ID   CHST7_RAT               Reviewed;         485 AA.
AC   Q6XQG8; Q2TA65;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=Carbohydrate sulfotransferase 7;
DE            EC=2.8.2.-;
DE            EC=2.8.2.17;
DE   AltName: Full=Chondroitin 6-sulfotransferase 2;
DE            Short=C6ST-2;
DE   AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5;
DE            Short=GST-5;
DE   AltName: Full=N-acetylglucosamine 6-O-sulfotransferase 4;
DE            Short=GlcNAc6ST-4;
DE            Short=Gn6st-4;
GN   Name=Chst7;
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 [MRNA].
RC   STRAIN=Wistar;
RA   Seko A., Yamashita K.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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 non-reducing N-acetylglucosamine (GlcNAc) residues.
CC       Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the
CC       transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc)
CC       residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide
CC       and N-acetyllactosamine oligomer with a lower efficiency. Has weak or
CC       no activity toward keratan sulfate and oligosaccharides containing the
CC       Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not
CC       alpha- or beta-benzyl GalNAc (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=n 3'-phosphoadenylyl sulfate + chondroitin beta-D-glucuronate
CC         = n adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate + 2 H(+);
CC         Xref=Rhea:RHEA:11108, Rhea:RHEA-COMP:9827, Rhea:RHEA-COMP:9828,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57652, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:62065; EC=2.8.2.17;
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; AY216524; AAP51034.1; -; mRNA.
DR   EMBL; BC111079; AAI11080.1; -; mRNA.
DR   RefSeq; NP_997483.1; NM_207600.2.
DR   AlphaFoldDB; Q6XQG8; -.
DR   STRING; 10116.ENSRNOP00000005630; -.
DR   GlyCosmos; Q6XQG8; 3 sites, No reported glycans.
DR   GlyGen; Q6XQG8; 3 sites.
DR   PhosphoSitePlus; Q6XQG8; -.
DR   PaxDb; 10116-ENSRNOP00000005630; -.
DR   Ensembl; ENSRNOT00000005630.6; ENSRNOP00000005630.4; ENSRNOG00000004258.6.
DR   Ensembl; ENSRNOT00055028251; ENSRNOP00055022738; ENSRNOG00055016635.
DR   Ensembl; ENSRNOT00060039271; ENSRNOP00060032473; ENSRNOG00060022654.
DR   Ensembl; ENSRNOT00065034871; ENSRNOP00065028011; ENSRNOG00065020594.
DR   GeneID; 302302; -.
DR   KEGG; rno:302302; -.
DR   UCSC; RGD:1303028; rat.
DR   AGR; RGD:1303028; -.
DR   CTD; 56548; -.
DR   RGD; 1303028; Chst7.
DR   eggNOG; ENOG502QRPV; Eukaryota.
DR   GeneTree; ENSGT00940000162231; -.
DR   HOGENOM; CLU_028381_1_0_1; -.
DR   InParanoid; Q6XQG8; -.
DR   OMA; MNKVICS; -.
DR   OrthoDB; 3031241at2759; -.
DR   PhylomeDB; Q6XQG8; -.
DR   TreeFam; TF342871; -.
DR   Reactome; R-RNO-2022870; Chondroitin sulfate biosynthesis.
DR   PRO; PR:Q6XQG8; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000004258; Expressed in cerebellum and 16 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR   GO; GO:0008459; F:chondroitin 6-sulfotransferase activity; ISO:RGD.
DR   GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; ISO:RGD.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030206; P:chondroitin sulfate biosynthetic process; ISO:RGD.
DR   GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:RGD.
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:SF5; CARBOHYDRATE SULFOTRANSFERASE 7; 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; Membrane;
KW   Phosphoprotein; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..485
FT                   /note="Carbohydrate sulfotransferase 7"
FT                   /id="PRO_0000085200"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..485
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          66..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         109..115
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         277..285
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         461
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NS84"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   485 AA;  55091 MW;  C9A9C8F961478693 CRC64;
     MKGRRRRRRE YCKFTLLLAL YTLLLLLVPS VLDSGSEQDK GGRDCPGLQR SLGVWSLEAA
     AAGEREQGAE VRFQAEGNPD RSPRPQGNLS AIRESVTQEK QHIYVHATWR TGSSFLGELF
     NQHPDVFYLY EPMWHLWQAL YPGNAESLQG ALRDMLRSLF RCDFSVLRLY AQPGDPAERA
     PDSANLTTAM LFRWRTNKVI CSPPLCPAAP RARADVGLVE DKACESTCPP VPLRALEAEC
     RKYPVVVIKD VRLLDLGVLV PLLRDPGLNL KVVQLFRDPR AVHNSRLKSR HGLLRESIQV
     LRTRQRGDRF QRVLLAHGVG ARPGGQSRAL PSAPRADFFL TSALEVICEA WLRDLLFTRG
     APTWLRRRYL RLRYEDLVWQ PQVQLRRLLR FSGLRTLAAL DAFAFNMTRG SAYGADRPFH
     LSARDAREAV HAWRERLSQE QVRQVEAACD PAMRLLAYPR SGDERDVKTV RKGETPLETN
     ANWAT
//