CHST7_MOUSE
ID CHST7_MOUSE Reviewed; 484 AA.
AC Q9EP78; Q99NB0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
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 Short=mC6ST-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; Synonyms=Gst5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10913333; DOI=10.1006/bbrc.2000.3141;
RA Uchimura K., Fasakhany F., Kadomatsu K., Matsukawa T., Yamakawa T.,
RA Kurosawa N., Muramatsu T.;
RT "Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning
RT of a novel enzyme with different distribution and specificities.";
RL Biochem. Biophys. Res. Commun. 274:291-296(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=10956661; DOI=10.1074/jbc.m006414200;
RA Bhakta S., Bartes A., Bowman K.G., Kao W.-M., Polsky I., Lee J.-K.,
RA Cook B.N., Bruehl R.E., Rosen S.D., Bertozzi C.R., Hemmerich S.;
RT "Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-
RT 5).";
RL J. Biol. Chem. 275:40226-40234(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Kitagawa H., Uyama T., Sugahara K.;
RT "Cloning and expression of mouse chondroitin 6-sulfotransferase-2.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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. {ECO:0000269|PubMed:10913333}.
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 -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in kidney.
CC Expressed at lower level in heart, lung and liver.
CC {ECO:0000269|PubMed:10913333}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
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DR EMBL; AB040710; BAB13769.1; -; mRNA.
DR EMBL; AF280089; AAG48247.1; -; Genomic_DNA.
DR EMBL; AB046929; BAB40372.1; -; mRNA.
DR EMBL; AK011202; BAB27465.1; -; mRNA.
DR EMBL; BC019204; AAH19204.1; -; mRNA.
DR CCDS; CCDS30040.1; -.
DR PIR; JC7350; JC7350.
DR RefSeq; NP_068361.1; NM_021715.1.
DR AlphaFoldDB; Q9EP78; -.
DR STRING; 10090.ENSMUSP00000043222; -.
DR GlyGen; Q9EP78; 3 sites.
DR PhosphoSitePlus; Q9EP78; -.
DR SwissPalm; Q9EP78; -.
DR MaxQB; Q9EP78; -.
DR PaxDb; Q9EP78; -.
DR PeptideAtlas; Q9EP78; -.
DR PRIDE; Q9EP78; -.
DR ProteomicsDB; 281676; -.
DR Antibodypedia; 11072; 57 antibodies from 19 providers.
DR DNASU; 60322; -.
DR Ensembl; ENSMUST00000044138; ENSMUSP00000043222; ENSMUSG00000037347.
DR GeneID; 60322; -.
DR KEGG; mmu:60322; -.
DR UCSC; uc009sss.1; mouse.
DR CTD; 56548; -.
DR MGI; MGI:1891767; Chst7.
DR VEuPathDB; HostDB:ENSMUSG00000037347; -.
DR eggNOG; ENOG502QRPV; Eukaryota.
DR GeneTree; ENSGT00940000162231; -.
DR HOGENOM; CLU_028381_1_0_1; -.
DR InParanoid; Q9EP78; -.
DR OMA; WKMNKVI; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q9EP78; -.
DR TreeFam; TF342871; -.
DR BRENDA; 2.8.2.17; 3474.
DR Reactome; R-MMU-2022870; Chondroitin sulfate biosynthesis.
DR BioGRID-ORCS; 60322; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9EP78; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9EP78; protein.
DR Bgee; ENSMUSG00000037347; Expressed in right kidney and 126 other tissues.
DR Genevisible; Q9EP78; MM.
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:MGI.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; ISO:MGI.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:MGI.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:MGI.
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..484
FT /note="Carbohydrate sulfotransferase 7"
FT /id="PRO_0000085199"
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..484
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 71..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..114
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 276..284
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS84"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 10
FT /note="E -> K (in Ref. 3; BAB40372)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="E -> D (in Ref. 3; BAB40372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 54767 MW; 9B195537D7AB7193 CRC64;
MKGRRRRRRE YCKFTLLLAL YTLLLLLVPS VLDSHSEQDK GRNCPGLQRS LGVWSLEAAA
AGEREQGAEV RSLAEGNPDR SPGSPGNLSA VGEAVTQEKQ HIYVHATWRT GSSFLGELFN
QHPDVFYLYE PMWHLWQALY PGDAESLQGA LRDMLRSLFR CDFSVLRLYA QPGDPGERAP
DSANLTTAML FRWRTNKVIC SPPLCPAAPR ARADVGLVED KACESTCPPV SLRALEAECR
KYPVVVIKDV RLLDLGVLVP LLRDPGLNLK VVQLFRDPRA VHNSRLKSRQ GLLRESIQVL
RTRQRGDHFH RVLLAHGVDA RPGGQARALP SAPRADFFLT SALEVICEAW LRDLLFTRGA
PAWLRRRYLR LRYEDLVWQP QAQLRRLLRF SGLRTLAALD AFAFNMTRGS AYGADRPFHL
SARDAREAVH AWRERLSQEQ VRQVETACAP AMRLLAYPRS GDERDRKTVR EGETPLETKA
NWAV
