ID A0A0K0E8S0_STRER Unreviewed; 1514 AA.
AC A0A0K0E8S0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase {ECO:0000313|WBParaSite:SSTP_0000590200.1};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000590200.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000590200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) 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 AlphaFoldDB; A0A0K0E8S0; -.
DR STRING; 6248.A0A0K0E8S0; -.
DR WBParaSite; SSTP_0000590200.1; SSTP_0000590200.1; SSTP_0000590200.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000035681; 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:UP000035681};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1514
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005327654"
FT DOMAIN 38..218
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 290..421
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 437..677
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 708..926
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1225..1492
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
SQ SEQUENCE 1514 AA; 174064 MW; BF9E82E4C85D18AA CRC64;
MKWRYTLLLL LFIVKSTYSS NNGGKLVVTS LSAKWNHTSF IAETAEFIGK EDPQLFFKYI
DLLEKKNDIN LDNPEKEYEL GIKLAGEILS ESRLDLLKFS LSLRVASPAI ELFQKLGKEK
IDGKNCNSFV EIGDKFICSP EELEKVLENG NDFNAETYSI DHIFYSKKIK NNENFGTIVL
YGSYGSNDFN KLYNICKKTS KNGKFNFAVR FYDSKEKSEL MPVSLSGYGV ELSIKNTEYK
AIDDSNQKKD NFEDDLPELN DVQGFNFNIL KKKHVDLIEQ LKQLKVFLSE SDELTPLKQW
EVQDISYQAA QKVFNEPNAE AAIDTLIDVS QNFPLRARSI SQVAVDPKLR KEVQANQERL
NDEFEIGPGE NNIFINGISI DADSLDIYNL LDILKQEERL ANDFYEMGYR REYLSLLFSL
DFSESKESFA IDFREAFPEY INNLDKDPEY KKMGNSVKLM LQPYFPGMIR PIARNFFNLI
FVVDPGKADQ LVLLKIAHSF YAHQIPIRIG IIFDVSNDKD VNGMNDVGVA IVNFFNYAKS
EKNSAKALNL CNKMFDALMN NINIEGIHKF FKKNFKDVEI EDVFGKNSDY NQGIATGRSW
IKKSGLGKTP KVLLNGVVFD ESSLALDKIE EAVMNEISKQ TPFIQKAIMN GKLTDKDNVM
NWIMSRPTVL LRLNNRILDN DGKYLKMTNV MPCKFENSDK FDQLSDVEKT QCIISRMKYL
MRSDVESTKP LTVWLVGDMD EFESREMLRN ALKFLKKSKS SRIGIINNPK DGTKKIGKVT
KVINSIIRLL PQNIVKQILP KILVETVVKK IMIDKFSIEE FAVNGMSTDS FNKEAKLLSN
EQIEIESNYA ASVLNLNHGD RTYIVNGKLY GVLEEKEVVE VDDFDLLEKM AITKGANKIA
LQIDRWGVEK ENGKSSDVVM RSISVIGSSN TKKTRHWVVL ANDQKSVVHS ISQDDKKAVI
DIIIVIDPLT KGAQKLSGIL KLILRSCNAD LKIVLNPQDK LSELPLKRFY RFVADQEVSF
TTDGKVISPV AVFENLPKKQ LLTLNVISPD SWMIQPIFAE YDLDNIKMEN VEKNIIAKFE
LRNILLEGHC FDDITGSPPR GLQFVLSTYN RKINYDTIVM ANLGYFQLKS NPGIWDLSLR
EGRSKEIYDI VEHKNTESQN KTVVKVMIDS LLGRVIKIKV SKKSDKLEEN LLSDDKGSYE
DEYDEENSIW SSVSKYVNGE KYDEINIFSL ASGHMYERLM RIMMVSVMKH TKYPVKFWLL
NNYVSPQFRN SLEPMAKKYG FSYELVEYKW PRWLHKQTEK QRIMWGYKIL FLDVLFPLHV
KKIIFVDADQ IVRTDLMELM NFDLNGAPYG YTPFCDNKKE MDGFRFWKTG YWANHLAGRK
YHISALYVVD LVKFRKIAAG DRLRGQYQGL SADPNSLANL DQDLPNNMIH QVKIKSLPQE
WLWCETWCDE GSKKNAKTID LCNNPLTKEP KLDAARRIVP EWIEYDEEIK ELLEKAKISE
VVKDDEKKDT HTEL
//
