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Q9EP78 (CHST7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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 7

EC=2.8.2.-
EC=2.8.2.17
Alternative name(s):
Chondroitin 6-sulfotransferase 2
Short name=C6ST-2
Short name=mC6ST-2
Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 5
Short name=GST-5
N-acetylglucosamine 6-O-sulfotransferase 4
Short name=GlcNAc6ST-4
Short name=Gn6st-4
Gene names
Name:Chst7
Synonyms:Gst5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length484 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. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc. Ref.1

Catalytic activity

3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Widely expressed. Highly expressed in kidney. Expressed at lower level in heart, lung and liver. Ref.1

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Carbohydrate sulfotransferase 7
PRO_0000085199

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain34 – 484451Lumenal Potential
Nucleotide binding108 – 1147PAPS By similarity
Nucleotide binding276 – 2849PAPS By similarity

Amino acid modifications

Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation4051N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict101E → K in BAB40372. Ref.3
Sequence conflict1301E → D in BAB40372. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9EP78 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9B195537D7AB7193

FASTA48454,767
        10         20         30         40         50         60 
MKGRRRRRRE YCKFTLLLAL YTLLLLLVPS VLDSHSEQDK GRNCPGLQRS LGVWSLEAAA 

        70         80         90        100        110        120 
AGEREQGAEV RSLAEGNPDR SPGSPGNLSA VGEAVTQEKQ HIYVHATWRT GSSFLGELFN 

       130        140        150        160        170        180 
QHPDVFYLYE PMWHLWQALY PGDAESLQGA LRDMLRSLFR CDFSVLRLYA QPGDPGERAP 

       190        200        210        220        230        240 
DSANLTTAML FRWRTNKVIC SPPLCPAAPR ARADVGLVED KACESTCPPV SLRALEAECR 

       250        260        270        280        290        300 
KYPVVVIKDV RLLDLGVLVP LLRDPGLNLK VVQLFRDPRA VHNSRLKSRQ GLLRESIQVL 

       310        320        330        340        350        360 
RTRQRGDHFH RVLLAHGVDA RPGGQARALP SAPRADFFLT SALEVICEAW LRDLLFTRGA 

       370        380        390        400        410        420 
PAWLRRRYLR LRYEDLVWQP QAQLRRLLRF SGLRTLAALD AFAFNMTRGS AYGADRPFHL 

       430        440        450        460        470        480 
SARDAREAVH AWRERLSQEQ VRQVETACAP AMRLLAYPRS GDERDRKTVR EGETPLETKA 


NWAV 

« Hide

References

« Hide 'large scale' references
[1]"Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning of a novel enzyme with different distribution and specificities."
Uchimura K., Fasakhany F., Kadomatsu K., Matsukawa T., Yamakawa T., Kurosawa N., Muramatsu T.
Biochem. Biophys. Res. Commun. 274:291-296(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-5)."
Bhakta S., Bartes A., Bowman K.G., Kao W.-M., Polsky I., Lee J.-K., Cook B.N., Bruehl R.E., Rosen S.D., Bertozzi C.R., Hemmerich S.
J. Biol. Chem. 275:40226-40234(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/6.
[3]"Cloning and expression of mouse chondroitin 6-sulfotransferase-2."
Kitagawa H., Uyama T., Sugahara K.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[4]"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.
[5]"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: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB040710 mRNA. Translation: BAB13769.1.
AF280089 Genomic DNA. Translation: AAG48247.1.
AB046929 mRNA. Translation: BAB40372.1.
AK011202 mRNA. Translation: BAB27465.1.
BC019204 mRNA. Translation: AAH19204.1.
CCDSCCDS30040.1.
PIRJC7350.
RefSeqNP_068361.1. NM_021715.1.
UniGeneMm.44827.

3D structure databases

ProteinModelPortalQ9EP78.
SMRQ9EP78. Positions 99-137, 365-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000043222.

PTM databases

PhosphoSiteQ9EP78.

Proteomic databases

PRIDEQ9EP78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044138; ENSMUSP00000043222; ENSMUSG00000037347.
GeneID60322.
KEGGmmu:60322.
UCSCuc009sss.1. mouse.

Organism-specific databases

CTD56548.
MGIMGI:1891767. Chst7.

Phylogenomic databases

eggNOGNOG71363.
GeneTreeENSGT00530000062902.
HOGENOMHOG000261614.
HOVERGENHBG050949.
InParanoidQ9EP78.
KOK04743.
OMADKGAGHC.
OrthoDBEOG7RZ5S0.
PhylomeDBQ9EP78.
TreeFamTF342871.

Enzyme and pathway databases

BRENDA2.8.2.17. 3474.

Gene expression databases

BgeeQ9EP78.
GenevestigatorQ9EP78.

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. 3 hits.
ProtoNetSearch...

Other

NextBio314817.
PROQ9EP78.
SOURCESearch...

Entry information

Entry nameCHST7_MOUSE
AccessionPrimary (citable) accession number: Q9EP78
Secondary accession number(s): Q99NB0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 1, 2001
Last modified: July 9, 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