CHST7_RAT
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 03-AUG-2022, entry version 110.
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 GlyGen; Q6XQG8; 3 sites.
DR PaxDb; Q6XQG8; -.
DR Ensembl; ENSRNOT00000005630; ENSRNOP00000005630; ENSRNOG00000004258.
DR GeneID; 302302; -.
DR KEGG; rno:302302; -.
DR UCSC; RGD:1303028; rat.
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; WKMNKVI; -.
DR OrthoDB; 1246608at2759; -.
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 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: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; -; 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; 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
