ID A0A443SJB6_9ACAR Unreviewed; 1560 AA.
AC A0A443SJB6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase 1-like protein {ECO:0000313|EMBL:RWS27572.1};
GN ORFNames=B4U80_10989 {ECO:0000313|EMBL:RWS27572.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS27572.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS27572.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS27572.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS27572.1}.
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; NCKV01001919; RWS27572.1; -; Genomic_DNA.
DR STRING; 299467.A0A443SJB6; -.
DR EnsemblMetazoa; LDEU004470-RA; LDEU004470-PA; LDEU004470.
DR VEuPathDB; VectorBase:LDEU004470; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000288716; 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 Reference proteome {ECO:0000313|Proteomes:UP000288716};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RWS27572.1}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1560
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019461408"
FT DOMAIN 49..245
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 321..449
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 462..713
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 754..955
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1265..1532
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1538..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1560 AA; 177429 MW; 951806C604EBA0C3 CRC64;
MRLEIHCFAL FALYSVLFVT VKCGKTSKSA TKGSQKSVTV SLNSKWQDTP LLLEAAEYLA
EESQDYFWSF IELFHQKYAS EGWKAGKPKE EYDTVLSLVQ EIVNLPSKIS LLKLSLSLRS
HSPAVGMFNQ IAKEKQKSFQ LNENECSAFV EFSSPSNKPL FACDKNSLLD ALQTLKSTTE
DLTHPFIHKI DHIYPQTHSS SNILILYGEI GTKSFTDLYD VIKEKTKDFS FKFLVRHFVA
RKSRSKVALS GYGVELAIKS TEYKAQDDTR VKGEKSTLVD SEAEGEDKPD EVEGFIFSTL
EKQHPENVAK LNEFRTYLMD SNKEIATLKA WQLQELSLQV AKKIVSSPKE EQLQLLQDIS
QNFPSFAKSL INVIVDNRLK TEVERNQMLF MQHLNLATTD TALFVNGMYF DMDSTDIFTL
LHYLKQEVRL IEGLHKIIGN DATFVKNLLK LEVSGEKNEY QIDIRDSAVV YINDIETDKE
YLNWPSSLQD MLRPTYPGML RNVRRNMFHL VLVVEPGSKS SFDVMKLAES FYIHRAPLRI
GFVFAVNPDM TVNGYKDAGV ACLNAFNFIS EEKTMYEGLS FLTDVIASTE ADTKNRDLQA
DEVIAHFKRK FPKANLELVF GSDSAFDTGR KLSWDFLNRT GIGGPHKALM NGVLLKESHL
NGELFEEAVL TEIMRLTPII QKSIYKGELT DSMNVLDWLM SQKTVMPRLN YRILGSPNSE
SFSRNLDLSS TVIDTSSAEV DSANLHQSEL VSRFHRKLRY LSSSETDCLS VTVWLACNFD
TPEGRNILAS VVEHLKSNSV NMRLGIIHSS NSLLSSVIET ALNTFKTNIS VLNFLSKLLS
AFDDPKFQLD NVSKLVPSDL VEAFESKLKL IKSDESYLSS HTLFRKNVLK IGENDIAVIV
NGKLIEVPKD ELFTERDFAL IEKQVMLTYG EKIRDQLTSK QTEDVDKCTN LVMAIGNVIT
SFPQTKTRHE IHSYESKHSV ISLDAADPSI PAVDLIAVVE PISRGAQKIA PILITLQQAI
NANIKVYLNC VDKHSEMPLK NYFRYVIHSS PTFSEKTGEL IKPRAHFVSM PSSSLLTLGM
VTPDNWLVEA VRCPYDLDNI HLKEVEASGV VADFELAHLL LEGHCFEQSS GNPPRGLQFV
LGTNSTPAVF DTIVMANLGY FQLKSNPGAW NLRLRHGRSQ DLYTIVSHEN TDSAGAHGDV
NVVIHSFRSH IVKIRVNKRP GKQHEELLRD EDDIEADAGI WGSLKSWTTG SAKKNETIDD
ENEKLNIFSV ASGHLYERLL RIMVLSVLKH TTSPVKFWFL KNYLSPAFKD FMPVMAQKYG
FEYELVEYKW PRWLHQQSEK QRIIWGYKIL FLDVLFPLHV KKIIFVDADQ VVRTDLAELR
ELDLEGAPYG YTPFCDSRKE MDGYRFWRSG YWASHLHGRK YHISALYVVD LVKFRRIAAG
DRLRGQYQGL SQDPNSLSNL DQDLPNNMIH QVSIKSLPQE WLWCETWCDD KSKKTAKTID
LCNNPKTKEP KLTAARRIVP EWEGYDNEIR KLLDEYHTEK QKSEHKQPSG DKAHVPHSEL
//
