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 01-APR-2015, entry version 77. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA 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., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA 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 RT thaliana."; RL Nature 408:820-822(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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 RT related to cytochromes b561 and potentially involved in catecholamine RT biochemistry 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 RT b-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 RT transport."; RL Antioxid. Redox Signal. 19:1026-1035(2013). CC -!- FUNCTION: May act as a catecholamine-responsive trans-membrane CC electron transporter. {ECO:0000269|PubMed:15022831}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; CC Note=Binds 2 heme groups non-covalently. {ECO:0000250}; 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). CC DOMON domain could bind one heme b (PubMed:19386804). CC {ECO:0000269|PubMed:15022831, ECO:0000269|PubMed:19386804}. CC -!- SIMILARITY: Contains 1 cytochrome b561 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00242}. CC -!- SIMILARITY: Contains 1 DOMON domain. {ECO:0000255|PROSITE- CC ProRule:PRU00246}. 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_116040.1. DR UniGene; At.50302; -. DR ProteinModelPortal; Q9M363; -. DR SMR; Q9M363; 214-341. DR PRIDE; Q9M363; -. DR EnsemblPlants; AT3G61750.1; AT3G61750.1; AT3G61750. DR GeneID; 825348; -. DR KEGG; ath:AT3G61750; -. DR TAIR; AT3G61750; -. DR eggNOG; NOG281275; -. DR HOGENOM; HOG000238174; -. DR InParanoid; Q9M363; -. DR OMA; IVARYCR; -. DR PhylomeDB; Q9M363; -. DR Proteomes; UP000006548; Chromosome 3. DR Genevestigator; Q9M363; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM. DR InterPro; IPR004877; Cyt_b561_dom. DR InterPro; IPR005018; DOMON_domain. 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 Complete proteome; Electron transport; Heme; Iron; Membrane; KW Metal-binding; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Transport. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 398 Cytochrome b561 and DOMON domain- FT containing protein At3g61750. FT /FTId=PRO_0000430477. FT TRANSMEM 222 242 Helical; Name=1. {ECO:0000255}. FT TRANSMEM 252 272 Helical; Name=2. {ECO:0000255}. FT TRANSMEM 287 307 Helical; Name=3. {ECO:0000255}. FT TRANSMEM 320 340 Helical; Name=4. {ECO:0000255}. FT TRANSMEM 351 371 Helical; Name=5. {ECO:0000255}. FT DOMAIN 64 177 DOMON. {ECO:0000255|PROSITE- FT ProRule:PRU00246}. FT DOMAIN 184 377 Cytochrome b561. {ECO:0000255|PROSITE- FT ProRule:PRU00242}. FT METAL 220 220 Iron (heme axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00242}. FT METAL 253 253 Iron (heme axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00242}. FT METAL 285 285 Iron (heme axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00242}. FT METAL 321 321 Iron (heme axial ligand). FT {ECO:0000255|PROSITE-ProRule:PRU00242}. 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 //