GALT1_CAEEL
ID GALT1_CAEEL Reviewed; 425 AA.
AC O16374; G4RVA7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 4.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Beta-1,4-galactosyltransferase galt-1 {ECO:0000303|PubMed:19858195};
DE EC=2.4.1.- {ECO:0000269|PubMed:19858195};
GN Name=galt-1 {ECO:0000312|WormBase:M03F8.4};
GN ORFNames=M03F8.4 {ECO:0000312|WormBase:M03F8.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND GLYCOSYLATION.
RX PubMed=19858195; DOI=10.1074/jbc.m109.058354;
RA Titz A., Butschi A., Henrissat B., Fan Y.Y., Hennet T., Razzazi-Fazeli E.,
RA Hengartner M.O., Wilson I.B., Kuenzler M., Aebi M.;
RT "Molecular basis for galactosylation of core fucose residues in
RT invertebrates: identification of caenorhabditis elegans N-glycan core
RT alpha1,6-fucoside beta1,4-galactosyltransferase GALT-1 as a member of a
RT novel glycosyltransferase family.";
RL J. Biol. Chem. 284:36223-36233(2009).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=20062796; DOI=10.1371/journal.ppat.1000717;
RA Butschi A., Titz A., Waelti M.A., Olieric V., Paschinger K., Noebauer K.,
RA Guo X., Seeberger P.H., Wilson I.B., Aebi M., Hengartner M.O., Kuenzler M.;
RT "Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity
RT towards nematotoxic fungal galectin CGL2.";
RL PLoS Pathog. 6:E1000717-E1000717(2010).
CC -!- FUNCTION: Catalyzes the transfer of beta-galactose from UDP-galactose
CC to position 4 of alpha-1,6-linked fucose at the reducing end GlcNAc in
CC N-glycan cores (PubMed:19858195). Involved in susceptibility to the
CC nematotoxic C.cinerea galectin Cgl2, likely by contributing to the
CC synthesis of core alpha-1,6-fucosylated N-glycans to which Cgl2 binds
CC (PubMed:20062796). {ECO:0000269|PubMed:19858195,
CC ECO:0000269|PubMed:20062796}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19858195};
CC Note=Can also use Fe(2+) and Co(2+). {ECO:0000269|PubMed:19858195};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, Cu(2+) and Zn(2+).
CC {ECO:0000269|PubMed:19858195}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=84 uM for UDP-galactose {ECO:0000269|PubMed:19858195};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000303|PubMed:19858195}; Single-pass type II membrane protein
CC {ECO:0000303|PubMed:19858195}. Note=Localizes to vesicles or organelles
CC in coelomocytes. {ECO:0000269|PubMed:19858195}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine and coelomocytes.
CC {ECO:0000269|PubMed:19858195}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19858195}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 92 family.
CC {ECO:0000305}.
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DR EMBL; BX284605; CCD64148.1; -; Genomic_DNA.
DR RefSeq; NP_504545.2; NM_072144.5.
DR AlphaFoldDB; O16374; -.
DR STRING; 6239.M03F8.4; -.
DR PaxDb; O16374; -.
DR EnsemblMetazoa; M03F8.4.1; M03F8.4.1; WBGene00019763.
DR GeneID; 187430; -.
DR KEGG; cel:CELE_M03F8.4; -.
DR UCSC; M03F8.4; c. elegans.
DR CTD; 187430; -.
DR WormBase; M03F8.4; CE40769; WBGene00019763; galt-1.
DR eggNOG; ENOG502S8SJ; Eukaryota.
DR HOGENOM; CLU_053206_0_0_1; -.
DR InParanoid; O16374; -.
DR OMA; RYRIQDE; -.
DR OrthoDB; 959479at2759; -.
DR PhylomeDB; O16374; -.
DR PRO; PR:O16374; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00019763; Expressed in embryo and 2 other tissues.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; IDA:WormBase.
DR GO; GO:0006491; P:N-glycan processing; IDA:WormBase.
DR GO; GO:0042125; P:protein galactosylation; IDA:UniProtKB.
DR InterPro; IPR008166; Glyco_transf_92.
DR Pfam; PF01697; Glyco_transf_92; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..425
FT /note="Beta-1,4-galactosyltransferase galt-1"
FT /id="PRO_0000438180"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..425
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 189..394
FT /note="GT92"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 425 AA; 49524 MW; 042E77F2ACBD87AE CRC64;
MPRITASKIV LLIALSFCIT VIYHFPIATR SSKEYDEYGN EYENVASIES DIKNVRRLLD
EVPDPSQNRL QFLKLDEHAF AFSAYTDDRN GNMGYKYVRV LMFITSQDNF SCEINGRKST
DVSLYEFSEN HKMKWQMFIL NCKLPDGIDF NNVSSVKVIR STTKQFVDVP IRYRIQDEKI
ITPDEYDYKM SICVPALFGN GYDAKRIVEF IELNTLQGIE KIYIYTNQKE LDGSMKKTLK
YYSDNHKITL IDYTLPFRED GVWYHGQLAT VTDCLLRNTG ITKYTFFNDF DEFFVPVIKS
RTLFETISGL FEDPTIGSQR TALKYINAKI KSAPYSLKNI VSEKRIETRF TKCVVRPEMV
FEQGIHHTSR VIQDNYKTVS HGGSLLRVYH YKDKKYCCED ESLLKKRHGD QLREKFDSVV
GLLDL
