ID A0A3P8XBE6_ESOLU Unreviewed; 1486 AA.
AC A0A3P8XBE6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase 1 {ECO:0000313|Ensembl:ENSELUP00000001960.2};
GN Name=UGGT2 {ECO:0000313|Ensembl:ENSELUP00000001960.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000001960.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000001960.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000001960.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 Ensembl; ENSELUT00000016528.2; ENSELUP00000001960.2; ENSELUG00000003443.2.
DR GeneTree; ENSGT00390000004600; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000265140; LG16.
DR Bgee; ENSELUG00000003443; Expressed in liver and 14 other cell types or tissues.
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:SF1; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 2; 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; 2.
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:UP000265140};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1486
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028429628"
FT DOMAIN 42..222
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 291..418
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 432..551
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 552..635
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 667..885
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1185..1452
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1463..1486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1486 AA; 168521 MW; 614BF511764FC4D6 CRC64;
MTNITRTMRN VLLLSLLLLK VQYVQSTSKG VSASLKAKWS MTPFLLETSE FIAEDGNEKF
WHFVDTVKEL TIYKNGESVR SYYNLVIKKA GQFLTELQVN LLKFALSLRS YSPAVYASQK
IASDEPPPEA CLAFVSVHGQ HGCSTKDLKK LLKAAAARPN PYLYKNDHKY PGLNGTDVPV
VILYAEIGTK KFGSFHKVLA EKAAAGKLIY VLRHFVAEPK PQKMLLSGYG VELAIKSTEY
KAVDDTQVKG TINTEEDDID EVQGFLFGKL KKSHPNLQKQ FGELRKYLLE STNDMAPLKV
WELQDLSFQA AASIMSVPRF DALKLMRDLS QNFPSKARSL TRVAVNQEMR KEIEDNQKGL
SETMGIHPGD GGLFINGLHI DLDVHNPFSI LDTIRGEAKI LEGLHNLGIK GDHLGKLLRL
PMNPVEENYA LDIRHPAITW INDIETDSMY RSWPSGVQEL LRATFPGVIR QIRRNLFNLV
LFLDPVQEES VELVKLAELF YKHKIPLRIG FVFVVNTDDK VDGNTDAGVA FFRLLNYIAD
EYDLSHALMS MVSAGALFYK KSGLGSLPLA LFNGVPLSAD EMDPDELETV ILQRIMDTTN
FFQRAVYMGQ LTEGTDVVEH LMDQPNVVPR INPLVLSTDR TYLDLTASPV ADEWEDTTMF
SYLDYKDKTA VIAKRMKYFT KNDEDGINGV TVWIIGDFEK ASGRRLLLNA LKHMRASSGV
RVGVIDNPSG RVASEDNTVI YRAVWSTLLT QKSRATLEFV QKILKEETVH LLQQGTKMKD
LLAQGMDSDA FEKRFNTMEV DFIRSQQLFC REVLKLNAGQ GVVVSNGRIL GPFEDEEEFS
VEDFHLLEKI TLRSTAEKIK ARIKQMGRKG KQASDLVMKV DALLAAAPKG EGRRDVRFVK
DKHSVLNFAP REKEVFYDVV AIVDPLTRDA QKMSSLLIVL TQVVNVKLQV FMNCRAKLSE
MPLKSFYRFV LESDVSFLAN ETVSAGPVAR FLELPESPLL TLNMITPESW MVEAVRSPYD
LDNIHLQEVK GVVMAEYELE HLLLEGHCFD LSTGQPPRGL QFTLGMSQDP LMQDTIVMAN
LGYFQLKANP GAWILNLRKG RSEDIYHIQS HDGTDSPADS GDVKVLLNSF HSKIIKVRVQ
KKADKMNEDL LTEATENKGL WDSIASLTGG GSSSEDEDKK REDVLNIFSV ASGHLYERFL
RIMMLSVLQH TKTPVKFWFL KNYLSPSFKE SIPYMAETYG FQYELVHYKW PRWLHQQTEK
QRIIWGYKIL FLDVLFPLAV DKIIFVDADQ IVRADLKELR DLDLEGAPYG YTPFCDSRKE
MEGYRFWKTG YWASHLGNRR YHISALYVVD LKKFRKIAAG DRLRGQYQAL SQDPNSLSNL
DQDLPNNMIH QVAIKSLPQE WLWCETWCDN ASKTTAKTID LCNNPKTKEP KLSAAVRIVP
EWVDYDNEIK QLLTNVQKRK EEATQIQTQA HSLSSPEKTG SQRDEL
//
