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B561G_ARATH
ID   B561G_ARATH             Reviewed;         404 AA.
AC   Q9SJ74; Q4PL86; Q8LFW0;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Cytochrome b561 and DOMON domain-containing protein At2g04850;
DE   AltName: Full=Protein b561A.tha7;
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g04850; ORFNames=F28I8.9;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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;
RA   Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-404.
RC   STRAIN=cv. Columbia;
RX   PubMed=12481096; DOI=10.1104/pp.010207;
RA   Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT   "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT   of Arabidopsis.";
RL   Plant Physiol. 130:2118-2128(2002).
RN   [6]
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   [7]
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   [8]
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   [9]
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAY82261.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC006955; AAD22321.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05876.1; -; Genomic_DNA.
DR   EMBL; BT025973; ABG25062.1; -; mRNA.
DR   EMBL; AY084618; AAM61181.1; -; mRNA.
DR   EMBL; DQ069802; AAY82261.1; ALT_INIT; mRNA.
DR   PIR; C84462; C84462.
DR   RefSeq; NP_565316.1; NM_126517.3.
DR   AlphaFoldDB; Q9SJ74; -.
DR   STRING; 3702.AT2G04850.1; -.
DR   PaxDb; Q9SJ74; -.
DR   PRIDE; Q9SJ74; -.
DR   ProteomicsDB; 241189; -.
DR   EnsemblPlants; AT2G04850.1; AT2G04850.1; AT2G04850.
DR   GeneID; 815031; -.
DR   Gramene; AT2G04850.1; AT2G04850.1; AT2G04850.
DR   KEGG; ath:AT2G04850; -.
DR   Araport; AT2G04850; -.
DR   TAIR; locus:2049254; AT2G04850.
DR   eggNOG; KOG4293; Eukaryota.
DR   HOGENOM; CLU_036675_1_1_1; -.
DR   InParanoid; Q9SJ74; -.
DR   OMA; YVHAGIQ; -.
DR   OrthoDB; 599276at2759; -.
DR   PhylomeDB; Q9SJ74; -.
DR   PRO; PR:Q9SJ74; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJ74; baseline and differential.
DR   Genevisible; Q9SJ74; 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   InterPro; IPR017214; UCP037471.
DR   Pfam; PF03188; Cytochrom_B561; 1.
DR   Pfam; PF04526; DUF568; 1.
DR   PIRSF; PIRSF037471; UCP037471; 1.
DR   SMART; SM00665; B561; 1.
DR   PROSITE; PS50939; CYTOCHROME_B561; 1.
DR   PROSITE; PS50836; DOMON; 1.
PE   2: Evidence at transcript level;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..404
FT                   /note="Cytochrome b561 and DOMON domain-containing protein
FT                   At2g04850"
FT                   /id="PRO_0000430475"
FT   TRANSMEM        217..237
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..173
FT                   /note="DOMON"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT   DOMAIN          180..380
FT                   /note="Cytochrome b561"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00242"
FT   BINDING         219
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         255
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         288
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         324
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   CONFLICT        45
FT                   /note="A -> T (in Ref. 4; AAM61181)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   404 AA;  43876 MW;  AA26C0812204A777 CRC64;
     MATLILSFLL LLLATKLPES LAGHCTTTTA TKSFEKCISL PTQQASIAWT YHPHNATLDL
     CFFGTFISPS GWVGWGINPD SPAQMTGSRV LIAFPDPNSG QLILLPYVLD SSVKLQKGPL
     LSRPLDLVRL SSSSASLYGG KMATIRNGAS VQIYASVKLS SNNTKIHHVW NRGLYVQGYS
     PTIHPTTSTD LSSFSTFDVT SGFATVNQNS GSRALKVTHG VVNAISWGFL LPAGAVTARY
     LRQMQSIGPT WFYIHAAIQL TGFLLGTIGF SIGIVLGHNS PGVTYGLHRS LGIATFTAAA
     LQTLALLFRP KTTNKFRRYW KSYHHFVGYA CVVMGVVNVF QGFEVLREGR SYAKLGYCLC
     LSTLVGVCVA MEVNSWVVFC RKAKEEKMKR DGLTGVDRCS GSHS
 
 
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