKSKD VEADQPTVSV DVIGETEKAE RKKASGGIEI
QIENYNITKN FMIPSVFVIS YPHTSPPLLA FHSYHHPSTS IAATAA
