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Database: UniProt
Entry: A0A084VZH5_ANOSI
LinkDB: A0A084VZH5_ANOSI
Original site: A0A084VZH5_ANOSI 
ID   A0A084VZH5_ANOSI        Unreviewed;       965 AA.
AC   A0A084VZH5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=ZHAS_00011169 {ECO:0000313|EMBL:KFB43369.1};
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:KFB43369.1};
RN   [1] {ECO:0000313|EMBL:KFB43369.1, 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:ASIC011169-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000256|ARBA:ARBA00010701}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; ATLV01018820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ATLV01018821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ATLV01018822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ATLV01018823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ATLV01018824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KE525249; KFB43369.1; -; Genomic_DNA.
DR   STRING; 74873.A0A084VZH5; -.
DR   EnsemblMetazoa; ASIC011169-RA; ASIC011169-PA; ASIC011169.
DR   VEuPathDB; VectorBase:ASIC011169; -.
DR   VEuPathDB; VectorBase:ASIS005104; -.
DR   VEuPathDB; VectorBase:ASIS020835; -.
DR   OMA; NINRRNW; -.
DR   Proteomes; UP000030765; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   CDD; cd00707; Pancreat_lipase_like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR013818; Lipase.
DR   InterPro; IPR033906; Lipase_N.
DR   InterPro; IPR000734; TAG_lipase.
DR   PANTHER; PTHR11552:SF208; GLUCOSE DEHYDROGENASE [FAD, QUINONE]-LIKE PROTEIN; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF00151; Lipase; 1.
DR   PRINTS; PR00821; TAGLIPASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030765};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          484..507
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          660..674
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   965 AA;  106817 MW;  DBE796BEA6A05B25 CRC64;
     MGVNRCXXXX XXXXSIEALL KRREPRLKPN EVEFVLYTRD DDDDDGQRLG PFTEEYDFEG
     TNFRSDRPTR VIVHGWLNNK NSPFVEQLRH AYIRRWDYNV IVVDWSSCAK LWNYVRAVKC
     VPVVGKSLAF LLDELHRRRE LQLESVYIVG HSLGAHVAGI AGKRVQYGPI HTIVALDPAL
     PLFSMHAPGN RINAQDARYV EVWHTNGGWF GFLRPIGTAD VYPNGGTHQP GCGLPVAGLC
     SHSRAWELYV ESLVEPEENL LAHRVDSLEE INNSESQKGV GVIPFGQRVK MGGEPSSAGS
     ARGLYFIERI VPHTTFQSVG QCVSICRSDR MAVNVRWSSV TACRVVLLVA LCAWATVPGT
     GGQRGVPGTG GGGGGWLDKF NKLLSRSKQR NATEDNEVLD ADEYDFVIVG GGTAGMVLAS
     RLSENRDWRV LLLEAGQYGT KLFNIPIGFQ LAVLSDSYNW RLLSEKQTNA CWGTIDGRCP
     VDIGKGVGGS TLVNGLIYSR GNRDDYDRWS AAGNDGWSYD EVLPYFRKAE KAIGEGLDRD
     FRSNSGPLRI ERSSFRSEHA RIYMEAAKAA GYNEVDYNGR TQFGIAPVQA TMTKGQRLTA
     YNAYLQPVQK KRTNLKTLTG ALVTKILIDP DTKQTEGVQF TRNGQQYEVR ARKEVILSAG
     AILSPQLLMV SGVGPREHLE SVGVPVLVDL PVGESLYDHL GFSGLQIVMN GTGFFAPGDI
     PTFENFYEYL KGKGVLTVPA AVELVTYPNL TLAGRRGPTL ELMNLISSFA VDKGTTAKQS
     VRMRDDVYEA VYRPLETQNH FTIIVQNLHP LSRGSVRLRS GNPAQPPIVD PNYLAEELDV
     DVVLEGIREV QRVLETDELR RYGATVWTSG RLPNCAEHEP DSDDYWRCAV RTVSFSLTHF
     MGSCKMGPPT DADAVVAPDL KPYGLERLRV VDASVIPEPV SAHPMAAVYM LAERAADLIR
     LEHLP
//
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