ID A0A182RZF1_ANOFN Unreviewed; 1560 AA.
AC A0A182RZF1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=UDP-glucose:glycoprotein glucosyltransferase {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:AFUN011682-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:AFUN011682-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN011682-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC mannose isomer 9A1,2,3B1,2,3) + UDP-alpha-D-glucose = H(+) + N(4)-
CC (alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:61304, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:59080, ChEBI:CHEBI:139493;
CC Evidence={ECO:0000256|ARBA:ARBA00034426};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC {ECO:0000256|ARBA:ARBA00006351}.
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DR STRING; 62324.A0A182RZF1; -.
DR EnsemblMetazoa; AFUN011682-RA; AFUN011682-PA; AFUN011682.
DR VEuPathDB; VectorBase:AFUN011682; -.
DR VEuPathDB; VectorBase:AFUN2_013661; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000075900; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd06432; GT8_HUGT1_C_like; 1.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR InterPro; IPR040525; UGGT_TRXL_4.
DR PANTHER; PTHR11226; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11226:SF0; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF18403; Thioredoxin_15; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 51..234
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 311..441
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 451..697
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 731..949
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1256..1523
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 252..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1560 AA; 175597 MW; 5872CF6E6F3C33CE CRC64;
MPPFAMRKVS LTHFVPIVAV AFLCLFGVAF VHGEQKSHPI TTQLSAKWGI TPVQLEIAEF
IDEESANSFW DYVDLLNKVS GGLYHLETEE KRYQKSIELA SDILGDGQIG LLKLALSLHS
FSPKVQAHLQ VATEVLAKGD CETTIFASVN GKVACEVIDL VSILRSGTKD SSSVETFAID
HIYPGSENNS LTVVLYGEIG TREFKEFHDA IKLETEHGTV RYVLRHYVRK VSSRKVRLSG
YGVELHLKST EYKSQDDSPR AQDSSATADS SADSTDELEA EVEGFDFAQL KKRFPHLSHP
LDRFRNALLE KHEEIAPLKA WEFQELGLQA AQRIAEMQGD EALQMLQFIS QNFPTQAKSL
LTQTVPEDFK KEMRHNIEVF GRNLNLQPPD SALFLNGLFF DAETIDTVTL LDTLRSEMRV
LEGLNRINIR GGSATPLLGL DLSSSSKEFA IDIRDSAITW INDLENDAQY RRWPGSLKDL
LRPTFPGMLR NIRKNLFNLV LVVDPVEGDS AGRDIVKLAE SFVVHMAPVR IGLVFRTGEG
EDYRALTCGF NYVQQKKSAT EALGFLTDLY AATADQKVIR YADVRQVLKK KFNRLKLEEI
DEILGEDSDF DYGRQLAQEF IDRLGLKTVP QALLNGVLLP QSALTSDEFE ETILTEIMQQ
TPTLQKAVYM GDLHEGEPVI DYLMKQPHVM PRLNQRVLSQ DEPHFIDMSG RAHPDLEDIT
ALGQLSNPDL TATLMKNLKY FGGKSTFQKF LGYRVHFLTV WVVGDLREAA SRKQLKNALK
FMKSSSGTRV AFIPNVDGKD AIRSELKKDL NSLVWATINT LEADESYDLV MKLFEAYETD
PGNVASTVPD SVIGFLPATQ MHLKMLRVYC QRVLKLKASA GTVMANGRLL GVFEADEFFD
TEDFGLLESF NALQYTDKIR AAMKLASLSE ADDTPAITSD TIMKLVSILV PRQQSKSRYT
IPTEIQDNHT VVKLSPKRTD QPFFEIVAVL DPASRGAQKL SSLLLLLRDV VNCQMKIFFC
AIDKHSDMPV KTFYRFVVEP ELHFTKDGRL SAGPSAKFVG LPANPLLTQS LNVPENWLVE
VVRSVYDLDN IKLSEINGPV HSEYELEYLL LEGHCFDSTT GSPPRGLQIT LGTEDRPIIV
DTIVMANLGY FQLKANPGAW ILKLRHGKSA DIYDITSADG PNTVHTAEST RVIISSLRSH
VLKLRVTKKP GMAGVDLLGD EKDGAGGGGI WDSISSIVGT GGDSAGSTGT GETEELNIFS
VASGHLYERL LRIMMLSLLK HTKTPVKFWF LKNYLSPQFI DFLPHMAGEY GFQYELVQYK
WPRWLHQQTE KQRIIWGYKI LFLDVLFPLD VKKIIFVDAD QIVRADMKEL NDFELGGAPY
GYTPFCDSRQ EMEGFRFWKQ GYWKNHLQGR KYHISALYVV DLKRFRKIAA GDRIRGQYQA
LSQDPNSLSN LDQDLPNNMI HQVAIKSLPQ EWLWCETWCS SDTLQYAKTI DLCNNPLTKE
AKLTAAQRIV PEWKEYDAEI KRLQAKADDS EHEEQAAMGR DPSNVHSTEE SNVKRQHTEL
//
