ID   GNS_MOUSE               Reviewed;         544 AA.
AC   Q8BFR4; Q3TWT0; Q8BJJ7; Q8BK91;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=N-acetylglucosamine-6-sulfatase;
DE            EC=3.1.6.14;
DE   AltName: Full=Glucosamine-6-sulfatase;
DE            Short=G6S;
DE   Flags: Precursor;
GN   Name=Gns;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Oviduct, and Thymus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, 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         glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.;
CC         EC=3.1.6.14;
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   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
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}.
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DR   EMBL; AK030773; BAC27129.1; -; mRNA.
DR   EMBL; AK049162; BAC33578.1; -; mRNA.
DR   EMBL; AK054046; BAC35632.1; -; mRNA.
DR   EMBL; AK083597; BAC38966.1; -; mRNA.
DR   EMBL; AK159562; BAE35186.1; -; mRNA.
DR   EMBL; AK169485; BAE41197.1; -; mRNA.
DR   EMBL; AK165180; BAE38063.1; -; mRNA.
DR   EMBL; AK170791; BAE42031.1; -; mRNA.
DR   EMBL; BC055328; AAH55328.1; -; mRNA.
DR   CCDS; CCDS24210.1; -.
DR   RefSeq; NP_083640.1; NM_029364.3.
DR   AlphaFoldDB; Q8BFR4; -.
DR   SMR; Q8BFR4; -.
DR   BioGRID; 217615; 31.
DR   STRING; 10090.ENSMUSP00000043167; -.
DR   GlyConnect; 2527; 6 N-Linked glycans (4 sites).
DR   GlyCosmos; Q8BFR4; 12 sites, 6 glycans.
DR   GlyGen; Q8BFR4; 13 sites, 6 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BFR4; -.
DR   PhosphoSitePlus; Q8BFR4; -.
DR   SwissPalm; Q8BFR4; -.
DR   EPD; Q8BFR4; -.
DR   jPOST; Q8BFR4; -.
DR   MaxQB; Q8BFR4; -.
DR   PaxDb; 10090-ENSMUSP00000043167; -.
DR   PeptideAtlas; Q8BFR4; -.
DR   ProteomicsDB; 267740; -.
DR   Pumba; Q8BFR4; -.
DR   Antibodypedia; 2462; 268 antibodies from 33 providers.
DR   DNASU; 75612; -.
DR   Ensembl; ENSMUST00000040344.7; ENSMUSP00000043167.7; ENSMUSG00000034707.8.
DR   GeneID; 75612; -.
DR   KEGG; mmu:75612; -.
DR   UCSC; uc007hfo.1; mouse.
DR   AGR; MGI:1922862; -.
DR   CTD; 2799; -.
DR   MGI; MGI:1922862; Gns.
DR   VEuPathDB; HostDB:ENSMUSG00000034707; -.
DR   eggNOG; KOG3731; Eukaryota.
DR   GeneTree; ENSGT00940000158420; -.
DR   HOGENOM; CLU_006332_4_1_1; -.
DR   InParanoid; Q8BFR4; -.
DR   OMA; WCHGEHE; -.
DR   OrthoDB; 1365192at2759; -.
DR   PhylomeDB; Q8BFR4; -.
DR   TreeFam; TF313545; -.
DR   Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR   Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 75612; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Gns; mouse.
DR   PRO; PR:Q8BFR4; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8BFR4; Protein.
DR   Bgee; ENSMUSG00000034707; Expressed in ciliary body and 264 other cell types or tissues.
DR   ExpressionAtlas; Q8BFR4; baseline and differential.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0005539; F:glycosaminoglycan binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; ISO:MGI.
DR   GO; GO:0043199; F:sulfate binding; ISO:MGI.
DR   GO; GO:0008484; F:sulfuric ester hydrolase activity; ISO:MGI.
DR   GO; GO:0042340; P:keratan sulfate catabolic process; ISO:MGI.
DR   CDD; cd16147; G6S; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR012251; GlcNAc_6-SO4ase.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR43108:SF5; N-ACETYLGLUCOSAMINE-6-SULFATASE; 1.
DR   PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   PIRSF; PIRSF036666; G6S; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
DR   PROSITE; PS00149; SULFATASE_2; 1.
DR   Genevisible; Q8BFR4; MM.
PE   1: Evidence at protein level;
KW   Calcium; Glycoprotein; Hydrolase; Lysosome; Metal-binding; Phosphoprotein;
KW   Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..544
FT                   /note="N-acetylglucosamine-6-sulfatase"
FT                   /id="PRO_0000273189"
FT   ACT_SITE        83
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         83
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   MOD_RES         533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15586"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        379
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        441
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        472
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        65
FT                   /note="L -> V (in Ref. 1; BAC35632)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="F -> L (in Ref. 1; BAE35186)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="F -> L (in Ref. 1; BAC38966)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   544 AA;  61175 MW;  F9E95AFA6CBEA842 CRC64;
     MRLPSAAGPR PGRPRRLPAL LLLPLLGGCL GLVGAARRPN VLLLLTDDQD AELGGMTPLK
     KTKALIGEKG MTFSSAYVPS ALCCPSRASI LTGKYPHNHH VVNNTLEGNC SSKAWQKIQE
     PYTFPAILKS VCGYQTFFAG KYLNEYGAPD AGGLEHIPLG WSYWYALEKN SKYYNYTLSI
     NGKARKHGEN YSVDYLTDVL ANLSLDFLDY KSNSEPFFMM ISTPAPHSPW TAAPQYQKAF
     QNVIAPRNKN FNIHGTNKHW LIRQAKTPMT NSSIRFLDDA FRRRWQTLLS VDDLVEKLVK
     RLDSTGELDN TYIFYTSDNG YHTGQFSLPI DKRQLYEFDI KVPLLVRGPG IKPNQTSKML
     VSNIDLGPTI LDLAGYDLNK TQMDGMSLLP ILKGDRNLTW RSDVLVEYQG EGRNVTDPTC
     PSLSPGVSQC FPDCVCEDAY NNTYACVRTL SSLWNLQYCE FDDQEVFVEV YNITADPDQI
     TNIAKSIDPE LLGKMNYRLM MLQSCSGPTC RTPGVFDPGY RFDLRLMFNS HGSVRTRRFS
     KHPL
//