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Database: UniProt
Entry: A8MRD1_ARATH
LinkDB: A8MRD1_ARATH
Original site: A8MRD1_ARATH 
ID   A8MRD1_ARATH            Unreviewed;       353 AA.
AC   A8MRD1;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   SubName: Full=AT5G05690 protein {ECO:0000313|EMBL:BAH20171.1};
DE   SubName: Full=Cytochrome P450 superfamily protein {ECO:0000313|EMBL:AED90911.1};
GN   Name=CPD {ECO:0000313|EMBL:AED90911.1, ECO:0000313|TAIR:AT5G05690};
GN   Synonyms=CABBAGE 3 {ECO:0000313|EMBL:AED90911.1}, CBB3
GN   {ECO:0000313|EMBL:AED90911.1}, CYP90 {ECO:0000313|EMBL:AED90911.1},
GN   CYP90A {ECO:0000313|EMBL:AED90911.1}, CYP90A1
GN   {ECO:0000313|EMBL:AED90911.1}, CYTOCHROME P450
GN   {ECO:0000313|EMBL:AED90911.1}, CYTOCHROME P450 90A1
GN   {ECO:0000313|EMBL:AED90911.1}, CYTOCHROME P450 MONOOXYGENASE
GN   {ECO:0000313|EMBL:AED90911.1}, DWARF 3 {ECO:0000313|EMBL:AED90911.1},
GN   DWF3 {ECO:0000313|EMBL:AED90911.1}, MJJ3.9
GN   {ECO:0000313|EMBL:AED90911.1}, MJJ3_9 {ECO:0000313|EMBL:AED90911.1};
GN   OrderedLocusNames=At5g05690 {ECO:0000313|Araport:AT5G05690,
GN   ECO:0000313|EMBL:AED90911.1};
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 {ECO:0000313|EMBL:AED90911.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:AED90911.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=11130714; DOI=10.1038/35048507;
RG   Kazusa DNA Research Institute;
RG   Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG   European Union Arabidopsis Genome Sequencing Consortium;
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., See L.H., Vil D., Baker J.,
RA   Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA   Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA   Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA   Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA   Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA   Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2] {ECO:0000313|EMBL:BAH20171.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Rosette leaf {ECO:0000313|EMBL:BAH20171.1};
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 0:0-0(2009).
RN   [3] {ECO:0000313|EMBL:AED90911.1}
RP   NUCLEOTIDE SEQUENCE.
RG   TAIR;
RA   Swarbreck D., Lamesch P., Wilks C., Huala E.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AED90911.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Krishnakumar V., Cheng C.-Y., Chan A.P., Schobel S., Kim M., Ferlanti E.S.,
RA   Belyaeva I., Rosen B.D., Micklem G., Miller J.R., Vaughn M., Town C.D.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- PATHWAY: Hormone biosynthesis. {ECO:0000256|ARBA:ARBA00004972}.
CC   -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00037910}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   EMBL; CP002688; AED90911.1; -; Genomic_DNA.
DR   EMBL; AK317506; BAH20171.1; -; mRNA.
DR   RefSeq; NP_001078535.1; NM_001085066.1.
DR   AlphaFoldDB; A8MRD1; -.
DR   SMR; A8MRD1; -.
DR   EnsemblPlants; AT5G05690.3; AT5G05690.3; AT5G05690.
DR   GeneID; 830453; -.
DR   Gramene; AT5G05690.3; AT5G05690.3; AT5G05690.
DR   Araport; AT5G05690; -.
DR   TAIR; AT5G05690; CPD.
DR   HOGENOM; CLU_001570_15_1_1; -.
DR   OMA; KLWEVYM; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; A8MRD1; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd11043; CYP90-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR   PANTHER; PTHR24286:SF44; CYTOCHROME P450 90A1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|RuleBase:RU000461};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A8MRD1,
KW   ECO:0007829|ProteomicsDB:A8MRD1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   353 AA;  40504 MW;  2F4AC486F6317388 CRC64;
     MKGSLHKRMH SLTMSFANSS IIKDHLMLDI DRLVRFNLDS WSSRVLLMEE AKKITFELTV
     KQLMSFDPGE WSESLRKEYL LVIEGFFSLP LPLFSTTYRK AIQARRKVAE ALTVVVMKRR
     EEEEEGAERK KDMLAALLAA DDGFSDEEIV DFLVALLVAG YETTSTIMTL AVKFLTETPL
     ALAQLKEEHE KIRAMKSDSY SLEWSDYKSM PFTQCVVNET LRVANIIGGV FRRAMTDVEI
     KGYKIPKGWK VFSSFRAVHL DPNHFKDART FNPWRWQSNS VTTGPSNVFT PFGGGPRLCP
     GYELARVALS VFLHRLVTGF SWVPAEQDKL VFFPTTRTQK RYPIFVKRRD FAT
//
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