ID A0A084VN57_ANOSI Unreviewed; 502 AA.
AC A0A084VN57;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=AGAP008208-PA-like protein {ECO:0000313|EMBL:KFB39401.1};
GN ORFNames=ZHAS_00006838 {ECO:0000313|EMBL:KFB39401.1};
OS Anopheles sinensis (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=74873 {ECO:0000313|EMBL:KFB39401.1};
RN [1] {ECO:0000313|EMBL:KFB39401.1, ECO:0000313|Proteomes:UP000030765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24438588; DOI=10.1186/1471-2164-15-42;
RA Zhou D., Zhang D., Ding G., Shi L., Hou Q., Ye Y., Xu Y., Zhou H.,
RA Xiong C., Li S., Yu J., Hong S., Yu X., Zou P., Chen C., Chang X., Wang W.,
RA Lv Y., Sun Y., Ma L., Shen B., Zhu C.;
RT "Genome sequence of Anopheles sinensis provides insight into genetics basis
RT of mosquito competence for malaria parasites.";
RL BMC Genomics 15:42-42(2014).
RN [2] {ECO:0000313|EnsemblMetazoa:ASIC006838-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: May be involved in the metabolism of insect hormones and in
CC the breakdown of synthetic insecticides.
CC {ECO:0000256|ARBA:ARBA00003690}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR602403-1};
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}.
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; ATLV01014697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE524979; KFB39401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084VN57; -.
DR STRING; 74873.A0A084VN57; -.
DR EnsemblMetazoa; ASIC006838-RA; ASIC006838-PA; ASIC006838.
DR VEuPathDB; VectorBase:ASIC006838; -.
DR VEuPathDB; VectorBase:ASIS006322; -.
DR OMA; PYGGVFM; -.
DR Proteomes; UP000030765; 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; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24292:SF100; CYP6A16, ISOFORM B-RELATED; 1.
DR PANTHER; PTHR24292; CYTOCHROME P450; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..20
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 447
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:PIRSR602403-1"
SQ SEQUENCE 502 AA; 58243 MW; 8B210991FAE70E39 CRC64;
MLLEVAGIVL AIVVSCYVWL KRRYRFWKDR NVAYIVPEFP YGNFKTLGKV EHIAPITQRH
YEHFKRLNVP YGGVFMLTSP LLYIFDTKLI KTLLVKDFQY FPNRGVYFNE RDDPLSAHMF
AIEGQKWRAL RAKLSPTFTS GRIKTTFPLV TEVCRRFCDH LLEEVQRSND VEVHDLLSRF
TIDVIGACAF GIECNSFREP DNEFRRYGKI AFDKLRHSPL VVYLMKAFRA HANALGMKQL
HDDVSSFFLN VVKDTIEYRE REKIVRNDFM DLLVKLKNTG RLEDGGEEIG RLTFEEIAAQ
AFIFFTAGYD TSSTAMSYTL YELALNQAAQ EKARQCVKNT LQKYGGQVTY EATHDMPYLE
QCISETLRKH PPVAILERNA DKDYRLPDSG LLLRRGQKIM VPIYAMHRDP EHFPEPDEYR
PERFDPEEVA KRDSHCYLPF GEGPRICIGM RFGSIQAKVG LANLLNRFRF SVCDRTQIPV
QYSRTNFILG PANGVWLRAE TL
//
