ID A0A1L8HH73_XENLA Unreviewed; 1518 AA.
AC A0A1L8HH73;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase 2 {ECO:0000313|RefSeq:XP_018102735.1};
GN Name=uggt2.L {ECO:0000313|RefSeq:XP_018102735.1,
GN ECO:0000313|Xenbase:XB-GENE-17339524};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018102735.1};
RN [1] {ECO:0000313|RefSeq:XP_018102735.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018102735.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018102735.1};
RG RefSeq;
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}.
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DR RefSeq; XP_018102735.1; XM_018247246.2.
DR STRING; 8355.A0A1L8HH73; -.
DR PaxDb; 8355-A0A1L8HH73; -.
DR GeneID; 108708482; -.
DR KEGG; xla:108708482; -.
DR AGR; Xenbase:XB-GENE-17339524; -.
DR CTD; 108708482; -.
DR Xenbase; XB-GENE-17339524; uggt2.L.
DR OMA; FQTHQLF; -.
DR OrthoDB; 1734at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 108708482; Expressed in egg cell and 17 other cell types or tissues.
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: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:UP000186698};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1518
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035242684"
FT DOMAIN 38..216
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18400"
FT DOMAIN 290..419
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 430..677
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 708..928
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1227..1494
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
SQ SEQUENCE 1518 AA; 172691 MW; EB9D4C1DE4B78CB0 CRC64;
MQSPFILCFF FSLALSSALA QASSKGVTAS LAAKWPGSPF LLEASEFIAE EGNDKFWQFL
ATVQELTIYK NKDTEYSYYT LILKKAAQFL SDLQIALLKF AFSIRAYSPT IQMFQQIAAD
EPPPEGCSAF VAVHGMHTCK PSQIKKLLKE ASERSRPYLY KMDHTFPTLS KTAPVVILYA
EVGTKEFAKF HKTLAEKAES GEIIYVLRHY IQHPGTRKML LSGYGVELAI KNTEYKAMDD
TQVEANNSSP TSDEGIAEEV QGFYFDKLMQ MYPDLKENLA EFRKHLIEST NEMVPLKVWE
LQDLSFQAAS KIVSTPVYEA LKVLRDMSQN FPIKARSLTK VALNQEMKKE IEENQKHLSE
TFGIHPGDAS LYINGLHIDL DVHNSFSILE TLGTEGKTLN GLSALGIKNE DLGNYLRIQV
HSSDENYALD IRHSSITWIN DIETDHMYSP WPSSVQELLR PAFPGVIRPI RRNFFNLVLF
VDPVQENAAD YLKLAELFYR HNVPLRIGFV FVINSDEKVN TGEDAGAAFL QAFNYIAEES
DSAQAFSFII NMYNKVNDGE TLTVDIIKSV LKHDLPKVDV DEVMGLHSEN NNKIKAGATF
YKKSGLGPLP QVLFNGVPFN SEEMDIEEME TVILQKILDA TGFFQRAVFM GLLSDQFDAV
DFLMDQPNVV SRMNPSILTS EKNYINFISP SVAPKYTLND FDTFSFLDLQ DKSAVIAENM
KYLTKEDEDV IHAVTIWIIA DFDKPAGRQL LSTALKHLKK TSISRLGILN NPTIKIIEEN
TLISRALWAA LLTQKNQNMF KLLKRLSKEE TAEALFNGKK IKEFLAPEID DDAFEKKYNT
IGLDMLRTQE LYCREVLKLL PGQMATVSNG RLLTSTDGDE FSEDDFHLLE KVTYSTSAEK
IKNLVKKTTT LSNSAASNLV MKVDSLLSSV PKGESRQDVT LIKQKHSLVK VEPQDDGPFF
DVMAIVDPLS REAQMMSHFL IVLGRLINMK LSMFMNCKPK LSEMPLKSFY RLVLEPEVTF
LRNNSLSMGP SAKFLDMPES PLLTLNMITP ESWIVEAVQS SCDLDNIHLQ DIDGIVTANY
ELEYLLLEGH CFDVTTGQPP RGLQFTLGVK NDPVMVDTIV MANLGYFQLK ANPGAWTLRL
REGRSEEIYH IFSHMGTDSP SDQVEIIVVL NNFNSKIIKV HVQKKPDQMH ADLLSSESEE
KSGLWNSLMS FTGAGNSEDK EKKHDVLNIF SVASGHLYER FLRIMMLSVL RNTKTPVKFW
FLKNYLSPKF KEIIPFMAEK YGFQYELVQY KWPRWLHQQT EKQRIIWGYK ILFLDVLFPL
AVDKIIFVDA DQIVRADLNE LREFNLGGAP YGYTPFCDSR KEMDGYRFWK SGYWASHLGH
RKYHISALYV VDLKKFRKIA AGDRLRGQYQ ALSQDPNSLS NLDQDLPNNM IHQVAIKSLP
QEWLWCETWC DDKSKEKAKT IDLCNNPKTK EPKLKAAARI VPEWTQYDTE IRQLLKHIEE
ESRNITASSV NGLKHDEL
//
