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Database: UniProt
Entry: A0A182R2X8_ANOFN
LinkDB: A0A182R2X8_ANOFN
Original site: A0A182R2X8_ANOFN 
ID   A0A182R2X8_ANOFN        Unreviewed;       528 AA.
AC   A0A182R2X8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 2.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
OS   Anopheles funestus (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN000519-PA, ECO:0000313|Proteomes:UP000075900};
RN   [1] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA   Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA   Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA   Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT   "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT   Middle East: occurrence data, distribution maps and bionomic precis.";
RL   Parasit. Vectors 3:117-117(2010).
RN   [2] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA   Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA   Besansky N.J.;
RT   "A chromosome-scale assembly of the major African malaria vector Anopheles
RT   funestus.";
RL   Gigascience 8:0-0(2019).
RN   [3] {ECO:0000313|EnsemblMetazoa:AFUN000519-PA}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN000519-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Microsome membrane
CC       {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004174}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR   AlphaFoldDB; A0A182R2X8; -.
DR   STRING; 62324.A0A182R2X8; -.
DR   EnsemblMetazoa; AFUN000519-RA; AFUN000519-PA; AFUN000519.
DR   VEuPathDB; VectorBase:AFUN000519; -.
DR   VEuPathDB; VectorBase:AFUN2_001648; -.
DR   OrthoDB; 3430723at2759; -.
DR   Proteomes; UP000075900; 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:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11056; CYP6-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24292; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24292:SF45; CYTOCHROME P450 6G1-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000461}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   528 AA;  60589 MW;  840B24672620F7B1 CRC64;
     MINMIFPTID VVQSYMWLVL LCVVLYLLWF LTTAGTRYWQ GRHVPYIAGR PIVGNFFDAI
     LMRKSTFDMM IELYTNERVR NSAIFGISKL MTPTLVLRDP ELIKQVLVKD AAFFLNRSMS
     TDSHGDPIGY YNLLMIKNPP WKQLRSYLTP SLSLSKIKQM YRLLDQVGSE MVASLDALPE
     LRPGVRETEF KELCARFTTD VIASTFFGME ANCLKDENSE FRYYGRKIFD YGPARGLTMA
     SFFFAPKLVP YLRLKLFPRD TEAFLKAIIE QEITRREKTG ESRGDFIDSM ITLKNNNATL
     GVTEIPIKGD ILVAQAATFY MASFETTSSV LSFALYELTR NPKIQAQLRE EIRLVVRKYG
     KDIPYEAYAN EMPYLGMVIS ETARLYPVLP FIERQCTLPE GNTGYKLEPF HDFIIPNHMP
     VLIPIYAIHR DPKYFPNPEL FDPERFSKDN QDQIQPCTYM PFGVGPRTCL GSHFGTIQIK
     IALVKLLTKY RIDRSSSTPG VLTYRKNAFT LNSNEGLCAE LVEDALEM
//
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