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B651B_ARATH
ID   B651B_ARATH             Reviewed;         402 AA.
AC   Q8VYH6; O23571;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Cytochrome b561 and DOMON domain-containing protein At4g17280;
DE   AltName: Full=Protein b561A.tha2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g17280; ORFNames=dl4675c, FCAALL.393;
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=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
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   [4]
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   [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   -!- SEQUENCE CAUTION:
CC       Sequence=CAB10509.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78731.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Z97343; CAB10509.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161546; CAB78731.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE83873.1; -; Genomic_DNA.
DR   EMBL; AY072011; AAL57706.1; -; mRNA.
DR   EMBL; BT002717; AAO11633.1; -; mRNA.
DR   PIR; H71441; H71441.
DR   RefSeq; NP_193461.5; NM_117834.7.
DR   AlphaFoldDB; Q8VYH6; -.
DR   SMR; Q8VYH6; -.
DR   BioGRID; 12735; 4.
DR   STRING; 3702.AT4G17280.1; -.
DR   PaxDb; Q8VYH6; -.
DR   PRIDE; Q8VYH6; -.
DR   ProteomicsDB; 241118; -.
DR   EnsemblPlants; AT4G17280.1; AT4G17280.1; AT4G17280.
DR   GeneID; 827442; -.
DR   Gramene; AT4G17280.1; AT4G17280.1; AT4G17280.
DR   KEGG; ath:AT4G17280; -.
DR   Araport; AT4G17280; -.
DR   TAIR; locus:2130789; AT4G17280.
DR   eggNOG; KOG4293; Eukaryota.
DR   HOGENOM; CLU_036675_1_1_1; -.
DR   InParanoid; Q8VYH6; -.
DR   OMA; FDSCNDL; -.
DR   OrthoDB; 599276at2759; -.
DR   PhylomeDB; Q8VYH6; -.
DR   PRO; PR:Q8VYH6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8VYH6; baseline and differential.
DR   Genevisible; Q8VYH6; 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..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..402
FT                   /note="Cytochrome b561 and DOMON domain-containing protein
FT                   At4g17280"
FT                   /id="PRO_0000430473"
FT   TRANSMEM        218..238
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
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          54..171
FT                   /note="DOMON"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT   DOMAIN          183..379
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"
SQ   SEQUENCE   402 AA;  43679 MW;  FCCB1300223E4FD3 CRC64;
     MSNHMSIMKF LNQILCLSLI LSISMTTLSF AQTCSKYKFS SNNVFDSCND LPFLDSFLHY
     TYESSTGSLH IAYRHTKLTS GKWVAWAVNP TSTGMVGAQA IVAYPQSDGT VRVYTSPIRS
     YQTSLLEGDL SFNVSGLSAT YQNNEIVVLA SLKLAQDLGN GGTINTVWQD GSMSGNSLLP
     HPTSGNNVRS VSTLNLVSGV SAAAGGAGGS SKLRKRNIHG ILNGVSWGIM MPLGAIIARY
     LRVAKSADPA WFYIHVFCQA SAYIIGVAGW ATGLKLGGDS PGIQYSTHRA IGIALFSLAT
     VQVFAMFLRP KPEHKHRLYW NIYHHTIGYT IIILGVVNVF KGLGILSPKK QWKNAYIGII
     VVLAIVATLL EAFTWYVVIK RRKLEAKTAQ HGASNGTRSQ YA
 
 
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