ID A0A0V0XWD7_TRIPS Unreviewed; 1104 AA.
AC A0A0V0XWD7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase 1 {ECO:0000313|EMBL:KRX92285.1};
GN Name=Uggt1 {ECO:0000313|EMBL:KRX92285.1};
GN ORFNames=T4E_321 {ECO:0000313|EMBL:KRX92285.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX92285.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX92285.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX92285.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX92285.1}.
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DR EMBL; JYDU01000115; KRX92285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XWD7; -.
DR STRING; 6337.A0A0V0XWD7; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054815; 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:UP000054815};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRX92285.1}.
FT DOMAIN 1..178
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 233..278
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 307..421
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 488..597
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 819..1079
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 200..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 127117 MW; D4EB02560CCBD504 CRC64;
MEASEFMSKE SNEKFWQFIE AVIDKHQTSQ GNETDREIYS GILQIGEQIL KSKARLEFLK
LALTVRVHSA TVEMHRQIAA TSLDVQSDKS IYAVVHGKQI SDLQQLDTIL KHAEALARPV
TYDFDHEYPG SKHGSVCVLL YADIENPHFK RWHLHLKKLV QRDGISYILR HYPKMNDDTV
ALSGYAVELA IKSTEYKAVD DSDKQTDSES GVSSSEEEVT DLNGFNLHLL EADELTPLKV
WQLQHLSFQA GQRVMLAPKE EALRVLRDIS QNFPIMARKD FTLLYAVKGN DPSAEYAVDY
TQWSPQIFVL RLGDRASQNL LSTAYQMYEH VLPIRIGFIF VVNNDKSVSG YDDAGVAMLN
AFNFIKEDRS VSKAVMFLIK IYNTSMRETI SVEDVHKLFK SSYRDKNLKS IFNSEEYNEG
RSISSEHIEE AILSKVMRFT ADIQKDVYEG NLKENMDVQQ HLLKKPTVLP KLNYNILQME
NIFLDMTDTA MDMRIALIHN PKNEVQATKG IASLVQACIQ FLPLYQSKAV IGKIFANKIA
TLEDLINLSL SGISWSEFTK AYNSMSDIWI QLHVHYAKFV LNLDPGVGGI VANGKLLLYS
CVQIEASDPA AAQFDIVAIV DPLSAAAQKM SHLLVILSSV LNAHMKVCMN CKSKLSEIPL
KNFFRMVLPR ELEFAEDGSL KTQPSARFSA LPQKQLFTLN ILAPQSWMVE SVEAVYDLDN
IKMEEVKGDV MAKFQLEYIL LEGRCFDERS GSPPRGLQFT LGTFQEPFMF DTIVMANLVA
KKNDQLENEL LAESEDAESE SLWQSISKTF QSGEKYDMIN IFSLASGHLY ERFLRIMMLS
VLKHTKTAVK FWLLKNYLSP GFKEFLPYMA GHYNFSYELV QYKWPRWLHQ QTEKQRIMWG
YKILFLDVLF PLDVKKIIFV DADQVVRTDM LNLMELDLEG APYAYTPFCD SRKEMDGYRF
WKQGYWENHL SGRKYHISAL YVVDLKKFRQ VAAGDRLRGQ YHFLSRDPNS LSNLDQDLPN
NMIHQVKIKS LPQEWLWCET WCDDKSKKFA KTIDLEPKLQ SAMRIIEEWK DYDSEIKDLL
DQRMKDKWSI AEQKIQVTEQ KMLR
//
