C78A9_ARATH
ID C78A9_ARATH Reviewed; 534 AA.
AC Q9SLP1; Q8LBY2;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cytochrome P450 78A9;
DE EC=1.14.-.-;
GN Name=CYP78A9; OrderedLocusNames=At3g61880; ORFNames=F21F14.50;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11006330; DOI=10.2307/3871172;
RA Ito T., Meyerowitz E.M.;
RT "Overexpression of a gene encoding a cytochrome P450, CYP78A9, induces
RT large and seedless fruit in arabidopsis.";
RL Plant Cell 12:1541-1550(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19892740; DOI=10.1073/pnas.0907024106;
RA Adamski N.M., Anastasiou E., Eriksson S., O'Neill C.M., Lenhard M.;
RT "Local maternal control of seed size by KLUH/CYP78A5-dependent growth
RT signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20115-20120(2009).
RN [7]
RP FUNCTION.
RX PubMed=22251317; DOI=10.1111/j.1365-313x.2012.04907.x;
RA Fang W., Wang Z., Cui R., Li J., Li Y.;
RT "Maternal control of seed size by EOD3/CYP78A6 in Arabidopsis thaliana.";
RL Plant J. 70:929-939(2012).
CC -!- FUNCTION: Plays role in seed and fruit development. Functions probably
CC in association with CYP78A6 in the regulation of seed growth.
CC {ECO:0000269|PubMed:11006330, ECO:0000269|PubMed:19892740,
CC ECO:0000269|PubMed:22251317}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC Q9SLP1; P25854: CAM4; NbExp=2; IntAct=EBI-1238437, EBI-1235664;
CC Q9SLP1; P59220: CAM7; NbExp=2; IntAct=EBI-1238437, EBI-1236031;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SLP1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the funiculus of developing ovules.
CC {ECO:0000269|PubMed:11006330}.
CC -!- DISRUPTION PHENOTYPE: Slight reduction in seed size.
CC {ECO:0000269|PubMed:19892740}.
CC -!- MISCELLANEOUS: The gain of function mutant 28-5 (T-DNA tagging) in
CC apetala2-1 (ap2-1) mutant background show enlarged and wide pistils and
CC siliques. {ECO:0000305|PubMed:11006330}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB036059; BAA88569.1; -; mRNA.
DR EMBL; AL138642; CAB71895.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80273.1; -; Genomic_DNA.
DR EMBL; AY062748; AAL32826.1; -; mRNA.
DR EMBL; BT008891; AAP68330.1; -; mRNA.
DR EMBL; AY086928; AAM64492.1; -; mRNA.
DR PIR; T47980; T47980.
DR RefSeq; NP_191747.1; NM_116053.3. [Q9SLP1-1]
DR AlphaFoldDB; Q9SLP1; -.
DR SMR; Q9SLP1; -.
DR BioGRID; 10675; 6.
DR IntAct; Q9SLP1; 6.
DR STRING; 3702.AT3G61880.2; -.
DR PaxDb; Q9SLP1; -.
DR PRIDE; Q9SLP1; -.
DR ProteomicsDB; 240498; -. [Q9SLP1-1]
DR EnsemblPlants; AT3G61880.1; AT3G61880.1; AT3G61880. [Q9SLP1-1]
DR GeneID; 825361; -.
DR Gramene; AT3G61880.1; AT3G61880.1; AT3G61880. [Q9SLP1-1]
DR KEGG; ath:AT3G61880; -.
DR Araport; AT3G61880; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR OMA; GGRRSCM; -.
DR PhylomeDB; Q9SLP1; -.
DR BioCyc; ARA:AT3G61880-MON; -.
DR PRO; PR:Q9SLP1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SLP1; baseline and differential.
DR Genevisible; Q9SLP1; 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:0010154; P:fruit development; IGI:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0048316; P:seed development; IGI:UniProtKB.
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 Alternative splicing; Developmental protein; Growth regulation; Heme; Iron;
KW Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..534
FT /note="Cytochrome P450 78A9"
FT /id="PRO_0000422989"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 474
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 534 AA; 60036 MW; 240088AC87A6A502 CRC64;
MATKLDTSSL LLALLSKCSL LTQTNLALSL LVASLASLAL SLFFWSHPGG PAWGKYFLHR
RRQTTVIPGP RGLPFVGSMS LMSNTLAHRC IAATAEKFRA ERLMAFSLGE TRVIVTCNPD
VAKEILNSPV FADRPVKESA YSLMFNRAIG FAPYGVYWRT LRKIASNHLF SPKQIKRSET
QRSVIANQIV KCLTKQSNTK GLCFARDLIK TASLNNMMCS VFGKEYELEE EHEEVSELRE
LVEEGYDLLG TLNWTDHLPW LSEFDPQRIR SRCSNLVPKV NRFVNRIISD HREQTRDSPS
DFVDVLLSLD GPDKLSDPDI IAVLWEMIFR GTDTVAVLIE WILARMVLHP DIQSTVHNEL
DQIVGRSRAV EESDVVSLVY LTAVVKEVLR LHPPGPLLSW ARLAITDTII DGRRVPAGTT
AMVNMWAIAH DPHVWENPLE FKPERFVAKE GEVEFSVLGS DLRLAPFGSG RRVCPGKNLG
LTTVTFWTAT LLHEFEWLTP SDEKTVDLSE KLRLSCEMAN PLAAKLRPRR SFSV
