ID A0A2D0R3Y7_ICTPU Unreviewed; 1537 AA.
AC A0A2D0R3Y7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase 2 isoform X2 {ECO:0000313|RefSeq:XP_017324766.1};
GN Name=uggt2 {ECO:0000313|RefSeq:XP_017324766.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017324766.1};
RN [1] {ECO:0000313|RefSeq:XP_017324766.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017324766.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_017324766.1; XM_017469277.2.
DR STRING; 7998.ENSIPUP00000001456; -.
DR GeneID; 108266228; -.
DR CTD; 55757; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000221080; Chromosome 6.
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; 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, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012632722"
FT DOMAIN 45..225
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 297..424
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 438..685
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 711..935
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1242..1509
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1513..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1537 AA; 174300 MW; 8B5218AEEDB47EEE CRC64;
MAASIKTRHR TMRVLSLVLV LMQLQHAHSA SKGVTASLKA KWPTTPLLLE TSEFIGEAGD
DKFWQFVDTV KELTVYKHGE SVRSYYNLIV KKAGQFLSDL QVSLLKFSLS LRAYSPAVHA
FQQIASDEPP PDACAAFVSV HGQHACSTKN MKKLLKGAAG RPKPYLYKND HKYPGVNGTD
LPVAILYAEI GTKKFNTFHK VLSEKAEEGK LIYVLRHFVA EPKKQHMLLS GYGVELAIKS
TEYKAVDDTQ VKDSKSTATF EEDDTNDVQG FLFGKLRESH PELQEQLGEL RRHLLESTND
MAPLKVWELQ DLSFQAATQI ISVPKFDSLK LMRDLSQNFP SKARSLTRVA VNQEMRKEIE
ENQKRLSKSL GINPGDTSLY INGMHIDLDL HNTFSILDII RGEAKLLEGL HSLGIMGTTL
GKFLRLPVTT VEDGYALDIR HSAIMWVNDI ETDPTYRNWP SSIQELLRAT FPGVIRQVRR
NFFSLVLFLD PVQEESIELV KLAELFYKHK IPLRIGFVFV VNTDEKVDGY MDAGVAFFRV
LNYITEEYDI TQAFLSMVSM YNKVDVGDSL SVDTVTAYLK KKFPKANAAK ILGVDSSYDD
KRKAGAVFYR KSRLGALPVG LFNGVPLSTE EMDPDELETI LLQHIMDATN FFQRAVFMGQ
ISEGTDVVDF LMEQPNVVPR INPLILSSDR RYLDFTASPV SDDWDDSQMF SFLDSKDKTA
VVSKRMKYLT KHEDEMVYGV TFWIVADLEQ ASGRQILLNA LIHMKSSSSS SRVGVINNPS
DQPTEDNSSL YRAIWASFLT QSTKNTLDFT LKLLKEETVQ LLTQGTKIKD LLLKGMDHDA
FEKKFNTMEL GFLNSQQRFC QELLKVKAGQ TAVVSNGRVL GPFAEEEEFS TDDFHLLEKL
TLSTSADKIK AKVKQMNLTP KNACDLIMKV DALLSAAPKT EARKDVKFVK DKHSVLHLSP
REDEVFFDVV ATVDPLTRDA QKLAPLLIVL GQVVNLRVQL FMNCRAKLSE MPLKSFYRFV
MEADVAFLGN DTLSPGPMAR FAEIPESPLL TLNMITPESW MVEAVQSPYD LDNIHLQEVS
GVVNAVYELE YLLLEGHCFD LSTGQPPRGL QFTLGMKQEP LMHDTIVMAN LGYFQLKANP
GAWILRLRKG RSEDIYQIQA HDGTDSPADA GDVIVMLNSF HSKIIKVRVQ KKPEKIDEDL
LSESTESKGL WDSITSVWST LEKSFTGGSS VEEGDTKKED VLNIFSVASG HLYERFLRIM
MLSVLQHTKT PVKFWFLKNY LSPSFKESIP HMAEAYGFQY ELVQYKWPRW LHQQTEKQRI
IWGYKILFLD VLFPLAVDKI IFVDADQIVR ADLKELRDLD LEGAPYGYTP FCDSRREMDG
YRFWKTGYWA SHLGHRKYHI SALYVVDLKK FRKIAAGDRL RGQYQALSQD PNSLSNLDQD
LPNNMIHQVA IKSLPQDWLW CETWCDDVSK ASAKTIDLCN NPKTKEPKLS AAIRIVPEWS
RYDSEIKQLL KQVKGQKESR KSSASQTQHT GSRRDEL
//
