ID A0A2K6QS50_RHIRO Unreviewed; 1516 AA.
AC A0A2K6QS50;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=UDP-glucose glycoprotein glucosyltransferase 2 {ECO:0000313|Ensembl:ENSRROP00000031612.1};
GN Name=UGGT2 {ECO:0000313|Ensembl:ENSRROP00000031612.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000031612.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000031612.1}
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 RefSeq; XP_010357218.1; XM_010358916.1.
DR STRING; 61622.ENSRROP00000031612; -.
DR Ensembl; ENSRROT00000056028.1; ENSRROP00000031612.1; ENSRROG00000039464.1.
DR GeneID; 104658810; -.
DR KEGG; rro:104658810; -.
DR CTD; 55757; -.
DR GeneTree; ENSGT00390000004600; -.
DR OMA; FQTHQLF; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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:SF1; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE 2; 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:UP000233200};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1516
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014399519"
FT DOMAIN 45..226
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 297..426
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 438..686
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 715..933
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1231..1498
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
SQ SEQUENCE 1516 AA; 174630 MW; 52CA2D19A35323B4 CRC64;
MAPAKATNVV RLLLGSTALW LSQLGAGTVA ASKSVTAHLA AKWPETPLLL EASEFMAEES
NEKFWQFLET VQELAIYKQT ESDYSYYNLI LKKAGQFLDN LHINLLKFAF SIRAYSPAIQ
MFQQIAADEP PPDGCNAFVV IHKKHTCKIN EIKKLLKKAA SRTRPYLFKG DHKFPTNKEN
LPVVILYAEM GTRTFSAFHK VLSAKAQNEE ILYVLRHYIQ KPSSRKMYLS GYGVELAIKS
TEYKALDDTQ VKTVTNTTVE DETEANEVQG FLFGKLKEIY SDLRDNLTAF QKYLIESNKQ
MTPLKVWELQ DLSFQAASQI MSTPVYDAIK LMKDISQNFP IKARSLTRIA VNQHMREEIQ
ENQKDLRDRF KIQPGDARLF INGLHVDMDV HDSFSILDML KLEGKIMNGL RNLGINGEDM
SKFLKLNSHI WEYTYVLDIR HSSIMWINDL ENDDLYITWP TSHEKLLKPV FPGSIPYIRR
NFHNLVLFID PAQEYTLDFI KLADLFYSHK VPLRIGFVFI LNTDDEVDGA NDAGVALWRA
FNYITEEFDI SEAFISIVHM YQQVKKDQNI LTVDNVKSVL QNTFPHANVW DILGINSKYD
EERKTGASFY KMTGLGPLPQ ALYNGEPFKH EEMNIKELEM AVLQRMVDAS VYLQREVFLG
TLNDRTNAID FLMDRNNVVP RINSLILHAN QQYLNLISTS VTADVEDFST FFFLDSQDKS
AVIAKNMYYL TQDDDSKISA VTLWIIADFD KPSGRKLLFN ALKHMKTSVH SRLGIIYNPT
SKINEENTAI SRGILAAFLT QKTGFLRSFL GQLAKEETAT AIYSGDKIKT FLIEGMNKNA
FEKKYNTVGV NIFRTHQLFC QDVLKLRPGE MGIVSNGRFL GPLDDDLYAE DFYLLEKITF
SNLGEKIKDI VENMGINSNN TSDFIMKVDA LMSSLPKRAS RYDVTFLREN HSVIKMNPQE
NDMFFDVIAI VDPLTREAQK MAQLLIVLGK IINMKIKLFM NCRGRLSEAP LESFYRFVLE
PELMSGANDV SSLGPVAKFL DIPESPLLTL NMITPEGWLV EIVHSNCDLD NIHLKDTEKT
VTAEYELEYL LLEGHCFDKV TEQPPQGLQF TLGTKNKPVV VDTIVMANHG YFQLKANPGA
WILRLHQGKS EDIYQIIGHE GTDSQADLED IIVVLNSFKS KILEVKVKKE TGKIKEDILT
DEDEKTKGIW DSIKSFTIRL HKEDKKEKDV LNIFSVASGH LYERFLRIMM LSVLRNTKTP
VKFWLLKNYL SPTFKEVIPH MAKEYGFQYE LVQYRWPRWL RQQTERQRII WGYKILFLDV
LFPLAVDKII FIDADQIVRH DLKELRDFDL DGAPYGYTPF CDSRREMDGY RFWKTGYWAS
HLLRRKYHIS ALYVVDLEKF RRIGAGDRLR GQYQALSQDP NSLSNLDQDL PNDMIYQVAI
KSLPQDWLWC ETWCDDESKQ RAKTIDLCNN PKTKEPKLKA AARIVPEWVE YDAEIRQLLD
HLENKKQDTI LTHDEL
//
