B561A_ARATH
ID B561A_ARATH Reviewed; 907 AA.
AC Q9FFU6;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytochrome b561, DM13 and DOMON domain-containing protein At5g54830;
DE AltName: Full=Protein b561A.tha1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g54830; ORFNames=MBG8_9;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
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; AB005232; BAB08762.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96545.1; -; Genomic_DNA.
DR EMBL; AY090233; AAL90897.1; -; mRNA.
DR EMBL; BT002628; AAO11544.1; -; mRNA.
DR EMBL; AK227031; BAE99093.1; -; mRNA.
DR RefSeq; NP_200294.1; NM_124864.5.
DR AlphaFoldDB; Q9FFU6; -.
DR SMR; Q9FFU6; -.
DR STRING; 3702.AT5G54830.1; -.
DR PaxDb; Q9FFU6; -.
DR PRIDE; Q9FFU6; -.
DR ProteomicsDB; 241117; -.
DR EnsemblPlants; AT5G54830.1; AT5G54830.1; AT5G54830.
DR GeneID; 835573; -.
DR Gramene; AT5G54830.1; AT5G54830.1; AT5G54830.
DR KEGG; ath:AT5G54830; -.
DR Araport; AT5G54830; -.
DR TAIR; locus:2160220; AT5G54830.
DR eggNOG; KOG4293; Eukaryota.
DR eggNOG; KOG4731; Eukaryota.
DR HOGENOM; CLU_340217_0_0_1; -.
DR InParanoid; Q9FFU6; -.
DR OMA; LTYVRCR; -.
DR OrthoDB; 599276at2759; -.
DR PhylomeDB; Q9FFU6; -.
DR PRO; PR:Q9FFU6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFU6; baseline and differential.
DR Genevisible; Q9FFU6; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd09631; DOMON_DOH; 2.
DR InterPro; IPR045879; B561A.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR InterPro; IPR019545; DM13_domain.
DR InterPro; IPR045266; DOH_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR PANTHER; PTHR47281; PTHR47281; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR Pfam; PF10517; DM13; 1.
DR SMART; SM00665; B561; 1.
DR SMART; SM00686; DM13; 1.
DR SMART; SM00664; DoH; 2.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
DR PROSITE; PS51549; DM13; 1.
DR PROSITE; PS50836; DOMON; 2.
PE 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..907
FT /note="Cytochrome b561, DM13 and DOMON domain-containing
FT protein At5g54830"
FT /id="PRO_0000430472"
FT TRANSMEM 685..705
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 730..750
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 754..774
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..849
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT DOMAIN 31..139
FT /note="DM13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00882"
FT DOMAIN 184..329
FT /note="DOMON 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 524..645
FT /note="DOMON 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT DOMAIN 653..850
FT /note="Cytochrome b561"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT REGION 144..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 689
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 723
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 754
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 796
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 907 AA; 100533 MW; 0F91E2660D56C4EA CRC64;
MCDQRPNLLG SLVLLGFFIF FVNGEECSNS SSLIGHESEF KMLQHQLRGV FTVVDDCSFR
VSRFDMLSGS EVHWWGAMSS DFDNMTNDGF VISDQKLNQT FKNSSFIVRL LGNVTWDKLG
VVSVWDLPTA SDFGHVLLSN ATESDTSKAE SPPSESNDVA PGKSNNSEPF KAPTMFDNCK
KLSDKYRLRW SLNAEKGYVD IGLEATTGLL NYMAFGWAKP NSTSNLMLNA DVVVTGIRED
GFPFADDFYI TESSVCSVKE GTATGVCPDT VYEEADSVGS SVNNTKLVYG HRIDGVSFVR
YRRPLNDSDN KFDFPVNSTE SLTVIWALGV IKPPDVINPY YLPVNHGGVE SENFGHFSLN
LSDHVDECLG PLDADNKYDQ DVIIADAHAP LVVTAGPSVH YPNPPNPSKV LYINKKEAPV
LKVERGVPVK FSIEAGHDVS FYITSDFLGG NASLRNRTET IYAGGQETHG VLSSPSELVW
APNRNTPDQL YYHSIFQEKM GWKVQVVDGG LSDMYNNSVN LDDQQVKFFW TIVGDSISIA
ARGEKKSGYL AIGFGSEMTN SYAYIGWFDR NGTGHVNTYW IDGESASAVH PTTENMTYVR
CKSEEGIITL EFTRPLKPSC SHRDRPECKN MIDPTTPLKV IWAMGAKWTD GQLTERNMHS
VTSQRPVRVM LTRGSAEADQ DLRPVLGVHG FMMFLAWGIL LPGGILSARY LKHIKGDGWF
KIHMYLQCSG LAIVFLGLLF AVAELNGFSF SSTHVKFGFT AIVLACAQPV NAWLRPAKPA
QGELISSKRL IWEYSHSIVG QSAVVVGVVA LFTGMKHLGE RNGTENVDGL NLALGLWVFL
CVVTVAYLEY RERGRRRARN LSRGNWVLGN VEEDDSIDLI DSRGGFRDKD DEDRNGGRME
IQLEPLK
