ID U3DBX1_CALJA Unreviewed; 1556 AA.
AC U3DBX1; F7H6Y8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=UDP-glucose glycoprotein glucosyltransferase 1 {ECO:0000313|Ensembl:ENSCJAP00000020310.4};
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase 1 {ECO:0000313|EMBL:JAB10791.1};
GN Name=UGGT1 {ECO:0000313|EMBL:JAB10791.1,
GN ECO:0000313|Ensembl:ENSCJAP00000020310.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB10791.1};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000020310.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB10791.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB10791.1}, Cerebellum
RC {ECO:0000313|EMBL:JAB51295.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB25611.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB19834.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB38337.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000020310.4}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GAMT01001070; JAB10791.1; -; mRNA.
DR EMBL; GAMS01003302; JAB19834.1; -; mRNA.
DR EMBL; GAMR01008321; JAB25611.1; -; mRNA.
DR EMBL; GAMQ01003514; JAB38337.1; -; mRNA.
DR EMBL; GAMP01001460; JAB51295.1; -; mRNA.
DR RefSeq; XP_002749272.1; XM_002749226.3.
DR Ensembl; ENSCJAT00000021456.5; ENSCJAP00000020310.4; ENSCJAG00000010861.5.
DR GeneID; 100402843; -.
DR KEGG; cjc:100402843; -.
DR CTD; 56886; -.
DR eggNOG; KOG1879; Eukaryota.
DR GeneTree; ENSGT00390000004600; -.
DR HOGENOM; CLU_002668_1_1_1; -.
DR OrthoDB; 1734at2759; -.
DR TreeFam; TF300320; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008225; Chromosome 6.
DR Bgee; ENSCJAG00000010861; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:JAB10791.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..232
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 312..441
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 451..699
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 725..955
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1257..1524
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
FT REGION 1534..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1556 AA; 177282 MW; 05CD86D96357F976 CRC64;
MGSKGDASGA CAAAALPVTG VCCKMGVLIV LMVLWLFSSV KADSKAITTS LTTKWFSTPL
LLEASEFLAE DSQEKFWNFV ETSQNVGSSD HHDTDYSYYH AILEAAFQFL SPLQQNLLKF
CLSLRSYSAT IQAFQQIAAD EPPPEGCNSF FSVHGKKTCE FDSLETLLLT ASERPKPLLF
KGDHRYPSSN PESPVVIFYS EIGSEEFSNV HRQLVSKSNA GKISYVFRHY IFNLRKEPVY
LSGYGVELAI KSTEYKAKDD TQVKGTEVNT TVIGENDPID EVQGFLFGKL RDLHPDLEGQ
LKELRKHLVE STNEMAPLKV WQLQDLSFQT AARILASPVE LALVVMKDLS QNFPTKARAI
TKTAVSSELR TEVEENQKYF KGTLGLQPGD SALFINGLHI DLDTQDIFSL FDVLRNEARV
MEGLHRLGIE GLSLHNVLKL NIQPSEADYA VDIRSPAISW ANNLEVDSRY NSWPSSLQEL
LRPTFPGVIR QIRKNLHNMV FIVDPAHETT TELINTAEMF LSNHIPLRIG FIFVVNDSED
VDGMQDAGVA VLRAYNYVAQ DVDDYHAFQT LTHIYNKVRT GEKVKVEHVV SVLEKKYPYV
EVNSILGIDS AYDQNRKEAR GYYEQTGVGP LPVVLFNGMP FEKEQLDPDE LETITMHKIL
ETTTFFQRAV YLGELPHDQD VVEYIMNQPN VVPRINSRIL TAERDYLDLT ASNNFFVDDY
ARFTTLDSQG KTAAVVNSMN YLTKKGMSSK EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD
AIRHQKSSNN VRISMINNPA KEISYENTQI SRAIWAALQT QTSNAAKNFI TKMAKEGAAE
ALAAGADIAE FSVGGMDFSL FKEVFESSKM DFILSHAMYC RDVLKLKKGQ RAVISNGRII
GPLKDSELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV DALLSAQPKG
DARIEYQFFE DRHSAIKLRP KEGETYFDVV AVVDPVTRDA QRLAPLLLVL AQLINMNLRV
FMNCQSKLSD MPLKSFYRYV LEPEISFTSD NSFAKGPIAK FLDMPQSPLF TLNLNTPESW
MVESVRTPYD LDNIYLEEVD SVVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP
VIVDTIVMAN LGYFQLKANP GAWILRLRKG RSEDIYRIYS HDGTDSPPDA DEVVIVLNNF
KSKIIKVKVQ KKADMVNEDL LSDGTNENES GFWDSFKWGF TGGQKTEEVK QDKDDIINIF
SVASGHLYER FLRIMMLSVL KNTKTPVKFW FLKNYLSPTF KEFIPYMANE YNFQYELVQY
KWPRWLHQQT EKQRIIWGYK ILFLDVLFPL VVDKFLFVDA DQIVRTDLKE LRDFNLDGAP
YGYTPFCDSR REMDGYRFWK SGYWASHLAG RKYHISALYV VDLKKFRKIA AGDRLRGQYQ
GLSQDPNSLS NLDQDLPNNM IHQVPIKSLP QEWLWCETWC DDASKKRAKT IDLCNNPMTK
EPKLEAAVRI VPEWQDYDQE IKQLQIRFQK EKETGTLYKE KTKEPSREGP QKREEL
//
