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Carbohydrate sulfotransferase 3 (EC 2.8.2.17) (Chondroitin 6-O-sulfotransferase 1) (C6ST-1) (Chondroitin 6-sulfotransferase) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0) (GST-0)

 CHST3_HUMAN             Reviewed;         479 AA.
Q7LGC8; O75099; Q52M30;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
20-JUN-2018, entry version 136.
RecName: Full=Carbohydrate sulfotransferase 3;
EC=2.8.2.17;
AltName: Full=Chondroitin 6-O-sulfotransferase 1;
Short=C6ST-1;
AltName: Full=Chondroitin 6-sulfotransferase;
AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0;
Short=GST-0;
Name=CHST3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=9714738; DOI=10.1016/S0167-4781(98)00089-X;
Fukuta M., Kobayashi Y., Uchimura K., Kimata K., Habuchi O.;
"Molecular cloning and expression of human chondroitin 6-
sulfotransferase.";
Biochim. Biophys. Acta 1399:57-61(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Placenta;
PubMed=9883891; DOI=10.1016/S0014-5793(98)01532-4;
Tsutsumi K., Shimakawa H., Kitagawa H., Sugahara K.;
"Functional expression and genomic structure of human chondroitin 6-
sulfotransferase.";
FEBS Lett. 441:235-241(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-357.
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
VARIANT SEDCJD GLN-304.
PubMed=15215498; DOI=10.1073/pnas.0400334101;
Thiele H., Sakano M., Kitagawa H., Sugahara K., Rajab A., Hoehne W.,
Ritter H., Leschik G., Nuernberg P., Mundlos S.;
"Loss of chondroitin 6-O-sulfotransferase-1 function results in severe
human chondrodysplasia with progressive spinal involvement.";
Proc. Natl. Acad. Sci. U.S.A. 101:10155-10160(2004).
[5]
VARIANTS SEDCJD TRP-222; PRO-259; PRO-307 AND LYS-372, VARIANT
GLN-357, AND CHARACTERIZATION OF VARIANTS SEDCJD TRP-222 AND PRO-259.
PubMed=18513679; DOI=10.1016/j.ajhg.2008.05.006;
Hermanns P., Unger S., Rossi A., Perez-Aytes A., Cortina H.,
Bonafe L., Boccone L., Setzu V., Dutoit M., Sangiorgi L., Pecora F.,
Reicherter K., Nishimura G., Spranger J., Zabel B., Superti-Furga A.;
"Congenital joint dislocations caused by carbohydrate sulfotransferase
3 deficiency in recessive Larsen syndrome and humero-spinal
dysostosis.";
Am. J. Hum. Genet. 82:1368-1374(2008).
[6]
ERRATUM.
Hermanns P., Unger S., Rossi A., Perez-Aytes A., Cortina H.,
Bonafe L., Boccone L., Setzu V., Dutoit M., Sangiorgi L., Pecora F.,
Reicherter K., Nishimura G., Spranger J., Zabel B., Superti-Furga A.;
Am. J. Hum. Genet. 83:293-293(2008).
-!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl
sulfate (PAPS) as sulfonate donor to catalyze the transfer of
sulfate to position 6 of the N-acetylgalactosamine (GalNAc)
residue of chondroitin. Chondroitin sulfate constitutes the
predominant proteoglycan present in cartilage and is distributed
on the surfaces of many cells and extracellular matrices. Can also
sulfate Gal residues of keratan sulfate, another
glycosaminoglycan, and the Gal residues in sialyl N-
acetyllactosamine (sialyl LacNAc) oligosaccharides. May play a
role in the maintenance of naive T-lymphocytes in the spleen.
{ECO:0000269|PubMed:9714738, ECO:0000269|PubMed:9883891}.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + chondroitin =
adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Expressed
in heart, placenta, skeletal muscle and pancreas. Also expressed
in various immune tissues such as spleen, lymph node, thymus and
appendix. {ECO:0000269|PubMed:9714738}.
-!- DISEASE: Spondyloepiphyseal dysplasia with congenital joint
dislocations (SEDCJD) [MIM:143095]: A bone dysplasia clinically
characterized by dislocation of the knees and/or hips at birth,
clubfoot, elbow joint dysplasia with subluxation and limited
extension, short stature, and progressive kyphosis developing in
late childhood. The disorder is usually evident at birth, with
short stature and multiple joint dislocations or subluxations that
dominate the neonatal clinical and radiographic picture. During
childhood, the dislocations improve, both spontaneously and with
surgical treatment, and features of spondyloepiphyseal dysplasia
become apparent, leading to arthritis of the hips and spine with
intervertebral disk degeneration, rigid kyphoscoliosis, and trunk
shortening by late childhood. {ECO:0000269|PubMed:15215498,
ECO:0000269|PubMed:18513679}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
Gal/GlcNAc/GalNAc subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB012192; BAA32576.1; -; mRNA.
EMBL; AB017915; BAA36348.1; -; mRNA.
EMBL; BC093690; AAH93690.1; -; mRNA.
EMBL; BC104856; AAI04857.1; -; mRNA.
CCDS; CCDS7312.1; -.
RefSeq; NP_004264.2; NM_004273.4.
RefSeq; XP_006718138.1; XM_006718075.3.
RefSeq; XP_011538671.1; XM_011540369.2.
UniGene; Hs.158304; -.
ProteinModelPortal; Q7LGC8; -.
BioGrid; 114855; 6.
IntAct; Q7LGC8; 1.
STRING; 9606.ENSP00000362207; -.
iPTMnet; Q7LGC8; -.
PhosphoSitePlus; Q7LGC8; -.
BioMuta; CHST3; -.
DMDM; 116241297; -.
EPD; Q7LGC8; -.
MaxQB; Q7LGC8; -.
PaxDb; Q7LGC8; -.
PeptideAtlas; Q7LGC8; -.
PRIDE; Q7LGC8; -.
ProteomicsDB; 68868; -.
Ensembl; ENST00000373115; ENSP00000362207; ENSG00000122863.
GeneID; 9469; -.
KEGG; hsa:9469; -.
UCSC; uc001jsn.4; human.
CTD; 9469; -.
DisGeNET; 9469; -.
EuPathDB; HostDB:ENSG00000122863.5; -.
GeneCards; CHST3; -.
GeneReviews; CHST3; -.
HGNC; HGNC:1971; CHST3.
HPA; HPA047523; -.
HPA; HPA055704; -.
MalaCards; CHST3; -.
MIM; 143095; phenotype.
MIM; 603799; gene.
neXtProt; NX_Q7LGC8; -.
OpenTargets; ENSG00000122863; -.
Orphanet; 263463; CHST3-related skeletal dysplasia.
PharmGKB; PA26503; -.
eggNOG; ENOG410IIAV; Eukaryota.
eggNOG; ENOG410YDA4; LUCA.
GeneTree; ENSGT00530000062902; -.
HOGENOM; HOG000261614; -.
HOVERGEN; HBG106811; -.
InParanoid; Q7LGC8; -.
KO; K01020; -.
OMA; FERYHCK; -.
OrthoDB; EOG091G0V3Y; -.
PhylomeDB; Q7LGC8; -.
TreeFam; TF342871; -.
BioCyc; MetaCyc:HS04610-MONOMER; -.
BRENDA; 2.8.2.17; 2681.
Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
Reactome; R-HSA-3595172; Defective CHST3 causes SEDCJD.
GenomeRNAi; 9469; -.
PRO; PR:Q7LGC8; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000122863; -.
CleanEx; HS_CHST3; -.
Genevisible; Q7LGC8; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0008459; F:chondroitin 6-sulfotransferase activity; IDA:UniProtKB.
GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IBA:GO_Central.
GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:UniProtKB.
GO; GO:0006790; P:sulfur compound metabolic process; IDA:UniProtKB.
InterPro; IPR016469; Carbohydrate_sulfotransferase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000863; Sulfotransferase_dom.
Pfam; PF00685; Sulfotransfer_1; 1.
PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
SUPFAM; SSF52540; SSF52540; 2.
1: Evidence at protein level;
Carbohydrate metabolism; Complete proteome; Disease mutation;
Glycoprotein; Golgi apparatus; Membrane; Polymorphism;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 479 Carbohydrate sulfotransferase 3.
/FTId=PRO_0000085188.
TOPO_DOM 1 20 Cytoplasmic. {ECO:0000255}.
TRANSMEM 21 38 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 39 479 Lumenal. {ECO:0000255}.
NP_BIND 141 147 PAPS. {ECO:0000250}.
NP_BIND 301 309 PAPS. {ECO:0000250}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 420 420 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 222 222 R -> W (in SEDCJD; severely impairs or
abolishes the enzyme function;
dbSNP:rs121908617).
{ECO:0000269|PubMed:18513679}.
/FTId=VAR_047856.
VARIANT 259 259 L -> P (in SEDCJD; severely impairs or
abolishes the enzyme function;
dbSNP:rs121908616).
{ECO:0000269|PubMed:18513679}.
/FTId=VAR_047857.
VARIANT 304 304 R -> Q (in SEDCJD; abolishes enzyme
activity; dbSNP:rs28937593).
{ECO:0000269|PubMed:15215498}.
/FTId=VAR_021413.
VARIANT 307 307 L -> P (in SEDCJD; dbSNP:rs121908618).
{ECO:0000269|PubMed:18513679}.
/FTId=VAR_047858.
VARIANT 348 348 I -> M (in dbSNP:rs3740128).
/FTId=VAR_021414.
VARIANT 357 357 R -> Q (in dbSNP:rs3740129).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18513679}.
/FTId=VAR_021415.
VARIANT 372 372 E -> K (in SEDCJD; dbSNP:rs267606734).
{ECO:0000269|PubMed:18513679}.
/FTId=VAR_047859.
CONFLICT 387 387 R -> P (in Ref. 1; BAA32576).
{ECO:0000305}.
CONFLICT 443 443 A -> P (in Ref. 1; BAA32576).
{ECO:0000305}.
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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