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Carbohydrate sulfotransferase 4 (EC 2.8.2.-) (Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3) (GST-3) (High endothelial cells N-acetylglucosamine 6-O-sulfotransferase) (HEC-GlcNAc6ST) (L-selectin ligand sulfotransferase) (LSST) (N-acetylglucosamine 6-O-sulfotransferase 2) (GlcNAc6ST-2) (Gn6st-2)

 CHST4_HUMAN             Reviewed;         386 AA.
Q8NCG5; Q8IV46; Q9Y5R3;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 2.
27-SEP-2017, entry version 123.
RecName: Full=Carbohydrate sulfotransferase 4;
EC=2.8.2.-;
AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3;
Short=GST-3;
AltName: Full=High endothelial cells N-acetylglucosamine 6-O-sulfotransferase;
Short=HEC-GlcNAc6ST;
AltName: Full=L-selectin ligand sulfotransferase;
Short=LSST;
AltName: Full=N-acetylglucosamine 6-O-sulfotransferase 2;
Short=GlcNAc6ST-2;
Short=Gn6st-2;
Name=CHST4;
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=Tonsil;
PubMed=10330415; DOI=10.1083/jcb.145.4.899;
Bistrup A., Bhakta S., Lee J.K., Belov Y.Y., Gunn M.D., Zuo F.-R.,
Huang C.-C., Kannagi R., Rosen S.D., Hemmerich S.;
"Sulfotransferases of two specificities function in the reconstitution
of high endothelial cell ligands for L-selectin.";
J. Cell Biol. 145:899-910(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11439191; DOI=10.1016/S0092-8674(01)00394-4;
Yeh J.-C., Hiraoka N., Petryniak B., Nakayama J., Ellies L.G.,
Rabuka D., Hindsgaul O., Marth J.D., Lowe J.B., Fukuda M.;
"Novel sulfated lymphocyte homing receptors and their control by a
Core1 extension beta 1,3-N-acetylglucosaminyltransferase.";
Cell 105:957-969(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Tonsil;
PubMed=11181564; DOI=10.1093/glycob/11.1.75;
Hemmerich S., Lee J.K., Bhakta S., Bistrup A., Ruddle N.R.,
Rosen S.D.;
"Chromosomal localization and genomic organization for the galactose/
N-acetylgalactosamine/N-acetylglucosamine 6-O-sulfotransferase gene
family.";
Glycobiology 11:75-87(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[6]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11310842;
Li X., Tu L., Murphy P.G., Kadono T., Steeber D.A., Tedder T.F.;
"CHST1 and CHST2 sulfotransferase expression by vascular endothelial
cells regulates shear-resistant leukocyte rolling via L-selectin.";
J. Leukoc. Biol. 69:565-574(2001).
[7]
TISSUE SPECIFICITY.
PubMed=12107080; DOI=10.1093/glycob/12.6.379;
Seko A., Nagata K., Yonezawa S., Yamashita K.;
"Ectopic expression of a GlcNAc 6-O-sulfotransferase, GlcNAc6ST-2, in
colonic mucinous adenocarcinoma.";
Glycobiology 12:379-388(2002).
[8]
SUBSTRATE SPECIFICITY.
PubMed=11726653; DOI=10.1074/jbc.M106587200;
Uchimura K., El-Fasakhany F.M., Hori M., Hemmerich S., Blink S.E.,
Kansas G.S., Kanamori A., Kumamoto K., Kannagi R., Muramatsu T.;
"Specificities of N-acetylglucosamine-6-O-sulfotransferases in
relation to L-selectin ligand synthesis and tumor-associated enzyme
expression.";
J. Biol. Chem. 277:3979-3984(2002).
[9]
SUBCELLULAR LOCATION.
PubMed=12855678; DOI=10.1074/jbc.M304928200;
de Graffenried C.L., Bertozzi C.R.;
"Golgi localization of carbohydrate sulfotransferases is a determinant
of L-selectin ligand biosynthesis.";
J. Biol. Chem. 278:40282-40295(2003).
[10]
SUBUNIT.
PubMed=15220337; DOI=10.1074/jbc.M405709200;
de Graffenried C.L., Bertozzi C.R.;
"The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant
of substrate specificity.";
J. Biol. Chem. 279:40035-40043(2004).
-!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl
sulfate (PAPS) as sulfonate donor to catalyze the transfer of
sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc)
residues within mucin-associated glycans that ultimately serve as
SELL ligands. SELL ligands are present in high endothelial cells
(HEVs) and play a central role in lymphocyte homing at sites of
inflammation. Participates in biosynthesis of the SELL ligand
sialyl 6-sulfo Lewis X on receptors SPN/CD43, GLYCAM1 and MADCAM1.
Also involved in biosynthesis of SELL ligand recognized by MECA-79
antibody. Plays a central role in lymphocyte trafficking during
chronic inflammation. Has a catalytic preference for core 2-
branched mucin-type O-glycans. Can use GlcNAcbeta1-6[Galbeta1-
3]GalNAc-pNP (core 2), GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man
oligosaccharide structures as acceptors. Has also activity toward
core 3 of GlcNAcbeta1-3GalNAc-pNP. Its substrate specificity may
be influenced by its subcellular location.
{ECO:0000269|PubMed:10330415}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15220337}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:12855678}; Single-pass type II membrane
protein {ECO:0000269|PubMed:12855678}.
-!- TISSUE SPECIFICITY: Specifically expressed in HEV. Weakly
expressed in spleen. Not expressed in other tissues. Expressed in
colonic mucinous adenocarcinoma. {ECO:0000269|PubMed:10330415,
ECO:0000269|PubMed:11310842, ECO:0000269|PubMed:12107080}.
-!- INDUCTION: Upon cytokine activation, it is expressed at low level.
{ECO:0000269|PubMed:11310842}.
-!- MISCELLANEOUS: May serve as an antiinflammatory target.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
Gal/GlcNAc/GalNAc subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH35282.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF131235; AAD33015.1; -; mRNA.
EMBL; AF149783; AAK48417.1; -; mRNA.
EMBL; AF280088; AAG48246.1; -; mRNA.
EMBL; AK074746; BAC11177.1; -; mRNA.
EMBL; BC035282; AAH35282.1; ALT_INIT; mRNA.
CCDS; CCDS10902.1; -.
RefSeq; NP_001159867.1; NM_001166395.1.
RefSeq; NP_005760.1; NM_005769.2.
UniGene; Hs.251383; -.
ProteinModelPortal; Q8NCG5; -.
BioGrid; 115466; 2.
IntAct; Q8NCG5; 1.
STRING; 9606.ENSP00000341206; -.
ChEMBL; CHEMBL2239; -.
iPTMnet; Q8NCG5; -.
PhosphoSitePlus; Q8NCG5; -.
BioMuta; CHST4; -.
DMDM; 61211834; -.
EPD; Q8NCG5; -.
PaxDb; Q8NCG5; -.
PeptideAtlas; Q8NCG5; -.
PRIDE; Q8NCG5; -.
DNASU; 10164; -.
Ensembl; ENST00000338482; ENSP00000341206; ENSG00000140835.
Ensembl; ENST00000539698; ENSP00000441204; ENSG00000140835.
GeneID; 10164; -.
KEGG; hsa:10164; -.
UCSC; uc002fan.4; human.
CTD; 10164; -.
DisGeNET; 10164; -.
EuPathDB; HostDB:ENSG00000140835.9; -.
GeneCards; CHST4; -.
HGNC; HGNC:1972; CHST4.
HPA; HPA021955; -.
neXtProt; NX_Q8NCG5; -.
OpenTargets; ENSG00000140835; -.
PharmGKB; PA26504; -.
eggNOG; ENOG410IJXD; Eukaryota.
eggNOG; ENOG4110V0B; LUCA.
GeneTree; ENSGT00530000062902; -.
HOGENOM; HOG000261614; -.
HOVERGEN; HBG050949; -.
InParanoid; Q8NCG5; -.
KO; K04746; -.
OMA; MQVICQS; -.
OrthoDB; EOG091G0V3Y; -.
PhylomeDB; Q8NCG5; -.
TreeFam; TF342871; -.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
SABIO-RK; Q8NCG5; -.
GeneWiki; CHST4; -.
GenomeRNAi; 10164; -.
PRO; PR:Q8NCG5; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000140835; -.
CleanEx; HS_CHST4; -.
Genevisible; Q8NCG5; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0031228; C:intrinsic component of Golgi membrane; NAS:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IDA:UniProtKB.
GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0018146; P:keratan sulfate biosynthetic process; IBA:GO_Central.
GO; GO:0006928; P:movement of cell or subcellular component; TAS:ProtInc.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0006477; P:protein sulfation; TAS:ProtInc.
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; Glycoprotein;
Golgi apparatus; Inflammatory response; Membrane; Polymorphism;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 386 Carbohydrate sulfotransferase 4.
/FTId=PRO_0000085193.
TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.
TRANSMEM 8 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 386 Lumenal. {ECO:0000255}.
NP_BIND 51 57 PAPS. {ECO:0000250}.
NP_BIND 205 213 PAPS. {ECO:0000250}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 361 361 H -> Q (in dbSNP:rs3813744).
/FTId=VAR_052528.
CONFLICT 225 225 S -> N (in Ref. 4; BAC11177).
{ECO:0000305}.
SEQUENCE 386 AA; 45134 MW; 0C3BB4022417143A CRC64;
MLLPKKMKLL LFLVSQMAIL ALFFHMYSHN ISSLSMKAQP ERMHVLVLSS WRSGSSFVGQ
LFGQHPDVFY LMEPAWHVWM TFKQSTAWML HMAVRDLIRA VFLCDMSVFD AYMEPGPRRQ
SSLFQWENSR ALCSAPACDI IPQDEIIPRA HCRLLCSQQP FEVVEKACRS YSHVVLKEVR
FFNLQSLYPL LKDPSLNLHI VHLVRDPRAV FRSRERTKGD LMIDSRIVMG QHEQKLKKED
QPYYVMQVIC QSQLEIYKTI QSLPKALQER YLLVRYEDLA RAPVAQTSRM YEFVGLEFLP
HLQTWVHNIT RGKGMGDHAF HTNARDALNV SQAWRWSLPY EKVSRLQKAC GDAMNLLGYR
HVRSEQEQRN LLLDLLSTWT VPEQIH


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