ID I3IY77_ORENI Unreviewed; 1582 AA.
AC I3IY77;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=UDP-glucose glycoprotein glucosyltransferase 1 {ECO:0000313|Ensembl:ENSONIP00000001567.2};
GN Name=uggt1 {ECO:0000313|Ensembl:ENSONIP00000001567.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000001567.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000001567.2}
RP IDENTIFICATION.
RG Ensembl;
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 STRING; 8128.ENSONIP00000001567; -.
DR Ensembl; ENSONIT00000001566.2; ENSONIP00000001567.2; ENSONIG00000001242.2.
DR eggNOG; KOG1879; Eukaryota.
DR GeneTree; ENSGT00390000004600; -.
DR InParanoid; I3IY77; -.
DR OMA; KNFYRYV; -.
DR TreeFam; TF300320; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000005207; Linkage group LG19.
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:SF3; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 1; 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:UP000005207};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..45
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 46..1582
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025578869"
FT DOMAIN 63..239
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 317..446
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 456..704
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 735..952
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1279..1546
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1554..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1582 AA; 179330 MW; 45E8C45DFAB49A0C CRC64;
MLIIHSSSMW KSLASLPNSS VPSGVGLRMW LLWIVLLSLL SAASGSADSK AVTTTLTTKW
ADTPLLLEAS EFMAEESQEK FWDFVEANQN IEGEHDDTDQ AYYDLIMKRA SALLSSVQLN
MLKFALSLRA YSATVHSFQQ IASTEPPPSE CSAFLSIHGE KTCDTEKLEA LLKTAPQRTK
PYLFKGDHKY PGSNPDAPVV ILYAQFGTAD FQKLHQVILS KVNEGSVTYV LRHYLASPSR
GKKVYLSGYG VELAIKSQEY KAKDDTQVQG AEVNATMIGE NDPVDEVQGF LFGKLKTLYP
ELKEQLKELR KHLVESTNEM APLKVWQMQD LSFQTAARIL AAPAVDALNV MKDLSQNFPT
KARSITKTVV NSEIRKEIGE NQKFFKGTLG LQPGDSALFI NGLHIDLDAQ DIFSVFEVLR
SEARVMEGLR SLLIETPFIH DILKLNVQPS DSDYAVDIRS PAISWINNLE TDYRYSSWPS
NVQELLRPTF PGVIRQIRKN FHNLVIILDP TQENTVELLS VAEMFYANNI PLRIGLVFVV
SDEDDIDGMQ DAGVALVRAY NYITEEVDSQ NAFEAVMSMY NRVPVGGRLS VGDVVKVLEK
KFPYVEVSSV LGADSSYDSN RKEGRAYYEQ TGVGPLPVVM YNGIPYQREQ LDPDELETVT
MQKILETTSF YQRAVYLGEL ATDHDVVDFI MNQPSVVPRI NPRVLSTSRT YLDLSDTNNY
FIDDYARFST LDTVEKNTAV ANSMNYMTKK DDAYIRPVTF WVVGDFDKPS GRQLLYDAIK
HMKTSNNVRL GMINNPSADV SAETTRVTRA IWSAMQTQTA NNAKNFITKM AKEETAAALE
KGVDVGEFAV GGMDLSLFKS AYEAPKFDFL LSHAAYCRDV LKLKKGQRAV ISNGRIIGPL
EEAEVFNQDD FLLLESIILK TSGERIKSKV QNFGIEEDRA SDLVMKVDAL LSSQPKGEAR
VEYGFADDRY RRETLKRILN MFCLLDLLVD LLFVGSAVKI RPKEGDVYFD VVAVVDPVTR
EAQKLAPLLL VMKQLVNVNL RVFMNCQSKL SEMPLKSFYR YVLEPEVAFQ ADGSFSPGPM
AKFLDMPHSP LFTLNLNTPE SWMVESVHTR YDLDNIYLQE VENIVAAEYE LEHLLLEGHC
FDVSSGQPPR GLQFTLGTES EPVIVDTIVM ANLGYFQLKA NPGAWILKLR KGRSDEIYKI
YSHDGTDSPA DSDDIVVVLN NFKSRIIKVK VQKKPDKFSE ELLSDGTEEN DTGFWNSLTR
GFTSGGKTEE PKQDKEDTIN IFSVASGHLY ERFLRIMMLS VLKHTKTPVK FWFLKNYLSP
TFKEFIPHMA KEYGFQYELV QYKWPRWLHQ QTEKQRIIWG YKILFLDVLF PLAVDKILFV
DADQIVRTDL KELRDFDLEG APYGYTPFCE SRREMDGYRF WKSGYWASHL AGRKYHISAL
YVVDLKKFRK IAAGDRLRGQ YQGLSQDPNS LSNLDQDLPN NMIHQVPIKS LPQEWLWCET
WCDDSSKKSA KTIDLCNNPM TKEPKLQAAV RIVAEWTDYD QEIKRLQARI QDRANHMAKQ
QPTGAPRSRK PIRAAFRINH TD
//
