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C78A7_ARATH
ID   C78A7_ARATH             Reviewed;         536 AA.
AC   Q9FIB0;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Cytochrome P450 78A7;
DE            EC=1.14.-.-;
GN   Name=CYP78A7; OrderedLocusNames=At5g09970; ORFNames=MYH9.18;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
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 [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18492871; DOI=10.1105/tpc.108.058180;
RA   Wang J.W., Schwab R., Czech B., Mica E., Weigel D.;
RT   "Dual effects of miR156-targeted SPL genes and CYP78A5/KLUH on plastochron
RT   length and organ size in Arabidopsis thaliana.";
RL   Plant Cell 20:1231-1243(2008).
CC   -!- FUNCTION: Functions probably in association with CYP78A5 in regulating
CC       relative growth of the shoot apical meristem and plant organs via a
CC       non-cell-autonomous signal. {ECO:0000269|PubMed:18492871}.
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   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. {ECO:0000269|PubMed:18492871}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB016893; BAB09418.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91472.1; -; Genomic_DNA.
DR   EMBL; AY136401; AAM97067.1; -; mRNA.
DR   EMBL; BT000225; AAN15544.1; -; mRNA.
DR   EMBL; AK227001; BAE99066.1; -; mRNA.
DR   RefSeq; NP_196559.1; NM_121034.2.
DR   AlphaFoldDB; Q9FIB0; -.
DR   SMR; Q9FIB0; -.
DR   STRING; 3702.AT5G09970.1; -.
DR   iPTMnet; Q9FIB0; -.
DR   PaxDb; Q9FIB0; -.
DR   PRIDE; Q9FIB0; -.
DR   ProteomicsDB; 240580; -.
DR   EnsemblPlants; AT5G09970.1; AT5G09970.1; AT5G09970.
DR   GeneID; 830858; -.
DR   Gramene; AT5G09970.1; AT5G09970.1; AT5G09970.
DR   KEGG; ath:AT5G09970; -.
DR   Araport; AT5G09970; -.
DR   TAIR; locus:2178213; AT5G09970.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_0_1; -.
DR   InParanoid; Q9FIB0; -.
DR   OMA; VDATWWA; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; Q9FIB0; -.
DR   BioCyc; ARA:AT5G09970-MON; -.
DR   PRO; PR:Q9FIB0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIB0; baseline and differential.
DR   Genevisible; Q9FIB0; 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   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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   Developmental protein; Growth regulation; Heme; Iron; Membrane;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..536
FT                   /note="Cytochrome P450 78A7"
FT                   /id="PRO_0000422987"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         481
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   536 AA;  59494 MW;  64A39B79A69DAFD0 CRC64;
     MELMNLASKE TSYWMIALPA GFGSQNLHDV STLGYLFLAV VFLSIVTWAL AGGGGVAWKN
     GRNRLGRVAI PGPRGIPVFG SLFTLSRGLA HRTLAAMAWS RANTEIMAFS LGSTPVIVAS
     EPNIAREILM SPHFADRPVK QSAKSLMFSR AIGFAPNGTY WRMLRRIAST HLFAPRRILA
     HEAGRQLDCA EMVKAVSVEQ NGAGSVVLRK HLQLAALNNI MGSVFGRRYD PLAQKEDLDE
     LTSMVREGFE LLGAFNWSDY LPWLGYFYDS IRLNQRCSDL VPRIRTLVKK IIDEHRVSNS
     EKKRDIGDFV DVLLSLDGDE KLQEDDMIAV LWEMIFRGTD TTALLTEWTM AELVLNPNVQ
     TKLRDEILTA VGDGADGDVA DADLAKLPYL NAVVKETLRL HPPGPLLSWA RLSTSDVQLS
     NGMVIPKGTT AMVNMWAITH DQTVWSDPLK FDPERFTGNA DMDIRGGDLR LAPFGAGRRV
     CPGKNMGLAT VTRWVAELVR RFEWGQDQTE PVDLGEVLKL SCEMEHPLRA VVTEIF
 
 
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