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 24-JUL-2024, entry version 123. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q9M363; -. DR iPTMnet; Q9M363; -. DR PaxDb; 3702-AT3G61750-1; -. 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; AT3G61750; -. DR eggNOG; KOG4293; Eukaryota. DR HOGENOM; CLU_036675_0_1_1; -. DR InParanoid; Q9M363; -. DR OMA; LYHSWFG; -. DR OrthoDB; 469478at2759; -. DR PhylomeDB; Q9M363; -. DR PRO; PR:Q9M363; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9M363; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd08760; Cyt_b561_FRRS1_like; 1. DR CDD; cd09631; DOMON_DOH; 1. DR Gene3D; 1.20.120.1770; -; 1. DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM. DR InterPro; IPR045266; DOH_DOMON. DR InterPro; IPR005018; DOMON_domain. DR PANTHER; PTHR23130; CYTOCHROME B561 AND DOMON DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR23130:SF115; MEMBRANE PROTEIN-LIKE; 1. DR Pfam; PF03188; Cytochrom_B561; 1. DR Pfam; PF03351; DOMON; 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 //