ID A0A084WSB4_ANOSI Unreviewed; 501 AA.
AC A0A084WSB4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=AGAP002138-PA-like protein {ECO:0000313|EMBL:KFB53108.1};
GN ORFNames=ZHAS_00021402 {ECO:0000313|EMBL:KFB53108.1};
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:KFB53108.1};
RN [1] {ECO:0000313|EMBL:KFB53108.1, 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:ASIC021402-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 -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; ATLV01026435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KE525413; KFB53108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084WSB4; -.
DR STRING; 74873.A0A084WSB4; -.
DR EnsemblMetazoa; ASIC021402-RA; ASIC021402-PA; ASIC021402.
DR VEuPathDB; VectorBase:ASIC021402; -.
DR VEuPathDB; VectorBase:ASIS009186; -.
DR OMA; CAQRHPY; -.
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; cd11057; CYP313-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; PTHR24291:SF189; CYTOCHROME P450 4V2; 1.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 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}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000030765}.
FT REGION 257..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 57541 MW; E44E8F7ABC1DF1B4 CRC64;
MIVLVFIVVF ALAYYVNFRR SRKRLYELAK QIPGPFDYPL IGSILITLGK NPLQLVSHLM
ELMHHLPSPM RAWLGPYLLV VIDQPAMVQD VLSSPDCVQK PFMYDFFRIS KGLFGAPADT
WRRHRKLLNT SFSPVVLKSF VPMLNEKADG FVHELAAEAS AGTFDVHKPL ARYTVVSIAS
TTLGVDLSVE KRDTLEEYSS NAIELFTACF ERIYKAWLHP EVIFRRTNAF QVEQKRMQTF
KKMSKKIITL RQHVLAQESG HDRQDSDPED KQDTSPRGKI FIERLEEMAR DPALHIDDDG
FQQHIDTLLF GGNDTSAQTL ANTMLTLGMY PELQEKVYQE IVDVCPSGPI AYADLSRLVY
MEMFVKETLR LLPITGLIAR APTREIPSRG ITIPSGAIVM VPLLKMHRDK KIWGPDAETF
DPDNFLPERC IERHPYSFIP FSQGPRNCIG MKYGWLSMKI LLCHVLRRYR VSTDIKLRDI
KLSLSLVMKL NTKHMIRLER R
//
