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Q571E4 (GALNS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. 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:
N-acetylgalactosamine-6-sulfatase

EC=3.1.6.4
Alternative name(s):
Chondroitinsulfatase
Short name=Chondroitinase
Galactose-6-sulfate sulfatase
N-acetylgalactosamine-6-sulfate sulfatase
Short name=GalNAc6S sulfatase
Gene names
Name:Galns
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Lysosome By similarity.

Tissue specificity

Widely expressed. Higher expression in liver and kidney. Ref.1

Post-translational modification

The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity By similarity.

Sequence similarities

Belongs to the sulfatase family.

Sequence caution

The sequence BAD90170.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylgalactosamine-6-sulfatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sulfuric ester hydrolase activity

Inferred from sequence orthology PubMed 15962010. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 By similarity
Chain24 – 520497N-acetylgalactosamine-6-sulfatase
PRO_0000273148

Regions

Region24 – 377354Catalytic domain By similarity

Sites

Metal binding361Calcium By similarity
Metal binding371Calcium By similarity
Metal binding761Calcium; via 3-oxoalanine By similarity
Metal binding2861Calcium By similarity
Metal binding2871Calcium By similarity

Amino acid modifications

Modified residue7613-oxoalanine (Cys) By similarity
Glycosylation2011N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Disulfide bond306 ↔ 417 By similarity
Disulfide bond487 ↔ 516 By similarity
Disulfide bond499 ↔ 505 By similarity

Experimental info

Sequence conflict221A → V in AAH04002. Ref.4
Sequence conflict1541D → N in AAF63858. Ref.1
Sequence conflict1541D → N in AAF63155. Ref.1
Sequence conflict2071T → L in AAH04002. Ref.4
Sequence conflict2151Q → R in AAH04002. Ref.4
Sequence conflict2221S → G in AAH04002. Ref.4
Sequence conflict2681S → N in AAH04002. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q571E4 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 63428DFA8843A21D

FASTA52057,673
        10         20         30         40         50         60 
MAACTAAQQL LLVLSALGLL AAGAPQPPNI VLLLMDDMGW GDLGVNGEPS RETPNLDRMA 

        70         80         90        100        110        120 
AEGMLFPSFY SANPLCSPSR AALLTGRLPI RNGFYTTNAH ARNAYTPQEI MGGIPNSEHL 

       130        140        150        160        170        180 
LPELLKKAGY TNKIVGKWHL GHRPQFHPLK HGFDEWFGSP NCHFGPYDNK AKPNIPVYRD 

       190        200        210        220        230        240 
WEMVGRFYEE FPINRKTGEA NLTQLYTQEA LDFIQTQHAR QSPFFLYWAI DATHAPVYAS 

       250        260        270        280        290        300 
RQFLGTSLRG RYGDAVREID DSVGKILSLL QNLGISKNTF VFFTSDNGAA LISAPNEGGS 

       310        320        330        340        350        360 
NGPFLCGKQT TFEGGMREPA IAWWPGHIAA GQVSHQLGSI MDLFTTSLSL AGLKPPSDRV 

       370        380        390        400        410        420 
IDGLDLLPTM LKGQMMDRPI FYYRGNTLMA VTLGQYKAHL WTWTNSWEEF TQGTDFCPGQ 

       430        440        450        460        470        480 
NVSGVTTHTQ EEHTELPLIF HLGRDPGERF PLSFHSDEYQ DALSRTTQVV QEHQKSLVPG 

       490        500        510        520 
QPQLNVCNQA VMNWAPPGCE KLGKCLTPPE SVPEKCFWAH 

« Hide

References

« Hide 'large scale' references
[1]"The mouse N-acetylgalactosamine-6-sulfate sulfatase (Galns) gene: cDNA isolation, genomic characterization, chromosomal assignment and analysis of the 5'-flanking region."
Montano A.M., Yamagishi A., Tomatsu S., Fukuda S., Copeland N.G., Orii K.E., Isogai K., Yamada N., Kato Z.I., Jenkins N.A., Gilbert D.J., Sukegawa K., Orii T., Kondo N.
Biochim. Biophys. Acta 1500:323-334(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
Strain: 129/SvJ and C57BL/6.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreatic islet.
[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.
[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: Czech II.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF111346 mRNA. Translation: AAF63155.1.
AF112242 expand/collapse EMBL AC list , AF112230, AF112231, AF112233, AF112232, AF112234, AF112235, AF112236, AF112237, AF112238, AF112239, AF112240, AF112241 Genomic DNA. Translation: AAF63858.1.
AK220245 mRNA. Translation: BAD90170.1. Different initiation.
AK159592 mRNA. Translation: BAE35212.1.
BC004002 mRNA. Translation: AAH04002.1.
RefSeqNP_001180574.1. NM_001193645.1.
NP_057931.3. NM_016722.4.
UniGeneMm.34702.

3D structure databases

ProteinModelPortalQ571E4.
SMRQ571E4. Positions 25-518.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ571E4.

Proteomic databases

PaxDbQ571E4.
PRIDEQ571E4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015171; ENSMUSP00000015171; ENSMUSG00000015027.
GeneID50917.
KEGGmmu:50917.
UCSCuc012gmh.1. mouse.

Organism-specific databases

CTD2588.
MGIMGI:1355303. Galns.

Phylogenomic databases

eggNOGCOG3119.
GeneTreeENSGT00560000076940.
HOGENOMHOG000135352.
HOVERGENHBG004283.
InParanoidQ571E4.
KOK01132.
OMASFYSANP.
OrthoDBEOG7QZG9J.
PhylomeDBQ571E4.
TreeFamTF314186.

Enzyme and pathway databases

BRENDA3.1.6.4. 3474.

Gene expression databases

BgeeQ571E4.
CleanExMM_GALNS.
GenevestigatorQ571E4.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00523. SULFATASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio307919.
PROQ571E4.
SOURCESearch...

Entry information

Entry nameGALNS_MOUSE
AccessionPrimary (citable) accession number: Q571E4
Secondary accession number(s): Q3TWQ4, Q99KU8, Q9JHK9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 68 of the entry and version 2 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