ID A0A3B3T2Y8_9TELE Unreviewed; 1533 AA.
AC A0A3B3T2Y8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=UDP-glucose glycoprotein glucosyltransferase 1 {ECO:0000313|Ensembl:ENSPKIP00000037224.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000037224.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000037224.1}
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; ENSPKIT00000018186.1; ENSPKIP00000037224.1; ENSPKIG00000015319.1.
DR GeneTree; ENSGT00390000004600; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000261540; Unplaced.
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 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..1533
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017434390"
FT DOMAIN 34..214
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 288..423
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 427..675
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 705..931
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1233..1499
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1511..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1533 AA; 173550 MW; B2EE07BCE14D6F12 CRC64;
MHFLLVAFLA CLLVPHTQGD SKAITTSLTT KWPSTPLLLE ASEFFAEESQ ELFWNFVELN
QNIDDEHDGT DQSYYQLILE RAGTLLSQLQ LSMLRFSLSL RVYSSTVYAF QQIASNEPPP
EGCQAFFSVH GQRSCSVEHL KALLESAPDR PKPFLFKGDH KFPGSDPDAP VVILYAQMGS
REFPRLHQLF VSKANKGEVT YVLRHFMPNP SSSKVFLSGY GVELAIKNQE YKAKDDTQVQ
GADVNATVIG ESDSVDEVQG FLFGKLKTLY PELKEQLKEL RKHLVESTNE MAPLKVWQMQ
DLSFQTAARI LAAPSVDALT VMRDLSQNFP NKARSITRTM VNSEIRREIE ENQKYFKGTL
GLQPGDSGLF INGLHIDLDL HDIFSLLETL RNEARAMEGL HSLHLDSPVI HDMLHLNVQP
SDSDYAVDIR SPAVYWINNL ETDGRYASWP ANVQELLRPT FPGVIRQIRK NFHNLLIILD
PVHENTVELL SVAEMFLSNN IPLRIGLVFV VSDADEVDGM EDAGVAMLRA FNYIADEIDN
QHAFDALISM FNRVPSGGSL KVEHVVGVLE KRYPYVEVGS ILGADSSYDK NRKEGRAYYQ
QTGVGPLPVV LYNGMPYQRD QLDPDELETV TMHKILETTS FYQRAVYLGE LGSDQDVVDF
IMNQPNVVPR INSRILSPNR PYLDLSSTHN HFIDDYARFL FLNTKEKSGA VANSMSYLTK
KGMGSVDSYD DGVIRPVTFW VVGDFDQPDG RQLLYDAIRH MKSSNNVRLG LINNPAEGPS
NGTSRVARAI WAALQTQSAN NAKNFITKLA KEETAMALGA GLDIVEFAVG GMDVPLFMSV
YESAKVGFLL SHAAYCRDVL KLRKGQRAVI SNGRIIGPLD EGEIFNQDDF LLLESIILKT
SGERIKSKIE NLGLEEDGAS DLVMKVDALL SSQPKGEARV EHTFFEDRYS AVKIRPRENE
VYFDVVAVVD PVTRDAQKLV PLLTTLKTLV NINLRVFMNC QSKLSDMPLK SFYRYVLEPE
ISFTADGTFA PGPMAKFLDM PRTPLFTLNL NTPESWMVES VRTRYDLDNI YLEEVDGVVS
AEYELEYLLL EGHCFDVTTG QPPRGLQFTL GTAADPVIVD TIVMANLGYF QLKANPGAWI
LKLRKGRSDD IYKIYSHEGT DSLPEADDLI VVLNSFKSKI IKVKVQKKPD KINEELLSDG
TPDDEAGLWS SLKRTFTGTE KVDESKEEKD DIINIFSVAS GHLYERFLRI MMLSVLKNTK
TPVKFWFLKN YLSPSFKEFI PYMAEEYGFQ YELVQYKWPR WLHQQTEKQR IIWGYKILFL
DVLFPLAVDK ILFVDADQIV RTDLKELRDL DLDGAPYGYT PFCESRHEMD GYRFWKSGYW
ASHLAGRKYH ISALYVVDLK KFRKIAAGDR LRGQYQGLSQ DPNSLSNLDQ DLPNNMIHQV
PIKSLPQEWL WCETWCDDAS KKAAKTIDLC NNPQTKEPKL QAAVRIVAEW SDYDQEIKRI
YNKFLEEKER VGVASGNKTT PGTKTDPSQH TEL
//
