SQV8_CAEEL
ID SQV8_CAEEL Reviewed; 356 AA.
AC Q09363;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase sqv-8 {ECO:0000305|PubMed:11005858};
DE EC=2.4.1.135 {ECO:0000269|PubMed:11005858};
DE AltName: Full=Glucuronyl transferase I {ECO:0000303|PubMed:11005858};
DE Short=GlcAT-I {ECO:0000303|PubMed:11005858};
DE AltName: Full=Squashed vulva protein 8;
DE AltName: Full=Vulval invagination protein sqv-8;
GN Name=sqv-8; ORFNames=ZK1307.5;
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].
RC STRAIN=Bristol N2;
RX PubMed=9927678; DOI=10.1073/pnas.96.3.974;
RA Herman T., Horvitz H.R.;
RT "Three proteins involved in Caenorhabditis elegans vulval invagination are
RT similar to components of a glycosylation pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:974-979(1999).
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).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-200; GLY-205;
RP GLY-226 AND ASP-265.
RX PubMed=9927677; DOI=10.1073/pnas.96.3.968;
RA Herman T., Hartwieg E., Horvitz H.R.;
RT "sqv mutants of Caenorhabditis elegans are defective in vulval epithelial
RT invagination.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:968-973(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11005858; DOI=10.1073/pnas.97.20.10838;
RA Bulik D.A., Wei G., Toyoda H., Kinoshita-Toyoda A., Waldrip W.R.,
RA Esko J.D., Robbins P.W., Selleck S.B.;
RT "sqv-3, -7, and -8, a set of genes affecting morphogenesis in
RT Caenorhabditis elegans, encode enzymes required for glycosaminoglycan
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10838-10843(2000).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-200.
RX PubMed=16828468; DOI=10.1016/j.ydbio.2006.06.008;
RA Franks D.M., Izumikawa T., Kitagawa H., Sugahara K., Okkema P.G.;
RT "C. elegans pharyngeal morphogenesis requires both de novo synthesis of
RT pyrimidines and synthesis of heparan sulfate proteoglycans.";
RL Dev. Biol. 296:409-420(2006).
CC -!- FUNCTION: Glycosyltransferase required for the biosynthesis of the
CC tetrasaccharide (GlcA-Gal-Gal-Xyl-)Ser core linker of heparan sulfate
CC and chondroitin sulfate (PubMed:11005858). May be involved in the
CC biosynthesis of the HNK-1 carbohydrate epitope on glycoproteins
CC (PubMed:11005858). Required for embryonic development (PubMed:9927677).
CC Involved in the elongation of the pharyngeal isthmus during the later
CC stages of embryonic development (PubMed:16828468). Involved in vulval
CC epithelium invagination (PubMed:9927677). {ECO:0000269|PubMed:11005858,
CC ECO:0000269|PubMed:16828468, ECO:0000269|PubMed:9927677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-
CC xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571,
CC Rhea:RHEA-COMP:12573, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132090, ChEBI:CHEBI:132093;
CC EC=2.4.1.135; Evidence={ECO:0000269|PubMed:11005858};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11005858}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: F1 adults accumulate eggs in the uterus. Embryos
CC are predominantly arrested at the bean/comma embryonic stage.
CC {ECO:0000269|PubMed:9927677}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC {ECO:0000305}.
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DR EMBL; AJ005864; CAA06741.1; -; mRNA.
DR EMBL; Z47358; CAA87436.1; -; Genomic_DNA.
DR PIR; T27733; T27733.
DR RefSeq; NP_496076.1; NM_063675.4.
DR AlphaFoldDB; Q09363; -.
DR SMR; Q09363; -.
DR STRING; 6239.ZK1307.5; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR iPTMnet; Q09363; -.
DR EPD; Q09363; -.
DR PaxDb; Q09363; -.
DR PeptideAtlas; Q09363; -.
DR PRIDE; Q09363; -.
DR EnsemblMetazoa; ZK1307.5.1; ZK1307.5.1; WBGene00005026.
DR EnsemblMetazoa; ZK1307.5.2; ZK1307.5.2; WBGene00005026.
DR GeneID; 174517; -.
DR KEGG; cel:CELE_ZK1307.5; -.
DR UCSC; ZK1307.5; c. elegans.
DR CTD; 174517; -.
DR WormBase; ZK1307.5; CE01694; WBGene00005026; sqv-8.
DR eggNOG; KOG1476; Eukaryota.
DR HOGENOM; CLU_045177_3_0_1; -.
DR InParanoid; Q09363; -.
DR OMA; LMYALLQ; -.
DR OrthoDB; 901158at2759; -.
DR PhylomeDB; Q09363; -.
DR Reactome; R-CEL-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR PRO; PR:Q09363; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00005026; Expressed in germ line (C elegans) and 4 other tissues.
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:0016020; C:membrane; IDA:WormBase.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; IBA:GO_Central.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IMP:WormBase.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0060465; P:pharynx development; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0007286; P:spermatid development; IMP:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR CDD; cd00218; GlcAT-I; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005027; Glyco_trans_43.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..356
FT /note="Galactosylgalactosylxylosylprotein 3-beta-
FT glucuronosyltransferase sqv-8"
FT /id="PRO_0000195178"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..356
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 200
FT /note="G->D: In n2825; embryos are arrested at the
FT bean/comma or 2/3-fold embryonic stages. Pharyngeal isthmus
FT is shorter and thicker."
FT /evidence="ECO:0000269|PubMed:16828468,
FT ECO:0000269|PubMed:9927677"
FT MUTAGEN 205
FT /note="G->E: In n2847; embryos are predominantly arrested
FT at the bean/comma embryonic stage."
FT /evidence="ECO:0000269|PubMed:9927677,
FT ECO:0000269|PubMed:9927678"
FT MUTAGEN 226
FT /note="G->E: In n2843; embryos are predominantly arrested
FT at the bean/comma embryonic stage."
FT /evidence="ECO:0000269|PubMed:9927677,
FT ECO:0000269|PubMed:9927678"
FT MUTAGEN 265
FT /note="D->N: In n2851; embryos are predominantly arrested
FT at the bean/comma embryonic stage."
FT /evidence="ECO:0000269|PubMed:9927677,
FT ECO:0000269|PubMed:9927678"
SQ SEQUENCE 356 AA; 41089 MW; B1342554590251A9 CRC64;
MFPSRLLEKW WLRAFIALVI FFVWQLFYAI NRVQSLEEER ATLQATIEVL TRKSDGLRTQ
IFEKERNLVR LNGKVEEIDT QIRDHLSLLP RVNRSTPFIY FITPTHFRAA QRADLTRLSY
TLSHVPNLHW IVVEDSDELT PSIAGILKRS KIPNTHLNAR TPSDQKMRYD DPNWTLPRGV
EQRNRALLWI QNQLSGVKEG VVYFGDDDNT YDLKIFGEMR KVKNAGVWPV GIVGGMFVET
PILEKNGSIS HFNAVWKPER PFPIDMAAFA VNISLVLSNA NALFSFDVPR GYQESTFLEN
LGIHRYNMEP LAEMCTKVYV WHTRTEKPKL SKESIDRLTK KTGFNSLEAH ALGVDN
