CHST7_HUMAN
ID CHST7_HUMAN Reviewed; 486 AA.
AC Q9NS84; O75667;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Carbohydrate sulfotransferase 7;
DE EC=2.8.2.-;
DE EC=2.8.2.17 {ECO:0000269|PubMed:10781596};
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10781596; DOI=10.1074/jbc.m002101200;
RA Kitagawa H., Fujita M., Ito N., Sugahara K.;
RT "Molecular cloning and expression of a novel chondroitin 6-O-
RT sulfotransferase.";
RL J. Biol. Chem. 275:21075-21080(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-407.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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:10781596,
CC ECO:0000269|PubMed:10913333, ECO:0000269|PubMed:10956661}.
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 Evidence={ECO:0000269|PubMed:10781596};
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 heart,
CC spleen, liver and ovary. Expressed at lower level in brain, placenta,
CC thyroid, spinal cord and peripheral blood leukocytes. Not expressed in
CC adult skin. {ECO:0000269|PubMed:10781596, ECO:0000269|PubMed:10913333,
CC ECO:0000269|PubMed:10956661}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
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DR EMBL; AB040711; BAB13770.1; -; mRNA.
DR EMBL; AB037187; BAB03217.1; -; mRNA.
DR EMBL; AL022165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045537; AAH45537.1; -; mRNA.
DR CCDS; CCDS14268.1; -.
DR PIR; JC7351; JC7351.
DR RefSeq; NP_063939.2; NM_019886.3.
DR AlphaFoldDB; Q9NS84; -.
DR BioGRID; 121152; 58.
DR IntAct; Q9NS84; 1.
DR STRING; 9606.ENSP00000276055; -.
DR GlyGen; Q9NS84; 3 sites.
DR iPTMnet; Q9NS84; -.
DR PhosphoSitePlus; Q9NS84; -.
DR BioMuta; CHST7; -.
DR DMDM; 61212141; -.
DR EPD; Q9NS84; -.
DR MassIVE; Q9NS84; -.
DR MaxQB; Q9NS84; -.
DR PaxDb; Q9NS84; -.
DR PeptideAtlas; Q9NS84; -.
DR PRIDE; Q9NS84; -.
DR ProteomicsDB; 82508; -.
DR Antibodypedia; 11072; 57 antibodies from 19 providers.
DR DNASU; 56548; -.
DR Ensembl; ENST00000276055.4; ENSP00000276055.3; ENSG00000147119.4.
DR GeneID; 56548; -.
DR KEGG; hsa:56548; -.
DR MANE-Select; ENST00000276055.4; ENSP00000276055.3; NM_019886.4; NP_063939.2.
DR UCSC; uc004dgt.5; human.
DR CTD; 56548; -.
DR DisGeNET; 56548; -.
DR GeneCards; CHST7; -.
DR HGNC; HGNC:13817; CHST7.
DR HPA; ENSG00000147119; Tissue enhanced (ovary).
DR MIM; 300375; gene.
DR neXtProt; NX_Q9NS84; -.
DR OpenTargets; ENSG00000147119; -.
DR PharmGKB; PA26507; -.
DR VEuPathDB; HostDB:ENSG00000147119; -.
DR eggNOG; ENOG502QRPV; Eukaryota.
DR GeneTree; ENSGT00940000162231; -.
DR HOGENOM; CLU_028381_1_0_1; -.
DR InParanoid; Q9NS84; -.
DR OMA; WKMNKVI; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q9NS84; -.
DR TreeFam; TF342871; -.
DR BioCyc; MetaCyc:HS07394-MON; -.
DR BRENDA; 2.8.2.17; 2681.
DR PathwayCommons; Q9NS84; -.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR SABIO-RK; Q9NS84; -.
DR SignaLink; Q9NS84; -.
DR BioGRID-ORCS; 56548; 10 hits in 694 CRISPR screens.
DR ChiTaRS; CHST7; human.
DR GeneWiki; CHST7; -.
DR GenomeRNAi; 56548; -.
DR Pharos; Q9NS84; Tbio.
DR PRO; PR:Q9NS84; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NS84; protein.
DR Bgee; ENSG00000147119; Expressed in decidua and 112 other tissues.
DR Genevisible; Q9NS84; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0008459; F:chondroitin 6-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
DR GO; GO:0005976; P:polysaccharide metabolic process; TAS:UniProtKB.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..486
FT /note="Carbohydrate sulfotransferase 7"
FT /id="PRO_0000085198"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..486
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 66..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..116
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 278..286
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CONFLICT 448
FT /note="A -> V (in Ref. 2; BAB03217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 54266 MW; 3F1FD1430B3C8E95 CRC64;
MKGRRRRRRE YCKFALLLVL YTLVLLLVPS VLDGGRDGDK GAEHCPGLQR SLGVWSLEAA
AAGEREQGAE ARAAEEGGAN QSPRFPSNLS GAVGEAVSRE KQHIYVHATW RTGSSFLGEL
FNQHPDVFYL YEPMWHLWQA LYPGDAESLQ GALRDMLRSL FRCDFSVLRL YAPPGDPAAR
APDTANLTTA ALFRWRTNKV ICSPPLCPGA PRARAEVGLV EDTACERSCP PVAIRALEAE
CRKYPVVVIK DVRLLDLGVL VPLLRDPGLN LKVVQLFRDP RAVHNSRLKS RQGLLRESIQ
VLRTRQRGDR FHRVLLAHGV GARPGGQSRA LPAAPRADFF LTGALEVICE AWLRDLLFAR
GAPAWLRRRY LRLRYEDLVR QPRAQLRRLL RFSGLRALAA LDAFALNMTR GAAYGADRPF
HLSARDAREA VHAWRERLSR EQVRQVEAAC APAMRLLAYP RSGEEGDAEQ PREGETPLEM
DADGAT
