CHST_CAEEL
ID CHST_CAEEL Reviewed; 329 AA.
AC Q09272;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Carbohydrate sulfotransferase chst-1 {ECO:0000305};
DE EC=2.8.2.5 {ECO:0000269|PubMed:27645998, ECO:0000269|PubMed:27703236};
DE AltName: Full=Chondroitin 4-O-sulfotransferase {ECO:0000305};
DE AltName: Full=Chondroitin 4-sulfotransferase {ECO:0000305};
DE Short=C4S {ECO:0000305};
DE Short=C4ST {ECO:0000305};
GN Name=chst-1 {ECO:0000303|PubMed:27645998, ECO:0000312|WormBase:C41C4.1};
GN ORFNames=C41C4.1 {ECO:0000312|WormBase:C41C4.1};
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27645998; DOI=10.1074/jbc.m116.757328;
RA Izumikawa T., Dejima K., Watamoto Y., Nomura K.H., Kanaki N., Rikitake M.,
RA Tou M., Murata D., Yanagita E., Kano A., Mitani S., Nomura K., Kitagawa H.;
RT "Chondroitin 4-O-sulfotransferase ss indispensable for sulfation of
RT chondroitin and plays an important role in maintaining normal life span and
RT oxidative stress responses in nematodes.";
RL J. Biol. Chem. 291:23294-23304(2016).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27703236; DOI=10.1038/srep34662;
RA Dierker T., Shao C., Haitina T., Zaia J., Hinas A., Kjellen L.;
RT "Nematodes join the family of chondroitin sulfate-synthesizing organisms:
RT Identification of an active chondroitin sulfotransferase in Caenorhabditis
RT elegans.";
RL Sci. Rep. 6:34662-34662(2016).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of non-
CC reducing N-acetylgalactosamine (GalNAc) residue of chondroitin.
CC {ECO:0000269|PubMed:27645998, ECO:0000269|PubMed:27703236}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate
CC = n adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate + n H(+);
CC Xref=Rhea:RHEA:16101, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9829,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:58422; EC=2.8.2.5;
CC Evidence={ECO:0000269|PubMed:27645998, ECO:0000269|PubMed:27703236};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the head and tail of
CC hermaphrodites, in particular in amphid and phasmid sheath cells.
CC {ECO:0000269|PubMed:27645998}.
CC -!- DISRUPTION PHENOTYPE: The tm576 deletion mutant is lethal
CC (PubMed:27645998). The ok625 deletion mutant has reduced levels of 4-O-
CC sulfated disaccharides, but increased levels of 6-O-sulfated
CC disaccharides (PubMed:27645998, PubMed:27703236). Increased mortality
CC in response to oxidative stress (PubMed:27645998).
CC {ECO:0000269|PubMed:27645998, ECO:0000269|PubMed:27703236}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
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DR EMBL; Z48045; CAA88098.1; -; Genomic_DNA.
DR PIR; T19872; T19872.
DR RefSeq; NP_495699.1; NM_063298.3.
DR AlphaFoldDB; Q09272; -.
DR STRING; 6239.C41C4.1; -.
DR PaxDb; Q09272; -.
DR EnsemblMetazoa; C41C4.1.1; C41C4.1.1; WBGene00008050.
DR GeneID; 174304; -.
DR KEGG; cel:CELE_C41C4.1; -.
DR UCSC; C41C4.1; c. elegans.
DR CTD; 174304; -.
DR WormBase; C41C4.1; CE01516; WBGene00008050; chst-1.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00970000195842; -.
DR HOGENOM; CLU_069458_0_0_1; -.
DR InParanoid; Q09272; -.
DR OMA; CENEKNC; -.
DR OrthoDB; 1330889at2759; -.
DR PhylomeDB; Q09272; -.
DR BRENDA; 2.8.2.5; 1045.
DR PRO; PR:Q09272; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008050; Expressed in germ line (C elegans) and 3 other tissues.
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:0047756; F:chondroitin 4-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:UniProtKB.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB.
DR InterPro; IPR007669; Chst-1.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR22900; PTHR22900; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Golgi apparatus; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..329
FT /note="Carbohydrate sulfotransferase chst-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000065232"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 24..329
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT BINDING 91..97
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305"
FT BINDING 157..165
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 39010 MW; E8B5CA70B3C208ED CRC64;
MLKWFIISCC LLTAISYSTY YLFTSNSWIK TVKTHTYSRF YQLIKENTKT QLDRLQEEAK
LSGKSLIPPF INFDREYAIA PKYNISICRI KKSMSTLMSG VACVLYDTGK FMRNNRSILE
VWSHRFCGEK NEYRRMNEVK WRMGDAHHTF KKIVVIRDPI ARFISFFSNK CIFEAQKYPD
RKQCYNCQGN VTCFLEKQYE RFVQHSSDYS RIRPSYEDKH AAPLSWNCEF GKFLKDYKII
KLAVDPKDRK NGLANLMNVL KESNVPNSTL RFIEKSALEG ETMHATYDSD AHDVVKKEIE
NDKKIREWLK RIYYLDFVIF DFDTTFINS
