C76C1_ARATH
ID C76C1_ARATH Reviewed; 512 AA.
AC O64636; O65783;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cytochrome P450 76C1;
DE EC=1.14.-.-;
GN Name=CYP76C1; OrderedLocusNames=At2g45560; ORFNames=F17K2.9;
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] (ISOFORM LONG).
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=9620263; DOI=10.1023/a:1005921406884;
RA Mizutani M., Ward E., Ohta D.;
RT "Cytochrome P450 superfamily in Arabidopsis thaliana: isolation of cDNAs,
RT differential expression, and RFLP mapping of multiple cytochromes P450.";
RL Plant Mol. Biol. 37:39-52(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM LONG).
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] (ISOFORM SHORT).
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.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O64636-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O64636-2; Sequence=VSP_000619, VSP_000620;
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA28540.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D78600; BAA28540.1; ALT_FRAME; mRNA.
DR EMBL; AC003680; AAC06157.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10570.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10571.1; -; Genomic_DNA.
DR EMBL; AY078939; AAL84945.1; -; mRNA.
DR EMBL; AY124874; AAM70583.1; -; mRNA.
DR EMBL; AY085090; AAM61644.1; -; mRNA.
DR PIR; T00869; T00869.
DR PIR; T52168; T52168.
DR RefSeq; NP_850439.1; NM_180108.2. [O64636-1]
DR RefSeq; NP_850440.1; NM_180109.3. [O64636-2]
DR AlphaFoldDB; O64636; -.
DR SMR; O64636; -.
DR BioGRID; 4500; 10.
DR IntAct; O64636; 9.
DR STRING; 3702.AT2G45560.1; -.
DR PaxDb; O64636; -.
DR PRIDE; O64636; -.
DR ProteomicsDB; 239162; -. [O64636-1]
DR EnsemblPlants; AT2G45560.1; AT2G45560.1; AT2G45560. [O64636-1]
DR EnsemblPlants; AT2G45560.2; AT2G45560.2; AT2G45560. [O64636-2]
DR GeneID; 819164; -.
DR Gramene; AT2G45560.1; AT2G45560.1; AT2G45560. [O64636-1]
DR Gramene; AT2G45560.2; AT2G45560.2; AT2G45560. [O64636-2]
DR KEGG; ath:AT2G45560; -.
DR Araport; AT2G45560; -.
DR TAIR; locus:2043699; AT2G45560.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_2_1; -.
DR InParanoid; O64636; -.
DR OMA; IMKRPIN; -.
DR PhylomeDB; O64636; -.
DR BioCyc; ARA:AT2G45560-MON; -.
DR PRO; PR:O64636; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64636; baseline and differential.
DR Genevisible; O64636; 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 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 Alternative splicing; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="Cytochrome P450 76C1"
FT /id="PRO_0000052141"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 450
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"
FT VAR_SEQ 307..322
FT /note="DMFTAGTDTSSSTLEW -> VSLTLLQIIMIYKIME (in isoform
FT Short)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_000619"
FT VAR_SEQ 323..512
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_000620"
FT CONFLICT 323
FT /note="A -> P (in Ref. 1; BAA28540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 56801 MW; 314F9DEBF8C9B54B CRC64;
MDIISGQALL LLFCFILSCF LIFTTTRSGR ISRGATALPP GPPRLPIIGN IHLVGKHPHR
SFAELSKTYG PVMSLKLGSL NTVVIASPEA AREVLRTHDQ ILSARSPTNA VRSINHQDAS
LVWLPSSSAR WRLLRRLSVT QLLSPQRIEA TKALRMNKVK ELVSFISESS DREESVDISR
VAFITTLNII SNILFSVDLG SYNAKASING VQDTVISVMD AAGTPDAANY FPFLRFLDLQ
GNVKTFKVCT ERLVRVFRGF IDAKIAEKSS QNNPKDVSKN DFVDNLLDYK GDESELSISD
IEHLLLDMFT AGTDTSSSTL EWAMTELLKN PKTMAKAQAE IDCVIGQNGI VEESDISKLP
YLQAVVKETF RLHTPVPLLI PRKAESDAEI LGFMVLKDTQ VLVNVWAIGR DPSVWDNPSQ
FEPERFLGKD MDVRGRDYEL TPFGAGRRIC PGMPLAMKTV SLMLASLLYS FDWKLPKGVL
SEDLDMDETF GLTLHKTNPL HAVPVKKRAN IN