ID GALNS_RAT Reviewed; 524 AA.
AC Q32KJ6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP PROTEIN SEQUENCE OF 85-91, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP IDENTIFICATION.
RX PubMed=16174644; DOI=10.1093/hmg/ddi351;
RA Sardiello M., Annunziata I., Roma G., Ballabio A.;
RT "Sulfatases and sulfatase modifying factors: an exclusive and promiscuous
RT relationship.";
RL Hum. Mol. Genet. 14:3203-3217(2005).
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 -!- 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; AC134009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000741; CAI84987.1; -; mRNA.
DR RefSeq; NP_001041316.1; NM_001047851.1.
DR AlphaFoldDB; Q32KJ6; -.
DR SMR; Q32KJ6; -.
DR STRING; 10116.ENSRNOP00000019528; -.
DR GlyCosmos; Q32KJ6; 2 sites, No reported glycans.
DR GlyGen; Q32KJ6; 2 sites.
DR PhosphoSitePlus; Q32KJ6; -.
DR PaxDb; 10116-ENSRNOP00000019528; -.
DR Ensembl; ENSRNOT00000019528.5; ENSRNOP00000019528.3; ENSRNOG00000014461.8.
DR Ensembl; ENSRNOT00055035087; ENSRNOP00055028445; ENSRNOG00055020552.
DR Ensembl; ENSRNOT00060028827; ENSRNOP00060023199; ENSRNOG00060016854.
DR Ensembl; ENSRNOT00065030604; ENSRNOP00065024342; ENSRNOG00065018257.
DR GeneID; 292073; -.
DR KEGG; rno:292073; -.
DR UCSC; RGD:1565391; rat.
DR AGR; RGD:1565391; -.
DR CTD; 2588; -.
DR RGD; 1565391; Galns.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000157787; -.
DR HOGENOM; CLU_006332_13_5_1; -.
DR InParanoid; Q32KJ6; -.
DR OMA; YWEFHEG; -.
DR OrthoDB; 2913702at2759; -.
DR PhylomeDB; Q32KJ6; -.
DR TreeFam; TF314186; -.
DR Reactome; R-RNO-2022857; Keratan sulfate degradation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q32KJ6; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000014461; Expressed in skeletal muscle tissue and 18 other cell types or tissues.
DR ExpressionAtlas; Q32KJ6; baseline and differential.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; ISO:RGD.
DR CDD; cd16157; GALNS; 1.
DR Gene3D; 3.30.1120.10; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035626; GALNS.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR42693; ARYLSULFATASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42693:SF50; N-ACETYLGALACTOSAMINE-6-SULFATASE; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR Pfam; PF14707; Sulfatase_C; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lysosome; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..524
FT /note="N-acetylgalactosamine-6-sulfatase"
FT /id="PRO_0000273150"
FT REGION 28..381
FT /note="Catalytic domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 143
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 80
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..421
FT /evidence="ECO:0000250"
FT DISULFID 491..520
FT /evidence="ECO:0000250"
FT DISULFID 503..509
FT /evidence="ECO:0000250"
SQ SEQUENCE 524 AA; 58302 MW; A089BA7083017AF5 CRC64;
MTACSTAIRA QQLLLPVLSA LGLLAAGAPQ PPNIVLLLMD DMGWGDLGVY GEPSRETPNL
DRMAAEGMLF PSFYSANPLC SPSRAALLTG RLPIRNGFYT TNAHARNAYT PQEIMGGIPN
SEHLLPELLK KAGYTNKIVG KWHLGHRPQF HPLKHGFDEW FGSPNCHFGP YDNKVKPNIP
VYRDWEMVGR FYEEFPINLK TGEANLTQLY LQEALDFIRT QHARQSPFFL YWAIDATHAP
VYASKQFLGT SLRGRYGDAV REIDDSVGKI LSLLQNLGIS KNTFVFFTSD NGAALISAPK
EGGSNGPFLC GKQTTFEGGM REPAIAWWPG HIAAGQVSHQ LGSIMDLFTT SLSLAGLKPP
SDRVIDGLDL LPTMLQGHII DRPIFYYRGN TLMAVTLGQY KAHLWTWTNS WEEFRQGIDF
CPGQNVSGVT THTQEEHTEL PLIFHLGRDP GERFPLRFTS NEYQDALSRT TQVIQQHQKS
LVPGQPQLNV CNQAVMNWAP PGCEKLGKCL TPPESVPEKC FWAH
//
