位置:首页 > 蛋白库 > C70B3_ARATH
C70B3_ARATH
ID   C70B3_ARATH             Reviewed;         518 AA.
AC   Q9T093;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Cytochrome P450 709B3 {ECO:0000305};
DE            EC=1.14.-.- {ECO:0000305};
GN   Name=CYP709B3 {ECO:0000303|PubMed:15280363};
GN   OrderedLocusNames=At4g27710 {ECO:0000312|Araport:AT4G27710};
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=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   [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   FUNCTION.
RX   PubMed=15280363; DOI=10.1074/jbc.m406337200;
RA   Takei K., Yamaya T., Sakakibara H.;
RT   "Arabidopsis CYP735A1 and CYP735A2 encode cytokinin hydroxylases that
RT   catalyze the biosynthesis of trans-Zeatin.";
RL   J. Biol. Chem. 279:41866-41872(2004).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION BY SALT STRESS, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=24164720; DOI=10.1186/1471-2229-13-169;
RA   Mao G., Seebeck T., Schrenker D., Yu O.;
RT   "CYP709B3, a cytochrome P450 monooxygenase gene involved in salt tolerance
RT   in Arabidopsis thaliana.";
RL   BMC Plant Biol. 13:169-169(2013).
CC   -!- FUNCTION: Plays a role in abscisic acid (ABA) and salt stress response.
CC       May regulate the salt stress response independently of well-
CC       characterized pathways (PubMed:24164720). Does not function as
CC       cytokinin hydroxylase in yeast heterologous system (Probable).
CC       {ECO:0000269|PubMed:24164720, ECO:0000305|PubMed:15280363}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in rosette leaves and siliques,
CC       and at lower levels in flowers. {ECO:0000269|PubMed:24164720}.
CC   -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:24164720}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants show increased sensitivity to abscisic
CC       acid (ABA) treatment or salt stress. {ECO:0000269|PubMed:24164720}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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; AL035602; CAB38283.1; -; Genomic_DNA.
DR   EMBL; AL161571; CAB81421.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85384.1; -; Genomic_DNA.
DR   PIR; T05876; T05876.
DR   RefSeq; NP_194501.1; NM_118910.4.
DR   AlphaFoldDB; Q9T093; -.
DR   SMR; Q9T093; -.
DR   STRING; 3702.AT4G27710.1; -.
DR   PaxDb; Q9T093; -.
DR   PRIDE; Q9T093; -.
DR   ProteomicsDB; 240563; -.
DR   EnsemblPlants; AT4G27710.1; AT4G27710.1; AT4G27710.
DR   GeneID; 828885; -.
DR   Gramene; AT4G27710.1; AT4G27710.1; AT4G27710.
DR   KEGG; ath:AT4G27710; -.
DR   Araport; AT4G27710; -.
DR   TAIR; locus:2137697; AT4G27710.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_5_0_1; -.
DR   InParanoid; Q9T093; -.
DR   OMA; RRKDNEF; -.
DR   OrthoDB; 825914at2759; -.
DR   PhylomeDB; Q9T093; -.
DR   BioCyc; ARA:AT4G27710-MON; -.
DR   PRO; PR:Q9T093; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9T093; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Stress response; Transmembrane; Transmembrane helix.
FT   CHAIN           1..518
FT                   /note="Cytochrome P450 709B3"
FT                   /id="PRO_0000435384"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         465
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
SQ   SEQUENCE   518 AA;  59769 MW;  EDD93E3B0DC7F892 CRC64;
     MELISTINLL TIVLLLFVVS KIWKACWILL LRPLMLSKRF KKQGISGPKY KILYGNLSEI
     KKMKKEADLC VLDPNSNDIF PRVFPQYHQW MSQYGDTFLF WTGTKPTIYI SNHELAKQVL
     SSKFGFTIIP VKRPEVFILF GKGLSFIQGD DWIRHRRILN PAFSMDRLKA MTQPMGDCTL
     RIFEEWRKQR RNGEVLIKIE ISKEFHKLTA DIIATTAFGS SYAEGIELCR SQTELEKYYI
     SSLTNVFIPG TQYLPTPTNL KLWELHKKVK NSIKRIIDSR LKSKCKTYGY GDDLLGVMLT
     AAKSNEYERK MRMDEIIEEC KNFYYAGQGT TSILLTWTTM LLSLHQGWQE KLREEVFNEC
     GKDKIPDTDT FSKLKLMNMV LMESLRLYGP VIKISREATQ DMKVGHLEIP KGTSIIIPLL
     KMHRDKAIWG EDAEQFNPLR FENGISQATI HPNALLPFSI GPRACIAKNF AMVEAKTVLT
     MILQQFQLSL SPEYKHTPVD HFDLFPQYGL PVMLHPLG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024