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
//