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Q9R1I1 (CHST4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbohydrate sulfotransferase 4

EC=2.8.2.-
Alternative name(s):
Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3
Short name=GST-3
High endothelial cells N-acetylglucosamine 6-O-sulfotransferase
Short name=HEC-GlcNAc6ST
L-selectin ligand sulfotransferase
Short name=LSST
N-acetylglucosamine 6-O-sulfotransferase 2
Short name=GlcNAc6ST-2
Short name=Gn6st-2
Gene names
Name:Chst4
Synonyms:Gst3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8

Subunit structure

Monomer By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Ref.7.

Tissue specificity

Specifically expressed in HEV. Ref.1

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. Ref.5 Ref.6 Ref.7 Ref.8

Sequence similarities

Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Carbohydrate sulfotransferase 4
PRO_0000085194

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 388360Lumenal Potential
Nucleotide binding50 – 567PAPS By similarity
Nucleotide binding204 – 2129PAPS By similarity

Amino acid modifications

Glycosylation3071N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation3691N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2211V → M Ref.2
Sequence conflict2211V → M Ref.3
Sequence conflict3061H → Y Ref.2
Sequence conflict3061H → Y Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9R1I1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6D5371AFB6884AEE

FASTA38844,636
        10         20         30         40         50         60 
MMLLKKGRLL MFLGSQVIVV ALFIHMSVHR HLSQREESRR PVHVLVLSSW RSGSSFVGQL 

        70         80         90        100        110        120 
FGQHPDVFYL MEPAWHVWMT FTSSTAWKLH MAVRDLLRSV FLCDMSVFDA YMNPGPRKQS 

       130        140        150        160        170        180 
SLFQWEQSRA LCSAPVCDFF PAHEISSPKH CKLLCGQQPF DMVEKACRSH GFVVLKEVRF 

       190        200        210        220        230        240 
LSLQALYPLL TDPSLNLHVV HLVRDPRAVF RSREHTTIEL VVDSHIVLGQ HLETIKEEDQ 

       250        260        270        280        290        300 
PYYAMKIICK SQVDIVKAIQ TLPEALQQRY LFLRYEDLVR APLAQTTRLY KFVGLDFLPH 

       310        320        330        340        350        360 
LQTWVHNVTR GKGMGQHAFH TNARNALNVS QAWRWSLPYE KVSQLQDACG EAMDLLGYLQ 

       370        380 
VRSQQEQGNL SLDLLSSSHI LGQVFREG 

« Hide

References

« Hide 'large scale' references
[1]"A novel, high endothelial venule-specific sulfotransferase expresses 6-sulfo sialyl Lewis(x), an L-selectin ligand displayed by CD34."
Hiraoka N., Petryniak B., Nakayama J., Tsuboi S., Suzuki M., Yeh J.-C., Izawa D., Tanaka T., Miyasaka M., Lowe J.B., Fukuda M.
Immunity 11:79-89(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin."
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.
J. Cell Biol. 145:899-910(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/6.
Tissue: Tonsil.
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Tongue.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
[5]"Sulfation of L-selectin ligands by an HEV-restricted sulfotransferase regulates lymphocyte homing to lymph nodes."
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.
Immunity 15:237-247(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"Lymphocyte-HEV interactions in lymph nodes of a sulfotransferase-deficient mouse."
van Zante A., Gauguet J.-M., Bistrup A., Tsay D., von Andrian U.H., Rosen S.D.
J. Exp. Med. 198:1289-1300(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"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."
Bistrup A., Tsay D., Shenoy P., Singer M.S., Bangia N., Luther S.A., Cyster J.G., Ruddle N.H., Rosen S.D.
Am. J. Pathol. 164:1635-1644(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
[8]"Core 2 branching beta1,6-N-acetylglucosaminyltransferase and high endothelial venule-restricted sulfotransferase collaboratively control lymphocyte homing."
Hiraoka N., Kawashima H., Petryniak B., Nakayama J., Mitoma J., Marth J.D., Lowe J.B., Fukuda M.
J. Biol. Chem. 279:3058-3067(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF109155 mRNA. Translation: AAD45579.1.
AF131236 Genomic DNA. Translation: AAD33016.1.
AK009113 mRNA. Translation: BAB26078.1.
BC057886 mRNA. Translation: AAH57886.1.
RefSeqNP_036128.3. NM_011998.4.
XP_006531106.1. XM_006531043.1.
XP_006531107.1. XM_006531044.1.
XP_006531108.1. XM_006531045.1.
UniGeneMm.89207.

3D structure databases

ProteinModelPortalQ9R1I1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000104845.

PTM databases

PhosphoSiteQ9R1I1.

Proteomic databases

PRIDEQ9R1I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109222; ENSMUSP00000104845; ENSMUSG00000035930.
GeneID26887.
KEGGmmu:26887.
UCSCuc009njt.2. mouse.

Organism-specific databases

CTD10164.
MGIMGI:1349479. Chst4.

Phylogenomic databases

eggNOGNOG80862.
GeneTreeENSGT00530000062902.
HOGENOMHOG000261614.
HOVERGENHBG050949.
InParanoidQ9R1I1.
KOK04746.
OrthoDBEOG7RZ5S0.
PhylomeDBQ9R1I1.
TreeFamTF342871.

Gene expression databases

BgeeQ9R1I1.
GenevestigatorQ9R1I1.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
PIRSFPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

NextBio304707.
PROQ9R1I1.
SOURCESearch...

Entry information

Entry nameCHST4_MOUSE
AccessionPrimary (citable) accession number: Q9R1I1
Secondary accession number(s): Q9WUE5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot