C70A2_ARATH
ID C70A2_ARATH Reviewed; 510 AA.
AC Q9LNJ4;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cytochrome P450 703A2 {ECO:0000303|PubMed:17496121};
DE EC=1.14.14.130 {ECO:0000269|PubMed:17496121};
DE AltName: Full=Protein DEFECTIVE IN EXINE FORMATION 2 {ECO:0000303|PubMed:17496121};
GN Name=CYP703A2 {ECO:0000303|PubMed:17496121};
GN Synonyms=DEX2 {ECO:0000303|PubMed:17496121}; OrderedLocusNames=At1g01280;
GN ORFNames=F6F3.8;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17496121; DOI=10.1105/tpc.106.045948;
RA Morant M., Jorgensen K., Schaller H., Pinot F., Moller B.L.,
RA Werck-Reichhart D., Bak S.;
RT "CYP703 is an ancient cytochrome P450 in land plants catalyzing in-chain
RT hydroxylation of lauric acid to provide building blocks for sporopollenin
RT synthesis in pollen.";
RL Plant Cell 19:1473-1487(2007).
CC -!- FUNCTION: Involved in pollen wall development. Catalyzes the conversion
CC of medium-chain saturated fatty acids to the corresponding
CC monohydroxylated fatty acids, with a preferential hydroxylation of
CC lauric acid at the C-7 position. In-chain hydroxylated fatty acids,
CC together with omega-hydroxylated fatty acids, are key monomeric
CC aliphatic building blocks for sporopollenin synthesis during exine
CC formation. {ECO:0000269|PubMed:17496121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 7-
CC hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:45084, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:84921; EC=1.14.14.130;
CC Evidence={ECO:0000269|PubMed:17496121};
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: Specifically expressed in the tapetum cell layer
CC and the microspores of anthers at the tetrad stage. Expression starts
CC to decrease during pollen maturation and tapetum cell degeneration to
CC finally disappear. {ECO:0000269|PubMed:17496121}.
CC -!- DISRUPTION PHENOTYPE: Impaired pollen development and partial male-
CC sterile phenotype. {ECO:0000269|PubMed:17496121}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AC023628; AAF97323.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27265.1; -; Genomic_DNA.
DR EMBL; BT022023; AAY25435.1; -; mRNA.
DR PIR; A86143; A86143.
DR RefSeq; NP_171635.1; NM_100010.3.
DR AlphaFoldDB; Q9LNJ4; -.
DR SMR; Q9LNJ4; -.
DR STRING; 3702.AT1G01280.1; -.
DR PaxDb; Q9LNJ4; -.
DR PRIDE; Q9LNJ4; -.
DR ProteomicsDB; 240267; -.
DR EnsemblPlants; AT1G01280.1; AT1G01280.1; AT1G01280.
DR GeneID; 839470; -.
DR Gramene; AT1G01280.1; AT1G01280.1; AT1G01280.
DR KEGG; ath:AT1G01280; -.
DR Araport; AT1G01280; -.
DR TAIR; locus:2035267; AT1G01280.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9LNJ4; -.
DR OMA; GPQEAME; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9LNJ4; -.
DR BioCyc; ARA:AT1G01280-MON; -.
DR BioCyc; MetaCyc:AT1G01280-MON; -.
DR BRENDA; 1.14.14.130; 399.
DR PRO; PR:Q9LNJ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNJ4; baseline and differential.
DR Genevisible; Q9LNJ4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052722; F:fatty acid in-chain hydroxylase activity; IEA:EnsemblPlants.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:TAIR.
DR GO; GO:0048653; P:anther development; IEA:EnsemblPlants.
DR GO; GO:0002933; P:lipid hydroxylation; IEA:EnsemblPlants.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IDA:TAIR.
DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR GO; GO:0010208; P:pollen wall assembly; IMP:TAIR.
DR GO; GO:0080110; P:sporopollenin biosynthetic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..510
FT /note="Cytochrome P450 703A2"
FT /id="PRO_0000425850"
FT TRANSMEM 2..22
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"
SQ SEQUENCE 510 AA; 57854 MW; 4C8E8CA50CEA698E CRC64;
MILVLASLFA VLILNVLLWR WLKASACKAQ RLPPGPPRLP ILGNLLQLGP LPHRDLASLC
DKYGPLVYLR LGNVDAITTN DPDTIREILL RQDDVFSSRP KTLAAVHLAY GCGDVALAPM
GPHWKRMRRI CMEHLLTTKR LESFTTQRAE EARYLIRDVF KRSETGKPIN LKEVLGAFSM
NNVTRMLLGK QFFGPGSLVS PKEAQEFLHI THKLFWLLGV IYLGDYLPFW RWVDPSGCEK
EMRDVEKRVD EFHTKIIDEH RRAKLEDEDK NGDMDFVDVL LSLPGENGKA HMEDVEIKAL
IQDMIAAATD TSAVTNEWAM AEAIKQPRVM RKIQEELDNV VGSNRMVDES DLVHLNYLRC
VVRETFRMHP AGPFLIPHES VRATTINGYY IPAKTRVFIN THGLGRNTKI WDDVEDFRPE
RHWPVEGSGR VEISHGPDFK ILPFSAGKRK CPGAPLGVTM VLMALARLFH CFEWSSPGNI
DTVEVYGMTM PKAKPLRAIA KPRLAAHLYT
