ID   LGE1_CAEEL              Reviewed;         631 AA.
AC   Q21389;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Glycosyltransferase-like protein LARGE;
DE            EC=2.4.-.-;
GN   Name=lge-1; ORFNames=K09C8.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Probable glycosyltransferase. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR   EMBL; Z68006; CAA91997.4; -; Genomic_DNA.
DR   PIR; T23541; T23541.
DR   RefSeq; NP_509833.3; NM_077432.3.
DR   AlphaFoldDB; Q21389; -.
DR   STRING; 6239.K09C8.4; -.
DR   CAZy; GT49; Glycosyltransferase Family 49.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PaxDb; Q21389; -.
DR   EnsemblMetazoa; K09C8.4.1; K09C8.4.1; WBGene00010716.
DR   GeneID; 187206; -.
DR   KEGG; cel:CELE_K09C8.4; -.
DR   UCSC; K09C8.4; c. elegans.
DR   CTD; 187206; -.
DR   WormBase; K09C8.4; CE44089; WBGene00010716; lge-1.
DR   eggNOG; KOG3765; Eukaryota.
DR   GeneTree; ENSGT00940000170953; -.
DR   HOGENOM; CLU_019238_3_2_1; -.
DR   InParanoid; Q21389; -.
DR   OMA; WNIQLSD; -.
DR   OrthoDB; 729091at2759; -.
DR   PhylomeDB; Q21389; -.
DR   PRO; PR:Q21389; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00010716; Expressed in larva and 1 other tissue.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0042285; F:xylosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
DR   Gene3D; 3.90.550.10; -; 2.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   SUPFAM; SSF53448; SSF53448; 2.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..631
FT                   /note="Glycosyltransferase-like protein LARGE"
FT                   /id="PRO_0000226818"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..631
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        400
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        529
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        593
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   631 AA;  74525 MW;  F184CCC5C4959C90 CRC64;
     MQSNYSISYF LLILFTGTSS YFTIWNFVDH TRVGAFPEED YIRLAYIIGG NFMTRLMFMQ
     HFKSVLKYSD HFFRLHLITD ENHRSDIHEL MTSWNISNCE WFFHNLTEFE KRVAWIPNSH
     YSKYYGLSKL LIPEIIGNDI GKIMFMDVDI IFQTNIFDLW KQFRNFNNSQ VFGMVENLSD
     WYLNKDGKKS VWPALGRGFN TGIIMFDLDK LRKNGWASKW RVVANKYLRI HGKTAMSDQD
     IFNAYIHDYP TEIIQIPCAY NYQLGALTKS KELCPETPLA LHFNSQNKTV GKNYAFFDKI
     RKAFDEMDGS DLKRRRRSFK GNNQKDICHE YLPLDNFRII PNAIGRMTKP AELCMVTQFS
     KDRLNHFLES ANAWRHPIST AVYGKDKDLL DIAKAVTELN RTDITIHLVF EEPTESWMLD
     SLYPINFLRN VAIEHANCKY ILMTDVDFVV LGDYGTIIDQ TGNLKQKEVL VIPALEMTYP
     QLRLNLSNFL SRKDLVIEHL LNKTIQTFRE TIWPSSHVPT NISKWIKSNR TYMVNYEKNY
     EPYFVIKKEE CPFYDQRFGG FGWNKVTHVM QLKMMNYKFL VSPTSFMIHQ NHNASKSLKR
     WRRDPHYQKC LHTLKNKFMK KTASRLGIKL R