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Q571E4

- GALNS_MOUSE

UniProt

Q571E4 - GALNS_MOUSE

Protein

N-acetylgalactosamine-6-sulfatase

Gene

Galns

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    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.

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi36 – 361CalciumBy similarity
    Metal bindingi37 – 371CalciumBy similarity
    Metal bindingi76 – 761Calcium; via 3-oxoalanineBy similarity
    Metal bindingi286 – 2861CalciumBy similarity
    Metal bindingi287 – 2871CalciumBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. N-acetylgalactosamine-6-sulfatase activity Source: UniProtKB-EC
    3. sulfuric ester hydrolase activity Source: MGI

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.6.4. 3474.
    ReactomeiREACT_198960. Keratan sulfate degradation.

    Names & Taxonomyi

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

    Organism-specific databases

    MGIiMGI:1355303. Galns.

    Subcellular locationi

    Lysosome By similarity

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323By similarityAdd
    BLAST
    Chaini24 – 520497N-acetylgalactosamine-6-sulfatasePRO_0000273148Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 7613-oxoalanine (Cys)By similarity
    Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi306 ↔ 417By similarity
    Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi487 ↔ 516By similarity
    Disulfide bondi499 ↔ 505By similarity

    Post-translational modificationi

    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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ571E4.
    PaxDbiQ571E4.
    PRIDEiQ571E4.

    PTM databases

    PhosphoSiteiQ571E4.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiQ571E4.
    CleanExiMM_GALNS.
    GenevestigatoriQ571E4.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ571E4.
    SMRiQ571E4. Positions 25-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 377354Catalytic domainBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the sulfatase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3119.
    GeneTreeiENSGT00560000076940.
    HOGENOMiHOG000135352.
    HOVERGENiHBG004283.
    InParanoidiQ571E4.
    KOiK01132.
    OMAiLTQVYLQ.
    OrthoDBiEOG7QZG9J.
    PhylomeDBiQ571E4.
    TreeFamiTF314186.

    Family and domain databases

    Gene3Di3.40.720.10. 1 hit.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR000917. Sulfatase.
    IPR024607. Sulfatase_CS.
    [Graphical view]
    PfamiPF00884. Sulfatase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53649. SSF53649. 1 hit.
    PROSITEiPS00523. SULFATASE_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q571E4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAACTAAQQL LLVLSALGLL AAGAPQPPNI VLLLMDDMGW GDLGVNGEPS    50
    RETPNLDRMA AEGMLFPSFY SANPLCSPSR AALLTGRLPI RNGFYTTNAH 100
    ARNAYTPQEI MGGIPNSEHL LPELLKKAGY TNKIVGKWHL GHRPQFHPLK 150
    HGFDEWFGSP NCHFGPYDNK AKPNIPVYRD WEMVGRFYEE FPINRKTGEA 200
    NLTQLYTQEA LDFIQTQHAR QSPFFLYWAI DATHAPVYAS RQFLGTSLRG 250
    RYGDAVREID DSVGKILSLL QNLGISKNTF VFFTSDNGAA LISAPNEGGS 300
    NGPFLCGKQT TFEGGMREPA IAWWPGHIAA GQVSHQLGSI MDLFTTSLSL 350
    AGLKPPSDRV IDGLDLLPTM LKGQMMDRPI FYYRGNTLMA VTLGQYKAHL 400
    WTWTNSWEEF TQGTDFCPGQ NVSGVTTHTQ EEHTELPLIF HLGRDPGERF 450
    PLSFHSDEYQ DALSRTTQVV QEHQKSLVPG QPQLNVCNQA VMNWAPPGCE 500
    KLGKCLTPPE SVPEKCFWAH 520
    Length:520
    Mass (Da):57,673
    Last modified:January 23, 2007 - v2
    Checksum:i63428DFA8843A21D
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221A → V in AAH04002. (PubMed:15489334)Curated
    Sequence conflicti154 – 1541D → N in AAF63858. (PubMed:10699374)Curated
    Sequence conflicti154 – 1541D → N in AAF63155. (PubMed:10699374)Curated
    Sequence conflicti207 – 2071T → L in AAH04002. (PubMed:15489334)Curated
    Sequence conflicti215 – 2151Q → R in AAH04002. (PubMed:15489334)Curated
    Sequence conflicti222 – 2221S → G in AAH04002. (PubMed:15489334)Curated
    Sequence conflicti268 – 2681S → N in AAH04002. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF111346 mRNA. Translation: AAF63155.1.
    AF112242
    , 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.
    CCDSiCCDS40504.1.
    RefSeqiNP_001180574.1. NM_001193645.1.
    NP_057931.3. NM_016722.4.
    UniGeneiMm.34702.

    Genome annotation databases

    EnsembliENSMUST00000015171; ENSMUSP00000015171; ENSMUSG00000015027.
    GeneIDi50917.
    KEGGimmu:50917.
    UCSCiuc012gmh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF111346 mRNA. Translation: AAF63155.1 .
    AF112242
    , 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 .
    CCDSi CCDS40504.1.
    RefSeqi NP_001180574.1. NM_001193645.1.
    NP_057931.3. NM_016722.4.
    UniGenei Mm.34702.

    3D structure databases

    ProteinModelPortali Q571E4.
    SMRi Q571E4. Positions 25-518.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q571E4.

    Proteomic databases

    MaxQBi Q571E4.
    PaxDbi Q571E4.
    PRIDEi Q571E4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000015171 ; ENSMUSP00000015171 ; ENSMUSG00000015027 .
    GeneIDi 50917.
    KEGGi mmu:50917.
    UCSCi uc012gmh.1. mouse.

    Organism-specific databases

    CTDi 2588.
    MGIi MGI:1355303. Galns.

    Phylogenomic databases

    eggNOGi COG3119.
    GeneTreei ENSGT00560000076940.
    HOGENOMi HOG000135352.
    HOVERGENi HBG004283.
    InParanoidi Q571E4.
    KOi K01132.
    OMAi LTQVYLQ.
    OrthoDBi EOG7QZG9J.
    PhylomeDBi Q571E4.
    TreeFami TF314186.

    Enzyme and pathway databases

    BRENDAi 3.1.6.4. 3474.
    Reactomei REACT_198960. Keratan sulfate degradation.

    Miscellaneous databases

    NextBioi 307919.
    PROi Q571E4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q571E4.
    CleanExi MM_GALNS.
    Genevestigatori Q571E4.

    Family and domain databases

    Gene3Di 3.40.720.10. 1 hit.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR000917. Sulfatase.
    IPR024607. Sulfatase_CS.
    [Graphical view ]
    Pfami PF00884. Sulfatase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 1 hit.
    PROSITEi PS00523. SULFATASE_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiGALNS_MOUSE
    AccessioniPrimary (citable) accession number: Q571E4
    Secondary accession number(s): Q3TWQ4, Q99KU8, Q9JHK9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 72 of the entry and version 2 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