位置:首页 > 蛋白库 > C71AC_ARATH
C71AC_ARATH
ID   C71AC_ARATH             Reviewed;         497 AA.
AC   O49340; F4INX7; Q8LPP9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cytochrome P450 71A12;
DE            EC=1.14.-.- {ECO:0000305};
GN   Name=CYP71A12; OrderedLocusNames=At2g30750; ORFNames=T11J7.14;
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;
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   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26352477; DOI=10.1038/nature14907;
RA   Rajniak J., Barco B., Clay N.K., Sattely E.S.;
RT   "A new cyanogenic metabolite in Arabidopsis required for inducible pathogen
RT   defence.";
RL   Nature 525:376-379(2015).
CC   -!- FUNCTION: Converts indole-3-acetaldoxime to indole cyanohydrin.
CC       Involved in the biosynthetic pathway to 4-hydroxyindole-3-carbonyl
CC       nitrile (4-OH-ICN), a cyanogenic metabolite required for inducible
CC       pathogen defense. {ECO:0000269|PubMed:26352477}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: 90% decrease of all indole-3-carbonyl nitrile
CC       (ICN) derivatives and increased susceptibility to virulent Pseudomonas
CC       syringae. {ECO:0000269|PubMed:26352477}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM19850.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAN46800.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AC002340; AAC02746.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08435.2; -; Genomic_DNA.
DR   EMBL; AY094484; AAM19850.1; ALT_INIT; mRNA.
DR   EMBL; BT001046; AAN46800.1; ALT_INIT; mRNA.
DR   PIR; C84712; C84712.
DR   RefSeq; NP_180633.3; NM_128628.4.
DR   AlphaFoldDB; O49340; -.
DR   SMR; O49340; -.
DR   BioGRID; 2975; 2.
DR   STRING; 3702.AT2G30750.1; -.
DR   PaxDb; O49340; -.
DR   PRIDE; O49340; -.
DR   ProteomicsDB; 222826; -.
DR   EnsemblPlants; AT2G30750.1; AT2G30750.1; AT2G30750.
DR   GeneID; 817626; -.
DR   Gramene; AT2G30750.1; AT2G30750.1; AT2G30750.
DR   KEGG; ath:AT2G30750; -.
DR   Araport; AT2G30750; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_0_1; -.
DR   InParanoid; O49340; -.
DR   OMA; MEMILMV; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; O49340; -.
DR   PRO; PR:O49340; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O49340; baseline and differential.
DR   Genevisible; O49340; AT.
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; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..497
FT                   /note="Cytochrome P450 71A12"
FT                   /id="PRO_0000052063"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         439
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"
SQ   SEQUENCE   497 AA;  56152 MW;  BE6AC1A28A737C81 CRC64;
     MEMILMVSLC LTTLITLFLL KQFLKRTANK VNLPPSPWRL PLIGNLHQLS LHPHRSLHSL
     SLRYGPLMLL HFGRVPILVV SSGEAAQEVL KTHDLKFANR PRSKAVHGLM NGGRDVVFGP
     YGEYWRQMKS VCILNLLTNK MVASFEKIRE EELNEMIKKL EKASSSSSSE NLSELFVTLP
     SDVTSRIALG RKHSEDETAR DLKKRVRQIM ELLGEFPIGD YVPALAWIDR INGFNARIKE
     VSQGFSDLMD KVVQEHLEAG NHKEDFVDIL LSIESEKSIG FQAQRDDIKF MILDMFIGGT
     STSSTLLEWI MTELIRNPNV MKKLQDEIRS TIRPHGSYIK EKDVENMKYL KAVIKEVFRV
     HPPLPLILPR LLSEDVKVKG YNIAAGTEVI INAWAIQRDP AIWGPDAEEF KPERHLDSTL
     DYHGKDLNFI PFGSGRRICP GINLALGLVE VTVANLVGRF DWRAEAGPNG DQPDLTEAFG
     LDVCRKFPLI AFPSSVI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024