CHSSA_CAEEL
ID CHSSA_CAEEL Reviewed; 736 AA.
AC Q7Z1Z1; G5EGA1; O02330; Q7YTF6;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Chondroitin sulfate synthase sqv-5 {ECO:0000305|PubMed:12761549};
DE EC=2.4.1.174 {ECO:0000269|PubMed:12761549, ECO:0000269|PubMed:12761550};
DE EC=2.4.1.175 {ECO:0000269|PubMed:12761549, ECO:0000269|PubMed:12761550};
DE EC=2.4.1.226 {ECO:0000269|PubMed:12761549};
DE AltName: Full=Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N- acetylgalactosaminyltransferase 1 {ECO:0000303|PubMed:12761549, ECO:0000303|PubMed:12761550};
DE AltName: Full=Glucuronylgalactosylproteoglycan 4-beta-N- acetylgalactosaminyltransferase {ECO:0000303|PubMed:12761549, ECO:0000303|PubMed:12761550};
DE AltName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 1 {ECO:0000303|PubMed:12761549};
DE AltName: Full=Squashed vulva protein 5 {ECO:0000303|PubMed:12761549};
GN Name=sqv-5 {ECO:0000312|WormBase:T24D1.1b};
GN ORFNames=T24D1.1 {ECO:0000312|WormBase:T24D1.1b};
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|EMBL:BAC76780.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12761550; DOI=10.1038/nature01635;
RA Mizuguchi S., Uyama T., Kitagawa H., Nomura K.H., Dejima K.,
RA Gengyo-Ando K., Mitani S., Sugahara K., Nomura K.;
RT "Chondroitin proteoglycans are involved in cell division of Caenorhabditis
RT elegans.";
RL Nature 423:443-448(2003).
RN [2] {ECO:0000312|EMBL:AAO85274.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORMS B AND C), TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12761549; DOI=10.1038/nature01634;
RA Hwang H.Y., Olson S.K., Esko J.D., Robert Horvitz H.;
RT "Caenorhabditis elegans early embryogenesis and vulval morphogenesis
RT require chondroitin biosynthesis.";
RL Nature 423:439-443(2003).
RN [3] {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 [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15485872; DOI=10.1074/jbc.m409615200;
RA Izumikawa T., Kitagawa H., Mizuguchi S., Nomura K.H., Nomura K., Tamura J.,
RA Gengyo-Ando K., Mitani S., Sugahara K.;
RT "Nematode chondroitin polymerizing factor showing cell-/organ-specific
RT expression is indispensable for chondroitin synthesis and embryonic cell
RT division.";
RL J. Biol. Chem. 279:53755-53761(2004).
RN [5] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF LEU-564 AND GLY-665.
RX PubMed=16982046; DOI=10.1016/j.ydbio.2006.08.037;
RA Suzuki N., Toyoda H., Sano M., Nishiwaki K.;
RT "Chondroitin acts in the guidance of gonadal distal tip cells in C.
RT elegans.";
RL Dev. Biol. 300:635-646(2006).
RN [6]
RP INTERACTION WITH MIG-22.
RX PubMed=17237233; DOI=10.1074/jbc.m611107200;
RA Kitagawa H., Izumikawa T., Mizuguchi S., Dejima K., Nomura K.H., Egusa N.,
RA Taniguchi F., Tamura J., Gengyo-Ando K., Mitani S., Nomura K., Sugahara K.;
RT "Expression of rib-1, a Caenorhabditis elegans homolog of the human tumor
RT suppressor EXT genes, is indispensable for heparan sulfate synthesis and
RT embryonic morphogenesis.";
RL J. Biol. Chem. 282:8533-8544(2007).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF LEU-564.
RX PubMed=24052309; DOI=10.1126/science.1242528;
RA Pedersen M.E., Snieckute G., Kagias K., Nehammer C., Multhaupt H.A.,
RA Couchman J.R., Pocock R.;
RT "An epidermal microRNA regulates neuronal migration through control of the
RT cellular glycosylation state.";
RL Science 341:1404-1408(2013).
CC -!- FUNCTION: Has both beta-1,3-glucuronic acid and beta-1,4-N-
CC acetylgalactosamine transferase activity (PubMed:12761549). The beta-
CC 1,3-glucuronic acid transferase activity is controversial as it is not
CC detected using the purified recombinant enzyme (PubMed:12761550). Adds
CC the first N-acetylgalactosamine(GalNAc) to initiate the chondroitin
CC chain. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and GalNAc from
CC UDP-GalNAc to the non-reducing end of the elongating chondroitin
CC polymer (PubMed:12761549, PubMed:12761550). Together with mig-22,
CC required for chondroitin synthesis (PubMed:15485872). Plays a role in
CC early embryonic development by controlling cell division and
CC cytokinesis (PubMed:12761550). In addition, involved in vulva
CC morphogenesis and in the directed migration of gonadal distal tip cells
CC and hermaphrodite specific neurons (PubMed:12761549, PubMed:16982046,
CC PubMed:24052309). May be required for nunc6/netrin-mediated dorsal
CC guidance of distal tip cells (PubMed:16982046).
CC {ECO:0000269|PubMed:12761549, ECO:0000269|PubMed:12761550,
CC ECO:0000269|PubMed:15485872, ECO:0000269|PubMed:16982046,
CC ECO:0000269|PubMed:24052309}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine =
CC 3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-
CC D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23464, Rhea:RHEA-COMP:12573, Rhea:RHEA-COMP:12575,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:132093, ChEBI:CHEBI:132105; EC=2.4.1.174;
CC Evidence={ECO:0000269|PubMed:12761549, ECO:0000269|PubMed:12761550};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-(beta-D-GalNAc-
CC (1->4)-beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-
CC beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:20800, Rhea:RHEA-COMP:14058, Rhea:RHEA-
CC COMP:14059, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138442, ChEBI:CHEBI:138443; EC=2.4.1.175;
CC Evidence={ECO:0000269|PubMed:12761549, ECO:0000269|PubMed:12761550};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-
CC D-galactosamine = 3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-
CC (1->3)](n+1)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:55000, Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14301,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:138444, ChEBI:CHEBI:138445; EC=2.4.1.175;
CC Evidence={ECO:0000269|PubMed:12761549, ECO:0000269|PubMed:12761550};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-
CC glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-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:23428, Rhea:RHEA-COMP:12575,
CC Rhea:RHEA-COMP:14058, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132105, ChEBI:CHEBI:138442;
CC EC=2.4.1.226; Evidence={ECO:0000269|PubMed:12761549};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-
CC D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54996,
CC Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14061, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:138444,
CC ChEBI:CHEBI:138445; EC=2.4.1.226;
CC Evidence={ECO:0000269|PubMed:12761549};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q86X52};
CC -!- SUBUNIT: Interacts with mig-22. {ECO:0000269|PubMed:17237233}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305|PubMed:12761549}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:12761549}. Note=Localizes in punctate foci in the
CC cytoplasm. Co-localizes with sqv-1. {ECO:0000269|PubMed:12761549}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|EMBL:AAO85274.1};
CC IsoId=Q7Z1Z1-1; Sequence=Displayed;
CC Name=a {ECO:0000312|EMBL:BAC76780.1};
CC IsoId=Q7Z1Z1-2; Sequence=VSP_057739;
CC Name=b {ECO:0000312|WormBase:T24D1.1b};
CC IsoId=Q7Z1Z1-3; Sequence=VSP_057740;
CC -!- TISSUE SPECIFICITY: Expressed in vulva, uterus and oocytes.
CC {ECO:0000269|PubMed:12761549}.
CC -!- DISRUPTION PHENOTYPE: Mutant hermaphrodites have a defect in the
CC invagination of the vulva epithelium and produce fewer eggs
CC (PubMed:12761549). A similar defect is observed in RNAi-mediated
CC knockdown (PubMed:12761550). In addition, RNAi-mediated knockdown in
CC embryos shows severe cell division defects including cytokinesis
CC reversal and increased number of nuclei per cell resulting in early
CC embryonic death in utero (PubMed:12761550). RNAi-mediated knockdown in
CC adults shows a normal sperm production (PubMed:12761550).
CC {ECO:0000269|PubMed:12761549, ECO:0000269|PubMed:12761550}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB03422.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB088397; BAC76780.1; -; mRNA.
DR EMBL; AY241925; AAO85273.1; -; Genomic_DNA.
DR EMBL; AY241925; AAO85274.1; -; Genomic_DNA.
DR EMBL; BX284601; CAB03422.2; ALT_SEQ; Genomic_DNA.
DR EMBL; BX284601; CAE17977.2; -; Genomic_DNA.
DR PIR; T25233; T25233.
DR RefSeq; NP_001021639.3; NM_001026468.5. [Q7Z1Z1-2]
DR RefSeq; NP_001021640.2; NM_001026469.5. [Q7Z1Z1-3]
DR RefSeq; NP_001300439.1; NM_001313510.1. [Q7Z1Z1-1]
DR AlphaFoldDB; Q7Z1Z1; -.
DR SMR; Q7Z1Z1; -.
DR STRING; 6239.T24D1.1b; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR EPD; Q7Z1Z1; -.
DR PaxDb; Q7Z1Z1; -.
DR PRIDE; Q7Z1Z1; -.
DR EnsemblMetazoa; T24D1.1a.1; T24D1.1a.1; WBGene00005023. [Q7Z1Z1-2]
DR EnsemblMetazoa; T24D1.1b.1; T24D1.1b.1; WBGene00005023. [Q7Z1Z1-3]
DR GeneID; 172851; -.
DR KEGG; cel:CELE_T24D1.1; -.
DR UCSC; T24D1.1a; c. elegans.
DR CTD; 172851; -.
DR WormBase; T24D1.1a; CE50401; WBGene00005023; sqv-5. [Q7Z1Z1-2]
DR WormBase; T24D1.1b; CE39182; WBGene00005023; sqv-5. [Q7Z1Z1-3]
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_016244_2_0_1; -.
DR OMA; QGPQLPE; -.
DR PRO; PR:Q7Z1Z1; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00005023; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q7Z1Z1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
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:0008376; F:acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0047237; F:glucuronylgalactosylproteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IBA:GO_Central.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:UniProtKB.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008428; Chond_GalNAc.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF05679; CHGN; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Glycoprotein; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..736
FT /note="Chondroitin sulfate synthase sqv-5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433353"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..736
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 277..340
FT /evidence="ECO:0000255"
FT BINDING 583
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 698
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057739"
FT VAR_SEQ 4..5
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057740"
FT MUTAGEN 564
FT /note="L->F: In k175; reduced chondroitin levels. Impaired
FT directed migration of gonadal distal tip cells and
FT hermaphrodite specific neurons; mild defect in vulva
FT morphogenesis. Normal fertility."
FT /evidence="ECO:0000269|PubMed:16982046,
FT ECO:0000269|PubMed:24052309"
FT MUTAGEN 665
FT /note="G->E: In k172; reduced chondroitin levels. Impaired
FT directed migration of gonadal distal tip cells and mild
FT defect in vulva morphogenesis. Normal fertility."
FT /evidence="ECO:0000269|PubMed:16982046"
SQ SEQUENCE 736 AA; 83557 MW; 26E94E5FEA19D78A CRC64;
MRVFQRSTCR MPVSRATVTI LLGILFGFSI TYYLTALKSL TNPIICGPEQ QIGGFDYLDV
ISQRADADVF TRSQSLPGHR RGLILVAIMT AAKYVDTRAY NVWKTWAQHI PGRVLIFVAE
GTESVHEDMP LIRLKGVDDT YPPQKKSFAM VKWLAENMAD EYDWFLRADD DLYIRGEELA
LFLRSVDSSK AHIIGQAGLG NSAEYGLLAL GSTDNYCMGG PGIVMSRDTL LKVSPHLESC
LQHMLTSHED VELGRCIRKH VGVACTWNYE MQKLFHNNQS AIKESYAKNM KELKDAITLH
PIKDPAVMRK VHLRNREIKL REARAKRSLL SSELSTAKAQ TLVRMTPNRT NDLTPWEYIN
NNKILFCADR VNCPRHTVDL SIRTEMADTI TQLFDEFNTN ARQRGRVLQF QSLQYGYMRV
EPTKGVDYVL DMLLWFKKFR PPNRTTISVR RHAYVQQTFG KLRSLSEGVF RSNMRANSTL
IEDPTLHMIM PLRGRAAIFA RFAQHLKSIC ARGGDDLAVS LTIVLYSSED EMENRETIEM
LRASFIPVTV IEMGDVSFSR GVALMRGAET LPANALLFFT DVDMLFTCDA LKRIKSNTIL
NAQIYFPIVF SEFSHESWSE NDKLLADAFH YGRGRGYFRH FGYGLAAMYK ADLMDVGGFD
TKIEGWGKED VDLFEKAIKN GRLRVIRVPE PGLVHIYHPI HCDENMPTAQ KDMCHGSKAA
SLASIDTLVE QIAQYT
