GALNS_MOUSE
ID GALNS_MOUSE Reviewed; 520 AA.
AC Q571E4; Q3TWQ4; Q99KU8; Q9JHK9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=N-acetylgalactosamine-6-sulfatase;
DE EC=3.1.6.4;
DE AltName: Full=Chondroitinsulfatase;
DE Short=Chondroitinase;
DE AltName: Full=Galactose-6-sulfate sulfatase;
DE AltName: Full=N-acetylgalactosamine-6-sulfate sulfatase;
DE Short=GalNAc6S sulfatase;
DE Flags: Precursor;
GN Name=Galns;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ, and C57BL/6J;
RX PubMed=10699374; DOI=10.1016/s0925-4439(99)00119-2;
RA Montano A.M., Yamagishi A., Tomatsu S., Fukuda S., Copeland N.G.,
RA Orii K.E., Isogai K., Yamada N., Kato Z.I., Jenkins N.A., Gilbert D.J.,
RA Sukegawa K., Orii T., Kondo N.;
RT "The mouse N-acetylgalactosamine-6-sulfate sulfatase (Galns) gene: cDNA
RT isolation, genomic characterization, chromosomal assignment and analysis of
RT the 5'-flanking region.";
RL Biochim. Biophys. Acta 1500:323-334(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 6-sulfate groups of the N-acetyl-D-
CC galactosamine 6-sulfate units of chondroitin sulfate and of the D-
CC galactose 6-sulfate units of keratan sulfate.; EC=3.1.6.4;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Higher expression in liver and
CC kidney. {ECO:0000269|PubMed:10699374}.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF111346; AAF63155.1; -; mRNA.
DR EMBL; AF112242; AAF63858.1; -; Genomic_DNA.
DR EMBL; AF112230; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112231; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112233; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112232; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112234; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112235; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112236; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112237; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112238; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112239; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112240; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AF112241; AAF63858.1; JOINED; Genomic_DNA.
DR EMBL; AK220245; BAD90170.1; ALT_INIT; mRNA.
DR EMBL; AK159592; BAE35212.1; -; mRNA.
DR EMBL; BC004002; AAH04002.1; -; mRNA.
DR CCDS; CCDS40504.1; -.
DR RefSeq; NP_001180574.1; NM_001193645.1.
DR RefSeq; NP_057931.3; NM_016722.4.
DR AlphaFoldDB; Q571E4; -.
DR SMR; Q571E4; -.
DR BioGRID; 206156; 2.
DR STRING; 10090.ENSMUSP00000015171; -.
DR GlyConnect; 2525; 3 N-Linked glycans (2 sites).
DR GlyGen; Q571E4; 2 sites, 3 N-linked glycans (2 sites).
DR PhosphoSitePlus; Q571E4; -.
DR EPD; Q571E4; -.
DR jPOST; Q571E4; -.
DR MaxQB; Q571E4; -.
DR PaxDb; Q571E4; -.
DR PeptideAtlas; Q571E4; -.
DR PRIDE; Q571E4; -.
DR ProteomicsDB; 273414; -.
DR Antibodypedia; 30794; 327 antibodies from 36 providers.
DR DNASU; 50917; -.
DR Ensembl; ENSMUST00000015171; ENSMUSP00000015171; ENSMUSG00000015027.
DR GeneID; 50917; -.
DR KEGG; mmu:50917; -.
DR UCSC; uc012gmh.1; mouse.
DR CTD; 2588; -.
DR MGI; MGI:1355303; Galns.
DR VEuPathDB; HostDB:ENSMUSG00000015027; -.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000157787; -.
DR HOGENOM; CLU_006332_13_5_1; -.
DR InParanoid; Q571E4; -.
DR OMA; IMHHMDW; -.
DR OrthoDB; 515367at2759; -.
DR PhylomeDB; Q571E4; -.
DR TreeFam; TF314186; -.
DR BRENDA; 3.1.6.4; 3474.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 50917; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Galns; mouse.
DR PRO; PR:Q571E4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q571E4; protein.
DR Bgee; ENSMUSG00000015027; Expressed in placenta labyrinth and 196 other tissues.
DR ExpressionAtlas; Q571E4; baseline and differential.
DR Genevisible; Q571E4; MM.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043890; F:N-acetylgalactosamine-6-sulfatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; ISO:MGI.
DR CDD; cd16157; GALNS; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035626; GALNS.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Metal-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..520
FT /note="N-acetylgalactosamine-6-sulfatase"
FT /id="PRO_0000273148"
FT REGION 24..377
FT /note="Catalytic domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 139
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 306..417
FT /evidence="ECO:0000250"
FT DISULFID 487..516
FT /evidence="ECO:0000250"
FT DISULFID 499..505
FT /evidence="ECO:0000250"
FT CONFLICT 22
FT /note="A -> V (in Ref. 4; AAH04002)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="D -> N (in Ref. 1; AAF63858/AAF63155)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="T -> L (in Ref. 4; AAH04002)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="Q -> R (in Ref. 4; AAH04002)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="S -> G (in Ref. 4; AAH04002)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="S -> N (in Ref. 4; AAH04002)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 57673 MW; 63428DFA8843A21D CRC64;
MAACTAAQQL LLVLSALGLL AAGAPQPPNI VLLLMDDMGW GDLGVNGEPS RETPNLDRMA
AEGMLFPSFY SANPLCSPSR AALLTGRLPI RNGFYTTNAH ARNAYTPQEI MGGIPNSEHL
LPELLKKAGY TNKIVGKWHL GHRPQFHPLK HGFDEWFGSP NCHFGPYDNK AKPNIPVYRD
WEMVGRFYEE FPINRKTGEA NLTQLYTQEA LDFIQTQHAR QSPFFLYWAI DATHAPVYAS
RQFLGTSLRG RYGDAVREID DSVGKILSLL QNLGISKNTF VFFTSDNGAA LISAPNEGGS
NGPFLCGKQT TFEGGMREPA IAWWPGHIAA GQVSHQLGSI MDLFTTSLSL AGLKPPSDRV
IDGLDLLPTM LKGQMMDRPI FYYRGNTLMA VTLGQYKAHL WTWTNSWEEF TQGTDFCPGQ
NVSGVTTHTQ EEHTELPLIF HLGRDPGERF PLSFHSDEYQ DALSRTTQVV QEHQKSLVPG
QPQLNVCNQA VMNWAPPGCE KLGKCLTPPE SVPEKCFWAH
