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Q9R1I1

- CHST4_MOUSE

UniProt

Q9R1I1 - CHST4_MOUSE

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Protein

Carbohydrate sulfotransferase 4

Gene

Chst4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi50 – 567PAPSBy similarity
Nucleotide bindingi204 – 2129PAPSBy similarity

GO - Molecular functioni

  1. N-acetylglucosamine 6-O-sulfotransferase activity Source: Ensembl

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
  2. inflammatory response Source: UniProtKB-KW
  3. leukocyte tethering or rolling Source: MGI
  4. N-acetylglucosamine metabolic process Source: Ensembl
  5. protein sulfation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carbohydrate metabolism, Inflammatory response

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Chst4
Synonyms:Gst3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1349479. Chst4.

Subcellular locationi

Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

GO - Cellular componenti

  1. Golgi membrane Source: InterPro
  2. integral component of membrane Source: UniProtKB-KW
  3. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

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.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388Carbohydrate sulfotransferase 4PRO_0000085194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi369 – 3691N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9R1I1.

PTM databases

PhosphoSiteiQ9R1I1.

Expressioni

Tissue specificityi

Specifically expressed in HEV.1 Publication

Gene expression databases

BgeeiQ9R1I1.
GenevestigatoriQ9R1I1.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000104845.

Structurei

3D structure databases

ProteinModelPortaliQ9R1I1.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence Analysis
Topological domaini29 – 388360LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG80862.
GeneTreeiENSGT00530000062902.
HOGENOMiHOG000261614.
HOVERGENiHBG050949.
InParanoidiQ9R1I1.
KOiK04746.
OrthoDBiEOG7RZ5S0.
PhylomeDBiQ9R1I1.
TreeFamiTF342871.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9R1I1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMLLKKGRLL MFLGSQVIVV ALFIHMSVHR HLSQREESRR PVHVLVLSSW
60 70 80 90 100
RSGSSFVGQL FGQHPDVFYL MEPAWHVWMT FTSSTAWKLH MAVRDLLRSV
110 120 130 140 150
FLCDMSVFDA YMNPGPRKQS SLFQWEQSRA LCSAPVCDFF PAHEISSPKH
160 170 180 190 200
CKLLCGQQPF DMVEKACRSH GFVVLKEVRF LSLQALYPLL TDPSLNLHVV
210 220 230 240 250
HLVRDPRAVF RSREHTTIEL VVDSHIVLGQ HLETIKEEDQ PYYAMKIICK
260 270 280 290 300
SQVDIVKAIQ TLPEALQQRY LFLRYEDLVR APLAQTTRLY KFVGLDFLPH
310 320 330 340 350
LQTWVHNVTR GKGMGQHAFH TNARNALNVS QAWRWSLPYE KVSQLQDACG
360 370 380
EAMDLLGYLQ VRSQQEQGNL SLDLLSSSHI LGQVFREG
Length:388
Mass (Da):44,636
Last modified:May 1, 2000 - v1
Checksum:i6D5371AFB6884AEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti221 – 2211V → M(PubMed:10330415)Curated
Sequence conflicti221 – 2211V → M(PubMed:16141072)Curated
Sequence conflicti306 – 3061H → Y(PubMed:10330415)Curated
Sequence conflicti306 – 3061H → Y(PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF109155 mRNA. Translation: AAD45579.1.
AF131236 Genomic DNA. Translation: AAD33016.1.
AK009113 mRNA. Translation: BAB26078.1.
BC057886 mRNA. Translation: AAH57886.1.
CCDSiCCDS22659.1.
RefSeqiNP_036128.3. NM_011998.4.
XP_006531106.1. XM_006531043.1.
XP_006531107.1. XM_006531044.1.
XP_006531108.1. XM_006531045.1.
UniGeneiMm.89207.

Genome annotation databases

EnsembliENSMUST00000109222; ENSMUSP00000104845; ENSMUSG00000035930.
GeneIDi26887.
KEGGimmu:26887.
UCSCiuc009njt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF109155 mRNA. Translation: AAD45579.1 .
AF131236 Genomic DNA. Translation: AAD33016.1 .
AK009113 mRNA. Translation: BAB26078.1 .
BC057886 mRNA. Translation: AAH57886.1 .
CCDSi CCDS22659.1.
RefSeqi NP_036128.3. NM_011998.4.
XP_006531106.1. XM_006531043.1.
XP_006531107.1. XM_006531044.1.
XP_006531108.1. XM_006531045.1.
UniGenei Mm.89207.

3D structure databases

ProteinModelPortali Q9R1I1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000104845.

PTM databases

PhosphoSitei Q9R1I1.

Proteomic databases

PRIDEi Q9R1I1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000109222 ; ENSMUSP00000104845 ; ENSMUSG00000035930 .
GeneIDi 26887.
KEGGi mmu:26887.
UCSCi uc009njt.2. mouse.

Organism-specific databases

CTDi 10164.
MGIi MGI:1349479. Chst4.

Phylogenomic databases

eggNOGi NOG80862.
GeneTreei ENSGT00530000062902.
HOGENOMi HOG000261614.
HOVERGENi HBG050949.
InParanoidi Q9R1I1.
KOi K04746.
OrthoDBi EOG7RZ5S0.
PhylomeDBi Q9R1I1.
TreeFami TF342871.

Miscellaneous databases

NextBioi 304707.
PROi Q9R1I1.
SOURCEi Search...

Gene expression databases

Bgeei Q9R1I1.
Genevestigatori Q9R1I1.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view ]
Pfami PF00685. Sulfotransfer_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMi SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCHST4_MOUSE
AccessioniPrimary (citable) accession number: Q9R1I1
Secondary accession number(s): Q9WUE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3