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 Genevisible; Q8BFR4; MM.
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.
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
//
