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Database: UniProt
Entry: V3ZCQ5_LOTGI
LinkDB: V3ZCQ5_LOTGI
Original site: V3ZCQ5_LOTGI 
ID   V3ZCQ5_LOTGI            Unreviewed;       499 AA.
AC   V3ZCQ5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LOTGIDRAFT_234414 {ECO:0000313|EMBL:ESO88838.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO88838.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESO88838.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRNR:PIRNR000047, ECO:0000256|PIRSR:PIRSR000047-1};
CC   -!- PATHWAY: Lipid metabolism; bile acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004860}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|PIRNR:PIRNR000047}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|PIRNR:PIRNR000047}.
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DR   EMBL; KB202620; ESO88838.1; -; Genomic_DNA.
DR   RefSeq; XP_009060508.1; XM_009062260.1.
DR   AlphaFoldDB; V3ZCQ5; -.
DR   STRING; 225164.V3ZCQ5; -.
DR   EnsemblMetazoa; LotgiT234414; LotgiP234414; LotgiG234414.
DR   GeneID; 20249533; -.
DR   KEGG; lgi:LOTGIDRAFT_234414; -.
DR   CTD; 20249533; -.
DR   HOGENOM; CLU_018012_1_3_1; -.
DR   OMA; TENHNIW; -.
DR   OrthoDB; 1537669at2759; -.
DR   Proteomes; UP000030746; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum 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:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11040; CYP7_CYP8-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR024204; Cyt_P450_CYP7A1-type.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24304:SF4; 25-HYDROXYCHOLESTEROL 7-ALPHA-HYDROXYLASE-LIKE; 1.
DR   PANTHER; PTHR24304; CYTOCHROME P450 FAMILY 7; 1.
DR   Pfam; PF00067; p450; 1.
DR   PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR000047};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000047};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000047};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000047, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT   BINDING         380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT   BINDING         429
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:0000256|PIRSR:PIRSR000047-1"
SQ   SEQUENCE   499 AA;  57815 MW;  A8496B6AE811EA7A CRC64;
     MVAVTVYLAA IAIGLTVAFF KFIYRRRRPN EPEIVPGNLL WGNGAEFAEH AVNFLHRCQK
     KFGDIFTIRL LNQYITLVLD PHSYENLARE KVFDFDPIQR QVNHNVFNFE LIDARKMLSE
     AGKKVNGRFL TTGMRNFADN LKNAFAKVST VDENGNIYQT IGDNWGQDGL RDLTSKTLFS
     ALFYTIFGQG DAIETFEPQT FYKNFDSFHK YFNYLWLGLP VKLFPKATAA LNVLSQQPTS
     DEMLKRPGVS DYIKFSTEFM KANNQSEQDI VGHNLVFLHV NYNTFRLAFW VLYHILDDRA
     TFMALHKEVQ DLVERKTETA TENGPLGISI EEFDKLPILD SIIRETLRVT SGVFMVRYIT
     QDVEFEMDNG DKALMREGDR VAMYPPAIHK DPEIFEDPEI FKHDRFVDAK FYKNGKELKN
     PLVAFGSLCP GKKYSLLQTK WFLVNLMNSF DVRLVEGQKT ECDVNYYGHE ILPPTNDVQV
     QYRLKEKFQE LDFLARRQC
//
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