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C14A1_ARATH
ID   C14A1_ARATH             Reviewed;         532 AA.
AC   Q93Z79;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Cytochrome P450 714A1;
DE            EC=1.14.-.-;
DE   AltName: Full=EUI-like P450 A1;
GN   Name=CYP714A1; Synonyms=ELA1; OrderedLocusNames=At5g24910;
GN   ORFNames=F6A4.120;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
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, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=21457373; DOI=10.1111/j.1365-313x.2011.04596.x;
RA   Zhang Y., Zhang B., Yan D., Dong W., Yang W., Li Q., Zeng L., Wang J.,
RA   Wang L., Hicks L.M., He Z.;
RT   "Two Arabidopsis cytochrome P450 monooxygenases, CYP714A1 and CYP714A2,
RT   function redundantly in plant development through gibberellin
RT   deactivation.";
RL   Plant J. 67:342-353(2011).
CC   -!- FUNCTION: Involved in the inactivation of early gibberellin (GA)
CC       intermediates. {ECO:0000269|PubMed:21457373}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass type III membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the shoot apical meristem (SAM),
CC       petioles of young leaves and emerging leaves, in sepals, stigma, anther
CC       and filaments of the developing flowers, and in the receptacle and
CC       stigma of the developing siliques. {ECO:0000269|PubMed:21457373}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC       CYP714A2. Cyp714a1 and cyp714a2 double mutants flower earlier and have
CC       an increased plant size and biomass. {ECO:0000269|PubMed:21457373}.
CC   -!- MISCELLANEOUS: Overexpression of CYP714A1 causes severe dwarfism with
CC       defective leaf development. {ECO:0000305|PubMed:21457373}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF069716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED93377.1; -; Genomic_DNA.
DR   EMBL; AY058060; AAL24168.1; -; mRNA.
DR   EMBL; BT002687; AAO11603.1; -; mRNA.
DR   RefSeq; NP_568463.1; NM_122400.3.
DR   AlphaFoldDB; Q93Z79; -.
DR   SMR; Q93Z79; -.
DR   STRING; 3702.AT5G24910.1; -.
DR   PaxDb; Q93Z79; -.
DR   PRIDE; Q93Z79; -.
DR   ProteomicsDB; 240384; -.
DR   EnsemblPlants; AT5G24910.1; AT5G24910.1; AT5G24910.
DR   GeneID; 832560; -.
DR   Gramene; AT5G24910.1; AT5G24910.1; AT5G24910.
DR   KEGG; ath:AT5G24910; -.
DR   Araport; AT5G24910; -.
DR   TAIR; locus:2149438; AT5G24910.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_5_0_1; -.
DR   InParanoid; Q93Z79; -.
DR   OMA; DDWIPER; -.
DR   OrthoDB; 825914at2759; -.
DR   PhylomeDB; Q93Z79; -.
DR   BioCyc; ARA:AT5G24910-MON; -.
DR   PRO; PR:Q93Z79; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q93Z79; baseline and differential.
DR   Genevisible; Q93Z79; AT.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..532
FT                   /note="Cytochrome P450 714A1"
FT                   /id="PRO_0000422410"
FT   TOPO_DOM        1..4
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..25
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..532
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   BINDING         480
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   532 AA;  60335 MW;  02CE05FFFE666041 CRC64;
     MENFMVEMAK TISWIVVIGV LGLGIRVYGK VMAEQWRMRR KLTMQGVKGP PPSLFRGNVP
     EMQKIQSQIM SNSKHYSGDN IIAHDYTSSL FPYLDHWRKQ YGRVYTYSTG VKQHLYMNHP
     ELVKELNQAN TLNLGKVSYV TKRLKSILGR GVITSNGPHW AHQRRIIAPE FFLDKVKGMV
     GLVVESAMPM LSKWEEMMKR EGEMVCDIIV DEDLRAASAD VISRACFGSS FSKGKEIFSK
     LRCLQKAITH NNILFSLNGF TDVVFGTKKH GNGKIDELER HIESLIWETV KERERECVGD
     HKKDLMQLIL EGARSSCDGN LEDKTQSYKS FVVDNCKSIY FAGHETSAVA VSWCLMLLAL
     NPSWQTRIRD EVFLHCKNGI PDADSISNLK TVTMVIQETL RLYPPAAFVS REALEDTKLG
     NLVVPKGVCI WTLIPTLHRD PEIWGADANE FNPERFSEGV SKACKHPQSF VPFGLGTRLC
     LGKNFGMMEL KVLVSLIVSR FSFTLSPTYQ HSPVFRMLVE PQHGVVIRVL RQ
 
 
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