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C76C2_ARATH
ID   C76C2_ARATH             Reviewed;         512 AA.
AC   O64637; Q9CAZ4;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Cytochrome P450 76C2;
DE            EC=1.14.-.-;
DE   AltName: Full=Protein YELLOW-LEAF-SPECIFIC GENE 6;
GN   Name=CYP76C2; Synonyms=YLS6; OrderedLocusNames=At2g45570;
GN   ORFNames=F17K2.10;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 59-232, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=11230571; DOI=10.1093/pcp/pce021;
RA   Yoshida S., Ito M., Nishida I., Watanabe A.;
RT   "Isolation and RNA gel blot analysis of genes that could serve as potential
RT   molecular markers for leaf senescence in Arabidopsis thaliana.";
RL   Plant Cell Physiol. 42:170-178(2001).
RN   [5]
RP   INDUCTION.
RX   PubMed=9827554; DOI=10.1016/s0014-5793(98)01309-x;
RA   Godiard L., Sauviac L., Dalbin N., Liaubet L., Callard D., Czernic P.,
RA   Marco Y.;
RT   "CYP76C2, an Arabidopsis thaliana cytochrome P450 gene expressed during
RT   hypersensitive and developmental cell death.";
RL   FEBS Lett. 438:245-249(1998).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated in leaves during natural senescence.
CC       {ECO:0000269|PubMed:11230571}.
CC   -!- INDUCTION: By ethylene, abscisic acid (ABA), wounding, lead, dark and
CC       infection with the bacterial pathogen P.syringae pv. tomato.
CC       {ECO:0000269|PubMed:11230571, ECO:0000269|PubMed:9827554}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AC003680; AAC06158.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10572.1; -; Genomic_DNA.
DR   EMBL; AY062600; AAL32678.1; -; mRNA.
DR   EMBL; AY114660; AAM47979.1; -; mRNA.
DR   EMBL; AB047809; BAB32886.1; -; mRNA.
DR   PIR; T00870; T00870.
DR   RefSeq; NP_182081.1; NM_130119.4.
DR   AlphaFoldDB; O64637; -.
DR   SMR; O64637; -.
DR   STRING; 3702.AT2G45570.1; -.
DR   PaxDb; O64637; -.
DR   PRIDE; O64637; -.
DR   ProteomicsDB; 239133; -.
DR   EnsemblPlants; AT2G45570.1; AT2G45570.1; AT2G45570.
DR   GeneID; 819165; -.
DR   Gramene; AT2G45570.1; AT2G45570.1; AT2G45570.
DR   KEGG; ath:AT2G45570; -.
DR   Araport; AT2G45570; -.
DR   TAIR; locus:2043605; AT2G45570.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_2_1; -.
DR   InParanoid; O64637; -.
DR   OMA; TARLFWA; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; O64637; -.
DR   BioCyc; ARA:AT2G45570-MON; -.
DR   PRO; PR:O64637; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O64637; baseline and differential.
DR   Genevisible; O64637; 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..512
FT                   /note="Cytochrome P450 76C2"
FT                   /id="PRO_0000052142"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         451
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"
FT   CONFLICT        107
FT                   /note="P -> S (in Ref. 4; BAB32886)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="V -> G (in Ref. 4; BAB32886)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  57257 MW;  4FF5A1BE1C24C798 CRC64;
     MDIIFEQALF PLFCFVLSFF IIFFTTTRPR SSRKVVPSPP GPPRLPIIGN IHLVGRNPHH
     SFADLSKTYG PIMSLKFGSL NTVVVTSPEA AREVLRTYDQ ILSSRTPTNS IRSINHDKVS
     VVWLPPSSSR WRLLRKLSAT QLFSPQRIEA TKTLRENKVK ELVSFMSESS EREEAVDISR
     ATFITALNII SNILFSVDLG NYDSNKSGVF QDTVIGVMEA VGNPDAANFF PFLGFLDLQG
     NRKTLKACSE RLFKVFRGFI DAKLAEKSLR DTNSKDVRER DFVDVLLDLT EGDEAELNTN
     DIVHLLLDLF GAGTDTNSST VEWAMAELLR NPETMVKAQA EIDCVIGQKG VVEESDISAL
     PYLQAVVKET FRLHPAAPLL VPRKAESDVE VLGFMVPKDT QVFVNVWAIG RDPNVWENSS
     RFKPERFLGK DIDLRGRDYE LTPFGAGRRI CPGLPLAVKT VPLMLASLLY SFDWKLPNGV
     GSEDLDMDET FGLTLHKTNP LHAVPVKKRG RN
 
 
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