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CHST1_RAT
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   03-AUG-2022, entry version 112.
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   GlyGen; Q5RJQ0; 4 sites.
DR   PaxDb; Q5RJQ0; -.
DR   Ensembl; ENSRNOT00000010510; ENSRNOP00000010510; ENSRNOG00000007989.
DR   Ensembl; ENSRNOT00000095049; ENSRNOP00000090213; ENSRNOG00000007989.
DR   Ensembl; ENSRNOT00000095051; ENSRNOP00000081989; ENSRNOG00000007989.
DR   Ensembl; ENSRNOT00000098205; ENSRNOP00000087464; ENSRNOG00000007989.
DR   Ensembl; ENSRNOT00000113200; ENSRNOP00000079857; ENSRNOG00000007989.
DR   Ensembl; ENSRNOT00000114058; ENSRNOP00000086161; ENSRNOG00000007989.
DR   GeneID; 295934; -.
DR   KEGG; rno:295934; -.
DR   UCSC; RGD:1308142; rat.
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; 1246608at2759; -.
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 tissues.
DR   Genevisible; Q5RJQ0; RN.
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: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; -; 1.
DR   InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR   SUPFAM; SSF52540; SSF52540; 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
 
 
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