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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_MOUSE             Reviewed;         388 AA.
Q9R1I1; Q9WUE5;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
30-AUG-2017, entry version 114.
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; Synonyms=Gst3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=10435581; DOI=10.1016/S1074-7613(00)80083-7;
Hiraoka N., Petryniak B., Nakayama J., Tsuboi S., Suzuki M.,
Yeh J.-C., Izawa D., Tanaka T., Miyasaka M., Lowe J.B., Fukuda M.;
"A novel, high endothelial venule-specific sulfotransferase expresses
6-sulfo sialyl Lewis(x), an L-selectin ligand displayed by CD34.";
Immunity 11:79-89(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J; 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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Tongue;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon;
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).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11520459; DOI=10.1016/S1074-7613(01)00188-1;
Hemmerich S., Bistrup A., Singer M.S., van Zante A., Lee J.K.,
Tsay D., Peters M., Carminati J.L., Brennan T.J., Carver-Moore K.,
Leviten M., Fuentes M.E., Ruddle N.H., Rosen S.D.;
"Sulfation of L-selectin ligands by an HEV-restricted sulfotransferase
regulates lymphocyte homing to lymph nodes.";
Immunity 15:237-247(2001).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14597732; DOI=10.1084/jem.20030057;
van Zante A., Gauguet J.-M., Bistrup A., Tsay D., von Andrian U.H.,
Rosen S.D.;
"Lymphocyte-HEV interactions in lymph nodes of a sulfotransferase-
deficient mouse.";
J. Exp. Med. 198:1289-1300(2003).
[7]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=15111310; DOI=10.1016/S0002-9440(10)63722-4;
Bistrup A., Tsay D., Shenoy P., Singer M.S., Bangia N., Luther S.A.,
Cyster J.G., Ruddle N.H., Rosen S.D.;
"Detection of a sulfotransferase (HEC-GlcNAc6ST) in high endothelial
venules of lymph nodes and in high endothelial venule-like vessels
within ectopic lymphoid aggregates: relationship to the MECA-79
epitope.";
Am. J. Pathol. 164:1635-1644(2004).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14593101; DOI=10.1074/jbc.M311150200;
Hiraoka N., Kawashima H., Petryniak B., Nakayama J., Mitoma J.,
Marth J.D., Lowe J.B., Fukuda M.;
"Core 2 branching beta1,6-N-acetylglucosaminyltransferase and high
endothelial venule-restricted sulfotransferase collaboratively control
lymphocyte homing.";
J. Biol. Chem. 279:3058-3067(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 SELL ligand sialyl
6-sulfo Lewis X on SELL counter-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:10435581,
ECO:0000269|PubMed:11520459, ECO:0000269|PubMed:14593101,
ECO:0000269|PubMed:14597732, ECO:0000269|PubMed:15111310}.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:15111310}; Single-pass type II membrane
protein {ECO:0000269|PubMed:15111310}.
-!- TISSUE SPECIFICITY: Specifically expressed in HEV.
{ECO:0000269|PubMed:10435581}.
-!- DISRUPTION PHENOTYPE: Mice are impaired in lymphocyte homing and
exhibit faster lymphocyte rolling and reduced lymphocyte sticking
in HEV. The epitope of SELL ligands recognized by the MECA-79
antibody is greatly reduced or abolished in the abluminal aspect
of HEV. {ECO:0000269|PubMed:11520459, ECO:0000269|PubMed:14593101,
ECO:0000269|PubMed:14597732, ECO:0000269|PubMed:15111310}.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
Gal/GlcNAc/GalNAc subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF109155; AAD45579.1; -; mRNA.
EMBL; AF131236; AAD33016.1; -; Genomic_DNA.
EMBL; AK009113; BAB26078.1; -; mRNA.
EMBL; BC057886; AAH57886.1; -; mRNA.
CCDS; CCDS22659.1; -.
RefSeq; NP_036128.3; NM_011998.4.
RefSeq; XP_006531106.1; XM_006531043.3.
RefSeq; XP_006531107.1; XM_006531044.2.
RefSeq; XP_006531108.1; XM_006531045.3.
UniGene; Mm.89207; -.
ProteinModelPortal; Q9R1I1; -.
SMR; Q9R1I1; -.
STRING; 10090.ENSMUSP00000104845; -.
PhosphoSitePlus; Q9R1I1; -.
PaxDb; Q9R1I1; -.
PRIDE; Q9R1I1; -.
GeneID; 26887; -.
KEGG; mmu:26887; -.
UCSC; uc009njt.2; mouse.
CTD; 10164; -.
MGI; MGI:1349479; Chst4.
eggNOG; ENOG410IJXD; Eukaryota.
eggNOG; ENOG4110V0B; LUCA.
HOGENOM; HOG000261614; -.
HOVERGEN; HBG050949; -.
InParanoid; Q9R1I1; -.
KO; K04746; -.
PhylomeDB; Q9R1I1; -.
TreeFam; TF342871; -.
PRO; PR:Q9R1I1; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; ISO:MGI.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0018146; P:keratan sulfate biosynthetic process; IBA:GO_Central.
GO; GO:0050901; P:leukocyte tethering or rolling; IMP:MGI.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:MGI.
GO; GO:0006477; P:protein sulfation; IMP:MGI.
GO; GO:0006790; P:sulfur compound metabolic process; ISO:MGI.
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.
2: Evidence at transcript level;
Carbohydrate metabolism; Complete proteome; Glycoprotein;
Golgi apparatus; Inflammatory response; Membrane; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 388 Carbohydrate sulfotransferase 4.
/FTId=PRO_0000085194.
TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.
TRANSMEM 8 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 388 Lumenal. {ECO:0000255}.
NP_BIND 50 56 PAPS. {ECO:0000250}.
NP_BIND 204 212 PAPS. {ECO:0000250}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 369 369 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 221 221 V -> M (in Ref. 2 and 3). {ECO:0000305}.
CONFLICT 306 306 H -> Y (in Ref. 2 and 3). {ECO:0000305}.
SEQUENCE 388 AA; 44636 MW; 6D5371AFB6884AEE CRC64;
MMLLKKGRLL MFLGSQVIVV ALFIHMSVHR HLSQREESRR PVHVLVLSSW RSGSSFVGQL
FGQHPDVFYL MEPAWHVWMT FTSSTAWKLH MAVRDLLRSV FLCDMSVFDA YMNPGPRKQS
SLFQWEQSRA LCSAPVCDFF PAHEISSPKH CKLLCGQQPF DMVEKACRSH GFVVLKEVRF
LSLQALYPLL TDPSLNLHVV HLVRDPRAVF RSREHTTIEL VVDSHIVLGQ HLETIKEEDQ
PYYAMKIICK SQVDIVKAIQ TLPEALQQRY LFLRYEDLVR APLAQTTRLY KFVGLDFLPH
LQTWVHNVTR GKGMGQHAFH TNARNALNVS QAWRWSLPYE KVSQLQDACG EAMDLLGYLQ
VRSQQEQGNL SLDLLSSSHI LGQVFREG


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