SQV2_CAEEL
ID SQV2_CAEEL Reviewed; 330 AA.
AC Q9N491;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Beta-1,3-galactosyltransferase sqv-2;
DE EC=2.4.1.134;
DE AltName: Full=Squashed vulva protein 2;
GN Name=sqv-2; ORFNames=Y110A2AL.14;
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 [MRNA], FUNCTION, ENZYME ACTIVITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12584198; DOI=10.1074/jbc.c200518200;
RA Hwang H.-Y., Olson S.K., Brown J.R., Esko J.D., Horvitz H.R.;
RT "The Caenorhabditis elegans genes sqv-2 and sqv-6, which are required for
RT vulval morphogenesis, encode glycosaminoglycan galactosyltransferase II and
RT xylosyltransferase.";
RL J. Biol. Chem. 278:11735-11738(2003).
RN [2]
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: Beta-1,3-galactosyltransferase that transfers galactose from
CC UDP-galactose to substrates with a terminal beta-linked galactose
CC residue. Required for vulval morphogenesis and zygotic cytokinesis,
CC suggesting that glycosaminoglycans play a central role in vulval
CC morphogenesis. {ECO:0000269|PubMed:12584198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-
CC [protein] + UDP-alpha-D-galactose = 3-O-(beta-D-galactosyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:11780, Rhea:RHEA-COMP:12570, Rhea:RHEA-
CC COMP:12571, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:132088, ChEBI:CHEBI:132090; EC=2.4.1.134;
CC Evidence={ECO:0000269|PubMed:12584198};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Worms are infertile because of the failure of the
CC progeny of homozygous mutants to initiate cytokinesis and because of
CC the failure to form an extracellular space between the egg and the
CC eggshell. {ECO:0000269|PubMed:12584198}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AY241927; AAO85276.1; -; mRNA.
DR EMBL; FO081635; CCD72980.1; -; Genomic_DNA.
DR RefSeq; NP_494394.1; NM_061993.5.
DR AlphaFoldDB; Q9N491; -.
DR SMR; Q9N491; -.
DR STRING; 6239.Y110A2AL.14; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR EPD; Q9N491; -.
DR PaxDb; Q9N491; -.
DR PeptideAtlas; Q9N491; -.
DR EnsemblMetazoa; Y110A2AL.14.1; Y110A2AL.14.1; WBGene00005020.
DR GeneID; 173635; -.
DR KEGG; cel:CELE_Y110A2AL.14; -.
DR UCSC; Y110A2AL.14.1; c. elegans.
DR CTD; 173635; -.
DR WormBase; Y110A2AL.14; CE25190; WBGene00005020; sqv-2.
DR eggNOG; KOG2288; Eukaryota.
DR GeneTree; ENSGT00940000162229; -.
DR HOGENOM; CLU_046589_0_0_1; -.
DR InParanoid; Q9N491; -.
DR OMA; HVYRWHD; -.
DR OrthoDB; 640360at2759; -.
DR PhylomeDB; Q9N491; -.
DR BRENDA; 2.4.1.134; 1045.
DR Reactome; R-CEL-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR PRO; PR:Q9N491; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00005020; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IDA:WormBase.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047220; F:galactosylxylosylprotein 3-beta-galactosyltransferase activity; IDA:WormBase.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:WormBase.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..330
FT /note="Beta-1,3-galactosyltransferase sqv-2"
FT /id="PRO_0000219191"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..330
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 37973 MW; 33E66575156A3758 CRC64;
MRFYRTYLLV AGAFCSLCTL AVIFNCGWDD SPPATPSAIN GGGSNAPLIS SPTNLPETFL
YISILTSPNE TERRQNVRDT WFRLSTKGPS VFIAKFAVGT MGLAAEDRRL LAEENEKFGD
LALLDRHEES YERLAKKTLA CFVHAFANFK FKFFLKTDID SFVRITPLII NLKQIQDPML
YWGFLDGRAK PFRKGKWKEP EWNLCDRYLP YQLGGGYVLS YELIRFLAIN AQLFRHYRNE
DVSVGAWIGG LDVKYVHDPR FDTEWRSRGC NNEYLITHKH TEQEMQEMFE NLKKTGKLCA
KEFQKHPSYV YDFSKAPSEC CTRVNGSNIP
