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CHST3_HUMAN
ID   CHST3_HUMAN             Reviewed;         479 AA.
AC   Q7LGC8; O75099; Q52M30;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Carbohydrate sulfotransferase 3 {ECO:0000305|PubMed:15215498};
DE            EC=2.8.2.17 {ECO:0000269|PubMed:15215498, ECO:0000269|PubMed:9714738, ECO:0000269|PubMed:9883891};
DE            EC=2.8.2.21 {ECO:0000269|PubMed:9714738};
DE   AltName: Full=Chondroitin 6-O-sulfotransferase 1;
DE            Short=C6ST-1;
DE   AltName: Full=Chondroitin 6-sulfotransferase {ECO:0000303|PubMed:9714738};
DE            Short=C6ST {ECO:0000303|PubMed:9714738};
DE   AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0;
DE            Short=GST-0;
GN   Name=CHST3;
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, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=9714738; DOI=10.1016/s0167-4781(98)00089-x;
RA   Fukuta M., Kobayashi Y., Uchimura K., Kimata K., Habuchi O.;
RT   "Molecular cloning and expression of human chondroitin 6-
RT   sulfotransferase.";
RL   Biochim. Biophys. Acta 1399:57-61(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Placenta;
RX   PubMed=9883891; DOI=10.1016/s0014-5793(98)01532-4;
RA   Tsutsumi K., Shimakawa H., Kitagawa H., Sugahara K.;
RT   "Functional expression and genomic structure of human chondroitin 6-
RT   sulfotransferase.";
RL   FEBS Lett. 441:235-241(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-357.
RC   TISSUE=Liver;
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   [4]
RP   VARIANT SEDCJD GLN-304, CHARACTERIZATION OF VARIANT SEDCJD GLN-304,
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15215498; DOI=10.1073/pnas.0400334101;
RA   Thiele H., Sakano M., Kitagawa H., Sugahara K., Rajab A., Hoehne W.,
RA   Ritter H., Leschik G., Nuernberg P., Mundlos S.;
RT   "Loss of chondroitin 6-O-sulfotransferase-1 function results in severe
RT   human chondrodysplasia with progressive spinal involvement.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:10155-10160(2004).
RN   [5]
RP   VARIANTS SEDCJD TRP-222; PRO-259; PRO-307 AND LYS-372, VARIANT GLN-357, AND
RP   CHARACTERIZATION OF VARIANTS SEDCJD TRP-222 AND PRO-259.
RX   PubMed=18513679; DOI=10.1016/j.ajhg.2008.05.006;
RA   Hermanns P., Unger S., Rossi A., Perez-Aytes A., Cortina H., Bonafe L.,
RA   Boccone L., Setzu V., Dutoit M., Sangiorgi L., Pecora F., Reicherter K.,
RA   Nishimura G., Spranger J., Zabel B., Superti-Furga A.;
RT   "Congenital joint dislocations caused by carbohydrate sulfotransferase 3
RT   deficiency in recessive Larsen syndrome and humero-spinal dysostosis.";
RL   Am. J. Hum. Genet. 82:1368-1374(2008).
RN   [6]
RP   ERRATUM OF PUBMED:18513679.
RA   Hermanns P., Unger S., Rossi A., Perez-Aytes A., Cortina H., Bonafe L.,
RA   Boccone L., Setzu V., Dutoit M., Sangiorgi L., Pecora F., Reicherter K.,
RA   Nishimura G., Spranger J., Zabel B., Superti-Furga A.;
RL   Am. J. Hum. Genet. 83:293-293(2008).
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 the N-acetylgalactosamine (GalNAc) residue of chondroitin
CC       (PubMed:9714738, PubMed:9883891, PubMed:15215498). Chondroitin sulfate
CC       constitutes the predominant proteoglycan present in cartilage and is
CC       distributed on the surfaces of many cells and extracellular matrices
CC       (PubMed:9714738). Catalyzes with a lower efficiency the sulfation of
CC       Gal residues of keratan sulfate, another glycosaminoglycan
CC       (PubMed:9714738). Can also catalyze the sulfation of the Gal residues
CC       in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides (By
CC       similarity). May play a role in the maintenance of naive T-lymphocytes
CC       in the spleen (By similarity). {ECO:0000250|UniProtKB:O88199,
CC       ECO:0000250|UniProtKB:Q92179, ECO:0000269|PubMed:15215498,
CC       ECO:0000269|PubMed:9714738, ECO:0000269|PubMed:9883891,
CC       ECO:0000303|PubMed:9714738}.
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:15215498, ECO:0000269|PubMed:9714738,
CC         ECO:0000269|PubMed:9883891};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11109;
CC         Evidence={ECO:0000269|PubMed:15215498};
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:0000269|PubMed:9714738};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Expressed in
CC       heart, placenta, skeletal muscle and pancreas. Also expressed in
CC       various immune tissues such as spleen, lymph node, thymus and appendix.
CC       {ECO:0000269|PubMed:9714738}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q92179}.
CC   -!- DISEASE: Spondyloepiphyseal dysplasia with congenital joint
CC       dislocations (SEDCJD) [MIM:143095]: A bone dysplasia clinically
CC       characterized by dislocation of the knees and/or hips at birth,
CC       clubfoot, elbow joint dysplasia with subluxation and limited extension,
CC       short stature, and progressive kyphosis developing in late childhood.
CC       The disorder is usually evident at birth, with short stature and
CC       multiple joint dislocations or subluxations that dominate the neonatal
CC       clinical and radiographic picture. During childhood, the dislocations
CC       improve, both spontaneously and with surgical treatment, and features
CC       of spondyloepiphyseal dysplasia become apparent, leading to arthritis
CC       of the hips and spine with intervertebral disk degeneration, rigid
CC       kyphoscoliosis, and trunk shortening by late childhood.
CC       {ECO:0000269|PubMed:15215498, ECO:0000269|PubMed:18513679}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB012192; BAA32576.1; -; mRNA.
DR   EMBL; AB017915; BAA36348.1; -; mRNA.
DR   EMBL; BC093690; AAH93690.1; -; mRNA.
DR   EMBL; BC104856; AAI04857.1; -; mRNA.
DR   CCDS; CCDS7312.1; -.
DR   RefSeq; NP_004264.2; NM_004273.4.
DR   RefSeq; XP_006718138.1; XM_006718075.3.
DR   RefSeq; XP_011538671.1; XM_011540369.2.
DR   AlphaFoldDB; Q7LGC8; -.
DR   BioGRID; 114855; 14.
DR   IntAct; Q7LGC8; 5.
DR   STRING; 9606.ENSP00000362207; -.
DR   GlyGen; Q7LGC8; 6 sites.
DR   iPTMnet; Q7LGC8; -.
DR   PhosphoSitePlus; Q7LGC8; -.
DR   BioMuta; CHST3; -.
DR   DMDM; 116241297; -.
DR   CPTAC; CPTAC-1483; -.
DR   EPD; Q7LGC8; -.
DR   jPOST; Q7LGC8; -.
DR   MassIVE; Q7LGC8; -.
DR   MaxQB; Q7LGC8; -.
DR   PaxDb; Q7LGC8; -.
DR   PeptideAtlas; Q7LGC8; -.
DR   PRIDE; Q7LGC8; -.
DR   ProteomicsDB; 68868; -.
DR   Antibodypedia; 29214; 183 antibodies from 30 providers.
DR   DNASU; 9469; -.
DR   Ensembl; ENST00000373115.5; ENSP00000362207.4; ENSG00000122863.6.
DR   GeneID; 9469; -.
DR   KEGG; hsa:9469; -.
DR   MANE-Select; ENST00000373115.5; ENSP00000362207.4; NM_004273.5; NP_004264.2.
DR   UCSC; uc001jsn.4; human.
DR   CTD; 9469; -.
DR   DisGeNET; 9469; -.
DR   GeneCards; CHST3; -.
DR   GeneReviews; CHST3; -.
DR   HGNC; HGNC:1971; CHST3.
DR   HPA; ENSG00000122863; Low tissue specificity.
DR   MalaCards; CHST3; -.
DR   MIM; 143095; phenotype.
DR   MIM; 603799; gene.
DR   neXtProt; NX_Q7LGC8; -.
DR   OpenTargets; ENSG00000122863; -.
DR   Orphanet; 263463; CHST3-related skeletal dysplasia.
DR   PharmGKB; PA26503; -.
DR   VEuPathDB; HostDB:ENSG00000122863; -.
DR   eggNOG; ENOG502QWEX; Eukaryota.
DR   GeneTree; ENSGT00940000161045; -.
DR   HOGENOM; CLU_028381_3_2_1; -.
DR   InParanoid; Q7LGC8; -.
DR   OMA; QFDKWRF; -.
DR   OrthoDB; 1246608at2759; -.
DR   PhylomeDB; Q7LGC8; -.
DR   TreeFam; TF342871; -.
DR   BioCyc; MetaCyc:HS04610-MON; -.
DR   BRENDA; 2.8.2.17; 2681.
DR   PathwayCommons; Q7LGC8; -.
DR   Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR   Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
DR   SignaLink; Q7LGC8; -.
DR   BioGRID-ORCS; 9469; 15 hits in 1068 CRISPR screens.
DR   ChiTaRS; CHST3; human.
DR   GenomeRNAi; 9469; -.
DR   Pharos; Q7LGC8; Tbio.
DR   PRO; PR:Q7LGC8; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q7LGC8; protein.
DR   Bgee; ENSG00000122863; Expressed in tibia and 158 other tissues.
DR   Genevisible; Q7LGC8; HS.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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; IDA:UniProtKB.
DR   GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006044; P:N-acetylglucosamine metabolic process; IBA:GO_Central.
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; Disease variant; Glycoprotein; Golgi apparatus;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..479
FT                   /note="Carbohydrate sulfotransferase 3"
FT                   /id="PRO_0000085188"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..38
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..479
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          108..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         141..147
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         301..309
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         222
FT                   /note="R -> W (in SEDCJD; decreased chondroitin sulfate
FT                   biosynthetic process; dbSNP:rs121908617)"
FT                   /evidence="ECO:0000269|PubMed:18513679"
FT                   /id="VAR_047856"
FT   VARIANT         259
FT                   /note="L -> P (in SEDCJD; decreased chondroitin sulfate
FT                   biosynthetic process; dbSNP:rs121908616)"
FT                   /evidence="ECO:0000269|PubMed:18513679"
FT                   /id="VAR_047857"
FT   VARIANT         304
FT                   /note="R -> Q (in SEDCJD; loss of chondroitin 6-
FT                   sulfotransferase activity; dbSNP:rs28937593)"
FT                   /evidence="ECO:0000269|PubMed:15215498"
FT                   /id="VAR_021413"
FT   VARIANT         307
FT                   /note="L -> P (in SEDCJD; dbSNP:rs121908618)"
FT                   /evidence="ECO:0000269|PubMed:18513679"
FT                   /id="VAR_047858"
FT   VARIANT         348
FT                   /note="I -> M (in dbSNP:rs3740128)"
FT                   /id="VAR_021414"
FT   VARIANT         357
FT                   /note="R -> Q (in dbSNP:rs3740129)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:18513679"
FT                   /id="VAR_021415"
FT   VARIANT         372
FT                   /note="E -> K (in SEDCJD; dbSNP:rs267606734)"
FT                   /evidence="ECO:0000269|PubMed:18513679"
FT                   /id="VAR_047859"
FT   CONFLICT        387
FT                   /note="R -> P (in Ref. 1; BAA32576)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443
FT                   /note="A -> P (in Ref. 1; BAA32576)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   479 AA;  54706 MW;  7C290DC4970F66E0 CRC64;
     MEKGLTLPQD CRDFVHSLKM RSKYALFLVF VVIVFVFIEK ENKIISRVSD KLKQIPQALA
     DANSTDPALI LAENASLLSL SELDSAFSQL QSRLRNLSLQ LGVEPAMEAA GEEEEEQRKE
     EEPPRPAVAG PRRHVLLMAT TRTGSSFVGE FFNQQGNIFY LFEPLWHIER TVSFEPGGAN
     AAGSALVYRD VLKQLFLCDL YVLEHFITPL PEDHLTQFMF RRGSSRSLCE DPVCTPFVKK
     VFEKYHCKNR RCGPLNVTLA AEACRRKEHM ALKAVRIRQL EFLQPLAEDP RLDLRVIQLV
     RDPRAVLASR MVAFAGKYKT WKKWLDDEGQ DGLREEEVQR LRGNCESIRL SAELGLRQPA
     WLRGRYMLVR YEDVARGPLQ KAREMYRFAG IPLTPQVEDW IQKNTQAAHD GSGIYSTQKN
     SSEQFEKWRF SMPFKLAQVV QAACGPAMRL FGYKLARDAA ALTNRSVSLL EERGTFWVT
 
 
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