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Database: UniProt
Entry: D7L5V8_ARALL
LinkDB: D7L5V8_ARALL
Original site: D7L5V8_ARALL 
ID   D7L5V8_ARALL            Unreviewed;       228 AA.
AC   D7L5V8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFH59836.1};
GN   ORFNames=ARALYDRAFT_673591 {ECO:0000313|EMBL:EFH59836.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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}.
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DR   EMBL; GL348715; EFH59836.1; -; Genomic_DNA.
DR   RefSeq; XP_002883577.1; XM_002883531.1.
DR   AlphaFoldDB; D7L5V8; -.
DR   STRING; 81972.D7L5V8; -.
DR   EnsemblPlants; Al_scaffold_0003_2788; Al_scaffold_0003_2788; Al_scaffold_0003_2788.
DR   GeneID; 9321753; -.
DR   Gramene; Al_scaffold_0003_2788; Al_scaffold_0003_2788; Al_scaffold_0003_2788.
DR   KEGG; aly:9321753; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_29_3_1; -.
DR   OrthoDB; 470488at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
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   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR47947; CYTOCHROME P450 82C3-RELATED; 1.
DR   PANTHER; PTHR47947:SF25; DIMETHYLNONATRIENE SYNTHASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   228 AA;  25855 MW;  B23A7F7317A16DAE CRC64;
     MVEIELKKVA AKDQQGDVEY TGYPLSVKDV VLTLTGSDST SITLTWAVSL LLNNPATLKA
     AQEEIDNCVG KGRWVEESDI RNLNYLQAIA KETHRLYPRA PLTRIREARE DCFVGGYRVE
     KGIRLLVNIW KLHRDPMIIW PDPKTFKPER FMEEESQCGK GDFEYIPFIS GRRSCPGINL
     DLRVVHIVLA RLLQGFELRK VSGEPLDMAE GPGLALPKIN PVDKLDYF
//
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