ID CHST1_RAT Reviewed; 411 AA.
AC Q5RJQ0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 120.
DE RecName: Full=Carbohydrate sulfotransferase 1;
DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 1;
DE Short=GST-1;
DE AltName: Full=Keratan sulfate Gal-6 sulfotransferase;
DE Short=KS6ST;
DE Short=KSGal6ST;
DE Short=KSST;
DE EC=2.8.2.21 {ECO:0000250|UniProtKB:O43916, ECO:0000250|UniProtKB:Q9EQC0};
GN Name=Chst1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the transfer of sulfate to
CC position 6 of internal galactose (Gal) residues of keratan. Cooperates
CC with B4GALT4 and B3GNT7 glycosyltransferases and CHST6 sulfotransferase
CC to construct and elongate disulfated disaccharide unit [->3(6-
CC sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate
CC polymer. Has a preference for sulfating keratan sulfate, but it also
CC transfers sulfate to the unsulfated polymer (By similarity). Involved
CC in biosynthesis of phosphacan, a major keratan sulfate proteoglycan in
CC the developing brain (By similarity). Involved in biosynthesis of 6-
CC sulfoGalbeta-containing O-linked glycans in high endothelial venules of
CC lymph nodes. May act in a synergistic manner with CHST4 to generate
CC sialyl 6',6-disulfo Lewis X motif, a recognition determinant for immune
CC cell receptors implicated in leukocyte trafficking (By similarity).
CC Catalyzes sulfation of N-acetyllactosamine (LacNAc) oligosaccharides
CC with highest efficiency for sialylated LacNAc structures (By
CC similarity). {ECO:0000250|UniProtKB:O43916,
CC ECO:0000250|UniProtKB:Q9EQC0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + keratan = adenosine 3',5'-
CC bisphosphate + keratan 6'-sulfate.; EC=2.8.2.21;
CC Evidence={ECO:0000250|UniProtKB:O43916,
CC ECO:0000250|UniProtKB:Q9EQC0};
CC -!- PATHWAY: Glycan metabolism. {ECO:0000250|UniProtKB:O43916}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
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DR EMBL; BC086551; AAH86551.1; -; mRNA.
DR RefSeq; NP_001011955.1; NM_001011955.1.
DR RefSeq; XP_017447047.1; XM_017591558.1.
DR RefSeq; XP_017447048.1; XM_017591559.1.
DR RefSeq; XP_017447049.1; XM_017591560.1.
DR RefSeq; XP_017447050.1; XM_017591561.1.
DR RefSeq; XP_017447051.1; XM_017591562.1.
DR RefSeq; XP_017447052.1; XM_017591563.1.
DR RefSeq; XP_017447053.1; XM_017591564.1.
DR AlphaFoldDB; Q5RJQ0; -.
DR STRING; 10116.ENSRNOP00000010510; -.
DR GlyCosmos; Q5RJQ0; 4 sites, No reported glycans.
DR GlyGen; Q5RJQ0; 4 sites.
DR PhosphoSitePlus; Q5RJQ0; -.
DR PaxDb; 10116-ENSRNOP00000010510; -.
DR Ensembl; ENSRNOT00000010510.6; ENSRNOP00000010510.2; ENSRNOG00000007989.6.
DR Ensembl; ENSRNOT00000095049.1; ENSRNOP00000090213.1; ENSRNOG00000007989.6.
DR Ensembl; ENSRNOT00000095051.1; ENSRNOP00000081989.1; ENSRNOG00000007989.6.
DR Ensembl; ENSRNOT00000098205.1; ENSRNOP00000087464.1; ENSRNOG00000007989.6.
DR Ensembl; ENSRNOT00000113200.1; ENSRNOP00000079857.1; ENSRNOG00000007989.6.
DR Ensembl; ENSRNOT00000114058.1; ENSRNOP00000086161.1; ENSRNOG00000007989.6.
DR Ensembl; ENSRNOT00055028467; ENSRNOP00055022907; ENSRNOG00055016771.
DR Ensembl; ENSRNOT00055028471; ENSRNOP00055022911; ENSRNOG00055016771.
DR Ensembl; ENSRNOT00055028474; ENSRNOP00055022914; ENSRNOG00055016771.
DR Ensembl; ENSRNOT00055028481; ENSRNOP00055022921; ENSRNOG00055016771.
DR Ensembl; ENSRNOT00055028482; ENSRNOP00055022922; ENSRNOG00055016771.
DR Ensembl; ENSRNOT00055028487; ENSRNOP00055022927; ENSRNOG00055016771.
DR Ensembl; ENSRNOT00060004762; ENSRNOP00060003423; ENSRNOG00060002936.
DR Ensembl; ENSRNOT00060004766; ENSRNOP00060003427; ENSRNOG00060002936.
DR Ensembl; ENSRNOT00060004768; ENSRNOP00060003429; ENSRNOG00060002936.
DR Ensembl; ENSRNOT00060004770; ENSRNOP00060003430; ENSRNOG00060002936.
DR Ensembl; ENSRNOT00060004772; ENSRNOP00060003433; ENSRNOG00060002936.
DR Ensembl; ENSRNOT00060004773; ENSRNOP00060003434; ENSRNOG00060002936.
DR Ensembl; ENSRNOT00065042541; ENSRNOP00065034805; ENSRNOG00065024784.
DR Ensembl; ENSRNOT00065042546; ENSRNOP00065034811; ENSRNOG00065024784.
DR Ensembl; ENSRNOT00065042556; ENSRNOP00065034821; ENSRNOG00065024784.
DR Ensembl; ENSRNOT00065042568; ENSRNOP00065034831; ENSRNOG00065024784.
DR Ensembl; ENSRNOT00065042574; ENSRNOP00065034836; ENSRNOG00065024784.
DR Ensembl; ENSRNOT00065042577; ENSRNOP00065034840; ENSRNOG00065024784.
DR GeneID; 295934; -.
DR KEGG; rno:295934; -.
DR UCSC; RGD:1308142; rat.
DR AGR; RGD:1308142; -.
DR CTD; 8534; -.
DR RGD; 1308142; Chst1.
DR eggNOG; ENOG502S17I; Eukaryota.
DR GeneTree; ENSGT00940000161262; -.
DR HOGENOM; CLU_028381_3_2_1; -.
DR InParanoid; Q5RJQ0; -.
DR OMA; NQHQEIF; -.
DR OrthoDB; 3031241at2759; -.
DR PhylomeDB; Q5RJQ0; -.
DR TreeFam; TF342871; -.
DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR PRO; PR:Q5RJQ0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000007989; Expressed in frontal cortex and 18 other cell types or tissues.
DR Genevisible; Q5RJQ0; RN.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0045130; F:keratan sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0008146; F:sulfotransferase activity; ISO:RGD.
DR GO; GO:0006012; P:galactose metabolic process; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0018146; P:keratan sulfate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042339; P:keratan sulfate metabolic process; ISO:RGD.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:RGD.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10704; CARBOHYDRATE SULFOTRANSFERASE; 1.
DR PANTHER; PTHR10704:SF36; CARBOHYDRATE SULFOTRANSFERASE 1; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Golgi apparatus;
KW Inflammatory response; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..411
FT /note="Carbohydrate sulfotransferase 1"
FT /id="PRO_0000085184"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..411
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 337..339
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 69..75
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 234..242
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 411 AA; 46885 MW; 715998736106E5CD CRC64;
MQCSWKAVLL LALASIAIQY TAIRTFTAKS FHTCPGLTET GLAERLCEEG PTFSYNLSRK
THVLILATTR SGSSFVGQLF NQHMDVFYLF EPLYHVQNTL IPRFTQGKSP ADRRVMLGAS
RDLLRSLYDC DLYFLENYIK PPPVNHTTDR VFRRGASRVL CSRPVCDPPG ASDLILEEGD
CVRKCGLLNL TLAAEACRER SHVAIKTVRV PEVNDLRALV EDPRLNLKVI QLVRDPRGIL
ASRSETFRDT YRLWRLWYGT GRKPYNLDVT QLTTVCEDFS SSVSTGLMRP SWLKGKYMLV
RYEDLARNPM KKTEEIYEFL GIPLDSHVAR WIQNNTRGDP TLGKHKYGTV RNSAATAEKW
RFRLSYDIVA FAQNACQHVL AQLGYKMATS EEELKNPAIS LVEERDFRPF L
//
