C14A2_ARATH
ID C14A2_ARATH Reviewed; 525 AA.
AC Q6NKZ8;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Cytochrome P450 714A2;
DE EC=1.14.-.-;
DE AltName: Full=EUI-like P450 A2;
GN Name=CYP714A2; Synonyms=ELA2; OrderedLocusNames=At5g24900;
GN ORFNames=F6A4.110;
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].
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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, 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
CC {ECO:0000305|PubMed:21457373}; Single-pass type III membrane protein
CC {ECO:0000305|PubMed:21457373}.
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apical meristem (SAM) and
CC petioles of young leaves, in the leaf margin and petiole vein of
CC cotyledons, and at low levels in the filaments of developing flowers.
CC Not detected in siliques. {ECO:0000269|PubMed:21457373}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC CYP714A1. Cyp714a1 and cyp714a2 double mutants flower earlier and have
CC an increased plant size and biomass. {ECO:0000269|PubMed:21457373}.
CC -!- MISCELLANEOUS: Overexpression of CYP714A2 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; AED93376.1; -; Genomic_DNA.
DR EMBL; BT011240; AAR92276.1; -; mRNA.
DR EMBL; BT012545; AAS99689.1; -; mRNA.
DR EMBL; AK227205; BAE99244.1; -; mRNA.
DR RefSeq; NP_197872.1; NM_122399.3.
DR AlphaFoldDB; Q6NKZ8; -.
DR SMR; Q6NKZ8; -.
DR STRING; 3702.AT5G24900.1; -.
DR PaxDb; Q6NKZ8; -.
DR PRIDE; Q6NKZ8; -.
DR ProteomicsDB; 239108; -.
DR EnsemblPlants; AT5G24900.1; AT5G24900.1; AT5G24900.
DR GeneID; 832559; -.
DR Gramene; AT5G24900.1; AT5G24900.1; AT5G24900.
DR KEGG; ath:AT5G24900; -.
DR Araport; AT5G24900; -.
DR TAIR; locus:2149423; AT5G24900.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_5_0_1; -.
DR InParanoid; Q6NKZ8; -.
DR OMA; MESILHY; -.
DR OrthoDB; 786853at2759; -.
DR PhylomeDB; Q6NKZ8; -.
DR BioCyc; ARA:AT5G24900-MON; -.
DR PRO; PR:Q6NKZ8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NKZ8; baseline and differential.
DR Genevisible; Q6NKZ8; 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..525
FT /note="Cytochrome P450 714A2"
FT /id="PRO_0000422411"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 475
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 525 AA; 59334 MW; EDB265D851988599 CRC64;
MESLVVHTVN AIWCIVIVGI FSVGYHVYGR AVVEQWRMRR SLKLQGVKGP PPSIFNGNVS
EMQRIQSEAK HCSGDNIISH DYSSSLFPHF DHWRKQYGRI YTYSTGLKQH LYINHPEMVK
ELSQTNTLNL GRITHITKRL NPILGNGIIT SNGPHWAHQR RIIAYEFTHD KIKGMVGLMV
ESAMPMLNKW EEMVKRGGEM GCDIRVDEDL KDVSADVIAK ACFGSSFSKG KAIFSMIRDL
LTAITKRSVL FRFNGFTDMV FGSKKHGDVD IDALEMELES SIWETVKERE IECKDTHKKD
LMQLILEGAM RSCDGNLWDK SAYRRFVVDN CKSIYFAGHD STAVSVSWCL MLLALNPSWQ
VKIRDEILSS CKNGIPDAES IPNLKTVTMV IQETMRLYPP APIVGREASK DIRLGDLVVP
KGVCIWTLIP ALHRDPEIWG PDANDFKPER FSEGISKACK YPQSYIPFGL GPRTCVGKNF
GMMEVKVLVS LIVSKFSFTL SPTYQHSPSH KLLVEPQHGV VIRVV
