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Database: UniProt
Entry: A0A3P8V305_CYNSE
LinkDB: A0A3P8V305_CYNSE
Original site: A0A3P8V305_CYNSE 
ID   A0A3P8V305_CYNSE        Unreviewed;      1534 AA.
AC   A0A3P8V305;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=UDP-glucose glycoprotein glucosyltransferase 1 {ECO:0000313|Ensembl:ENSCSEP00000008494.1};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000008494.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000008494.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000008494.1}
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; ENSCSET00000008583.1; ENSCSEP00000008494.1; ENSCSEG00000005390.1.
DR   GeneTree; ENSGT00390000004600; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000265120; Chromosome 1.
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:UP000265120};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1534
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018336363"
FT   DOMAIN          50..233
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18400"
FT   DOMAIN          310..439
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18401"
FT   DOMAIN          449..697
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18402"
FT   DOMAIN          723..945
FT                   /note="UDP-glucose:glycoprotein glucosyltransferase
FT                   thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18403"
FT   DOMAIN          1247..1514
FT                   /note="Glucosyltransferase 24 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF18404"
SQ   SEQUENCE   1534 AA;  173890 MW;  8C00B26B2CC82E7B CRC64;
     MSPLLTIFSP GIGVRMWLLW ALLFSLVSAS SAGADSKAVT TTLTTKWADT PLLLEASEFL
     AEESQEKFWD FVESNQNIEG EHDDTDQAYY ELIVKKASAL LSSVQLNMLK FALSLRAYSA
     TVHSFQQCDY IPGDTFIASN EPPPSGCSAF FNVHGEKTCD ADGLDALLKM APERPKPYLF
     KGDHKYSGSN PDAPVVILYA EFGKPHFRDL HEVVASKARE GLVTYVLRHY LAVSRKVYLS
     GYGVELAIKS QEYKAKDDTQ VQGTEVNATV IGENDPVDEV QGFLFGKLKT IYPELKEQLK
     ELRKHLVEST NEMAPLKVWQ MQDLSFQTAA RILAAPAVEA LNVMKDLSQN FPTKARSITK
     TVVNSEIRKE IGDNQKFFKG TLGLQPGDSA LFINGLHIDM DTQDIFSVFE ILRSEARVME
     GLRSLLIDTP FIHDILKLNV QPSDSDYAVD IRNSAINWIN NLEADHRYSS WPSNVQELLR
     PTFPGVIRQI RKNFHNLVMI LDPSQESASE LLSVAEMFYA NNIPLRIGLV FVVSDEDDID
     GMQDPGVALV RAYNYISDEV NSQSAFEAVI SMFNRVPVGA KLSVGDVVKV LEKRFPYVEV
     SSVLGADSSY DSNRKEGRAY YEQTGVGPLP VVMYNGIPYQ REQLDSDELE TVTMQKILET
     TSFYQRAVYL GELVSDQDVV DFIMNQPNVV PRINPRVLST SRTYLDLSDT NNYFVDDYAR
     FSTLDTKEKS TAVANSMNYM TKKDDGYIRP VTFWVVGDFD RPSGRKLLYD AIRHMKTSNN
     IRLAMINNPS TDPSAETTRV ARAIWAAMQT QSANNAKNFI TKMAKEETAA TLQEDTDIGD
     FAVGGMDVVL FKSAYDSPQF DVLRSHATYC RDVLKLKKGQ RAVISNGRII GPLEDEEVFN
     QDDFLLLESI ILKTSGERIK NKVQHFEIEE DRASDLVMKV DALLSSQPKG EARVEYDFAD
     DRYSAVKIRP KEGDMYFDVV AVVDPVTRDA QKLAPLLTVL KQLVNVNMRV FMNCQSKLSE
     IPLKSFYRYV LEPEVMFQSD GSYSPGPLAK FLDMPQSPLF TLNLNTPESW MVESVHTRYD
     LDNIYLEEVD NIVAAEYELE HLLLEGHCFD VSSGQPPRGL QFTLGTASEP VIVDTIVMAN
     LGYFQLKANP GAWILKLRKG RSDEIYKIYS HDGTDSPADS DDVIVVLNNF KSRIIKVKVQ
     KKADKLNEEL LSDGTEENDT GFWESLTRGF TGGGKVEEVK QDKDDVINIF SVASGHLYER
     FLRIMMLSVR KHTNTPVKFW FLKNYLSPTF KEFIPHMAKE YGFQYELVQY KWPRWLHQQT
     EKQRIIWGYK ILFLDVLFPL AVDKILFVDA DQIVRTDLKE LRDLDLEGAP YGYTPFCESR
     REMDGYRFWK SGYWASHLAG RKYHISALYV VDLKKFRKIA AGDRLRGQYQ GLSQDPNSLS
     NLDQDLPNNM IHQVPIKSLP QDWLWCETWC DNSSKKNAKT IDLCNNPMTK EPKLQAAVRI
     VAEWTDYDQE IKRLQTRVQE GATLRPQEQQ GTGS
//
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