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Database: UniProt
Entry: A0A099ZE34_TINGU
LinkDB: A0A099ZE34_TINGU
Original site: A0A099ZE34_TINGU 
ID   A0A099ZE34_TINGU        Unreviewed;      1518 AA.
AC   A0A099ZE34;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=UDP-glucose:glycoprotein glucosyltransferase 1 {ECO:0000313|EMBL:KGL80036.1};
DE   Flags: Fragment;
GN   ORFNames=N309_07793 {ECO:0000313|EMBL:KGL80036.1};
OS   Tinamus guttatus (White-throated tinamou).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX   NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL80036.1, ECO:0000313|Proteomes:UP000053641};
RN   [1] {ECO:0000313|EMBL:KGL80036.1, ECO:0000313|Proteomes:UP000053641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL80036.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL892761; KGL80036.1; -; Genomic_DNA.
DR   STRING; 94827.A0A099ZE34; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000053641; Unassembled WGS sequence.
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:UP000053641};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGL80036.1}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1518
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001957941"
FT   DOMAIN          36..217
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18400"
FT   DOMAIN          291..420
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18401"
FT   DOMAIN          430..678
FT                   /note="UGGT thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18402"
FT   DOMAIN          706..934
FT                   /note="UDP-glucose:glycoprotein glucosyltransferase
FT                   thioredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18403"
FT   DOMAIN          1236..1503
FT                   /note="Glucosyltransferase 24 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF18404"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL80036.1"
FT   NON_TER         1518
FT                   /evidence="ECO:0000313|EMBL:KGL80036.1"
SQ   SEQUENCE   1518 AA;  173170 MW;  0C26140DB46D3794 CRC64;
     YKMGILIAIL GIWFSSSLAK GDSKAVTTSL TTKWSSTPLL LETSEFLSEE GQERFWNFVE
     ASQNINSSQH DGSDYSFYHE MLKVACRNLS PLQQNLLKFS LSLRSYSAAV QAFQQIAADE
     PPPKGCSLFF VVHGEKTCEF DSLGNLLQMA PERPRPFLFR GDHRYPAASP GAPVVILYAE
     IGTEEFYRFH KLLALKAEAG EITYVLRHYI ANPSKEKVYL SGYGVELAIK STEYKAKDDT
     QVKGTDVNAT VIDENDPVDE VQGFLFGKLR QLYPDLTEEL KELRKHLVES TNEMAPLKVW
     QLQDLSFQTA ARILAAPPVD ALMVMKDLSQ NFPTKARAIT KTVVSSELRT EIEENQKYFK
     GTLGLQPGDS ALFINGLHID LDTQDIFSLI DVLRNEARVM EGLHSLGIEG LSLHNVLKLN
     IQPSDSDYAV DIRSPAISWI NNLEVDSRYN SWPSNVQELL RPTFPGVIRQ IRKNFHNFVL
     IVDPTHETTA ELFNVAEMFF SNHIPLRIGL VFVVNDSDDV DGLQDPGVAL LRAYNYVAQE
     MDNNYAFQAV MSIYNKVKTG DQLRVEHVVS VLEKQYPYVE VNSILGIDSA YDQNRKAARS
     YYEQTGVGPL PVVLFNGMPF QKDQLDPDDL ETVTMHKILE TTSIFQRAVY LGELSNDQDV
     VEYIMNQPNV VPRINSRILM SDREYLDLTA MNNFYVDDYA RFTTLESKDK TAAVANSMTY
     LTKKGMSSKE IYDDSFVRPV TFWIVGDFDK PSGRQLLYDA IKHQKSSNNV RISMINNPSE
     DPNSKNTLVA KAIWAALQTQ TSNNAKNFIT KMAKEENAEA VEAGADILEF AVGGMDINVF
     KEAYESPRVD FILSHAIYCR DVLKLKKGQR AVISNGRIIG PLEDGEMFNQ DDFHLLENII
     LKTSGQKIKS QIQQLGFEED LASDLVMKVD ALLSAQPKGE ARIEYHFFEE QYSAVKLRPK
     EGETYFDVVA IADPVTREAQ RLAPLLLVLN QLINMNLRVF MNCQSKLSDM PLKSFYRYVL
     EPEISFTAEN NFASGPIAKF LDMPQSPLFT LNLNTPESWM VESVRTPYDL DNIYLEEVDN
     VVAAEYELEY LLLEGHCYDI TTGQPPRGLQ FTLGTSTSPV IVDTIVMANL GYFQLKANPG
     AWTLRLRKGR SEDIYRIYSH DGTDSPPEAS EVIVVLNNFK SKIIKVKVQK KMDMMNEDLL
     SDGTNENESG FWESLKWGFT GGQKTEDVKQ DKDDVLNIFS VASGHLYERF LRIMMLSVLK
     HTKTPLKFWF LKNYLSPTFK EFIPYMAEKY NFQYELVQYK WPRWLHQQTE KQRIIWGYKI
     LFLDVLFPLA VDKILFVDAD QIVRTDLKEL RDFNLDGAPY GYTPFCDSRR EMDGYRFWKS
     GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG LSQDPNSLSN LDQDLPNNMI
     HQVPIKSLPQ EWLWCETWCD DSSKKRAKTI DLCNNPMTKE PKLQAAMRIV PEWQDFDQEI
     KQLQSRFQEE KETGAPAK
//
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