ID   CP10_LYMST              Reviewed;         545 AA.
AC   P48416;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Cytochrome P450 10;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPX;
GN   Name=CYP10;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1400265; DOI=10.1093/oxfordjournals.jbchem.a123885;
RA   Teunissen Y., Geraerts W.P.M., van Heerikhuizen H., Planta R.J., Joosse J.;
RT   "Molecular cloning of a cDNA encoding a member of a novel cytochrome P450
RT   family in the mollusc Lymnaea stagnalis.";
RL   J. Biochem. 112:249-252(1992).
CC   -!- FUNCTION: May be involved in the synthesis of the female gonadotropic
CC       hormone produced by the dorsal bodies.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in the female gonadotropic
CC       hormone producing dorsal bodies.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {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; S46130; AAB23599.1; -; mRNA.
DR   PIR; JX0225; JX0225.
DR   AlphaFoldDB; P48416; -.
DR   SMR; P48416; -.
DR   KEGG; ag:AAB23599; -.
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   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..545
FT                   /note="Cytochrome P450 10"
FT                   /id="PRO_0000051922"
FT   BINDING         493
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   545 AA;  62360 MW;  56910FFAB5BF939D CRC64;
     MAIMKKFIHH SLKQLIKPNL TSTKRVVSTS PRKEQGVAAI SLEPSEMAQC PFRKSIDTFT
     ETTNAVKAPG MTEVQPFERI PGPKGLPIVG TLFDYFKKDG PKFSKMFEVY RQRALEFGNI
     YYEKVGHFHC VVISSPGEYS RLVHAERQYP NRREMVPIAY YRKQKGFDLG VVNSQGEEWY
     RQRTVVSKKM LKLAEVSNFS TQMGEVSDDF VKRLSHVRDS HGEIPALERE LFKWAMESIG
     TFLFEERIGC LGQETSPMAQ TFIANLEGFF KTLQPLMYNL PTYKLWSTKL WKQFENYSDN
     VIDIGRSLVE KKWHPCKMEV TQNLHLISYL VNNGSMSTKE VTGLIVDLML AAVETTSSAT
     VWCLYNLAKN PQVQEKLFQE ITEAQAKNNG TISAEDLCKL PMVKAVVKET LRLYPITYST
     SRNIAEDMEL GGYTIPAGTH VQANLYGMYR DPSLFPEPEG ILPERWLRMN GSQMDATIKS
     TSQLVWGHGA RMCLGRRIAE QEMHITLSKI IQNFTLSYNH DDVEPILNTM LTPDRPVRIE
     FKPRQ