ID K7F5W8_PELSI Unreviewed; 1297 AA.
AC K7F5W8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=UDP-glucose glycoprotein glucosyltransferase 2 {ECO:0000313|Ensembl:ENSPSIP00000003428.1};
GN Name=UGGT2 {ECO:0000313|Ensembl:ENSPSIP00000003428.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000003428.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000003428.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AGCU01120079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01120080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01120081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01120082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01120083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01120084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01120085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01120086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01120087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01120088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 13735.ENSPSIP00000003428; -.
DR Ensembl; ENSPSIT00000003445.1; ENSPSIP00000003428.1; ENSPSIG00000003272.1.
DR eggNOG; KOG1879; Eukaryota.
DR GeneTree; ENSGT00390000004600; -.
DR HOGENOM; CLU_002668_1_1_1; -.
DR OMA; FQTHQLF; -.
DR TreeFam; TF300320; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
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:InterPro.
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; 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; 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:UP000007267};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 72..198
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18401"
FT DOMAIN 212..459
FT /note="UGGT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18402"
FT DOMAIN 486..707
FT /note="UDP-glucose:glycoprotein glucosyltransferase
FT thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18403"
FT DOMAIN 1006..1273
FT /note="Glucosyltransferase 24 catalytic"
FT /evidence="ECO:0000259|Pfam:PF18404"
SQ SEQUENCE 1297 AA; 148850 MW; 7E8AD8501C82E181 CRC64;
MYLSGYGVEL AIKSTEYKAV DDIQIKATND TTEKEDDEAS EIQGFLFGKL KQMYPDLKDN
LKEFRKHLIE SANNLEPLKV WELQDLSFQA ASQIFSTPVY NVLKVIKGIS QNFPIKARSL
TRIPVNQQMR NEIEKNQKHF HEKLRIQPGE ARLFLNGLPI DLDIHDPFSI LETLKLEGKV
LHGLHELGIK EEAFNKFIRL QIHPVDDICA LDIRHSSIIW VNNIEEDNIY NKWPTSFKEL
LKQTFPGVIQ QIRRNLYNLI LFIDPVQTHA VDFVKLAELF FHHNIPLRVG FVFILNTNEE
VDGNKDAGVA LFRAFNYIRE ESDTTQAFIS MINMYHKMKD GEVFTVNHVR NVLRNEFPHA
DIQSILGVDS DYDDKRKAGA TFYKKTGLGS LPQALFNGVP FIGKEMTAAE LETVILQRIT
DATGFFQRAV FMGLLSDHMD AVDFLLDQHN VVSRINPTVL DTKRTYINFI STSVPVGVED
FSTFSFLDAQ DKSAVISQNM KYLSKKGEDV IYAVTIWIVA DFDKPGGRHL LSKALKHLKT
SNHMRLGIVN NPMSKIMEDN TAIARAILTA FLTQKNSNLK SFLSKISKEE TAKALATGTK
IKKLLVAGMD DSTFEKKYNT IGLDIIQTHQ LFCKEVLKLL PGQMAVVSNG RVLGPLDENE
FHTDDFHLLE KITFSTSAEK IKGIVKEMGI SSQRGSDLIM KVDALLSSLP KRGVRQKVEF
LKEQHSVVKI DPKENEPFYD VIAIVDPLTR EAQKMAHLLI VLGDIVNMKL RLFMNCRSKL
SEVPLKSFYR FVLEPELSSG ADKLFPSGPV AKFLEMPETL LLTLNMIIPE SWLVEAVNSS
YDLDNIHLQD VEGVVTGEYE LEYLLLEGHC FDVATGQPPR GLQFTLGMKN NPVMFDTIVM
ANLGYFQLKA NPGAWTLRLR KGRSEDIYHI FAHEGADSPV HMEDVIVVLN NFRSKILKVQ
VQKKPDKVDE DLLSIGVIEE KGAWESITSF SGDIQTEEKE KKNNVLNIFS VASGHLYERF
LRIMMISVLR HTKTRVKFWF LKNYLSPMFK EIIPHMAKEY QFQYELVQYK WPRWLHQQTE
KQRIIWGYKI LFLDVLFPLA VNKIIFVDAD QIVRSDLKEL RDIDLNGAPY GYAPFCDSRR
EMDGYRFWKS GYWASHLGRK KYHISALYVV DLKTFRKIAA GDRLRGQYQA LSQDPNSLSN
LDQDLPNNMI HQLAIKSLPQ EWLWCETWCD DESKKKAKTI DLCNNPKTKE PKLQAALRIV
PEWVQYDSEI RKLIKQIEKE KKNLTHTSRK VLKHDEL
//
