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B561C_ARATH
ID   B561C_ARATH             Reviewed;         393 AA.
AC   Q9LSE7;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Cytochrome b561 and DOMON domain-containing protein At3g25290;
DE   AltName: Full=Protein b561A.tha3;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g25290; ORFNames=MJL12_25;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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   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   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   [5]
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   [6]
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   [7]
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; AB026647; BAB02088.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77005.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77006.1; -; Genomic_DNA.
DR   EMBL; AY057704; AAL15334.1; -; mRNA.
DR   EMBL; BT002214; AAN72226.1; -; mRNA.
DR   RefSeq; NP_001030764.1; NM_001035687.1.
DR   RefSeq; NP_566763.1; NM_113435.3.
DR   AlphaFoldDB; Q9LSE7; -.
DR   SMR; Q9LSE7; -.
DR   BioGRID; 7454; 2.
DR   STRING; 3702.AT3G25290.1; -.
DR   iPTMnet; Q9LSE7; -.
DR   PaxDb; Q9LSE7; -.
DR   PRIDE; Q9LSE7; -.
DR   ProteomicsDB; 241188; -.
DR   EnsemblPlants; AT3G25290.1; AT3G25290.1; AT3G25290.
DR   EnsemblPlants; AT3G25290.2; AT3G25290.2; AT3G25290.
DR   GeneID; 822123; -.
DR   Gramene; AT3G25290.1; AT3G25290.1; AT3G25290.
DR   Gramene; AT3G25290.2; AT3G25290.2; AT3G25290.
DR   KEGG; ath:AT3G25290; -.
DR   Araport; AT3G25290; -.
DR   TAIR; locus:2090240; AT3G25290.
DR   eggNOG; KOG4293; Eukaryota.
DR   HOGENOM; CLU_036675_1_0_1; -.
DR   InParanoid; Q9LSE7; -.
DR   OMA; FTLATIQ; -.
DR   OrthoDB; 599276at2759; -.
DR   PhylomeDB; Q9LSE7; -.
DR   PRO; PR:Q9LSE7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LSE7; baseline and differential.
DR   Genevisible; Q9LSE7; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..393
FT                   /note="Cytochrome b561 and DOMON domain-containing protein
FT                   At3g25290"
FT                   /id="PRO_0000430474"
FT   TRANSMEM        219..239
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        360..380
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          48..168
FT                   /note="DOMON"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT   DOMAIN          184..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   393 AA;  42559 MW;  E3229A63BE01C55E CRC64;
     MSSSSSVRIS LSFIFLALLI SPAVSQTCKS QTFSGDKTYP HCLDLPQLKA FLHYSYDASN
     TTLAVVFSAP PAKPGGWIAW AINPKATGMV GSQTLVAYKD PGNGVAVVKT LNISSYSSLI
     PSKLAFDVWD MKAEEAARDG GSLRIFARVK VPADLVAKGK VNQVWQVGPE LGPGGMIGRH
     AFDSANLASM SSLDLKGDNS GGTISGGDEV NAKIKNRNIH GILNAVSWGI LFPIGAIIAR
     YMRVFDSADP AWFYLHVSCQ FSAYVIGVAG WATGLKLGNE SEGIRFSAHR NIGIALFTLA
     TIQMFAMLLR PKKDHKYRFY WNIYHHGVGY AILTLGIINV FKGLNILKPQ DTYKTAYIAV
     IAVLGGIALL LEAITWVVVL KRKSNNSMKP LRT
 
 
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