ID ARSB_FELCA Reviewed; 535 AA. AC P33727; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 27-MAR-2024, entry version 108. DE RecName: Full=Arylsulfatase B; DE Short=ASB; DE EC=3.1.6.12; DE AltName: Full=N-acetylgalactosamine-4-sulfatase; DE Short=G4S; DE Flags: Precursor; GN Name=ARSB; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis. OX NCBI_TaxID=9685; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=1427856; DOI=10.1016/s0888-7543(05)80233-2; RA Jackson C.E., Yuhki N., Desnick R.J., Haskins M.E., O'Brien S.J., RA Schuchman E.H.; RT "Feline arylsulfatase B (ARSB): isolation and expression of the cDNA, RT comparison with human ARSB, and gene localization to feline chromosome RT A1."; RL Genomics 14:403-411(1992). RN [2] RP DISEASE. RX PubMed=6794375; RA Haskins M.E., Jezyk P.F., Desnick R.J., Patterson D.F.; RT "Animal model of human disease: Mucopolysaccharidosis VI Maroteaux-Lamy RT syndrome, Arylsulfatase B-deficient mucopolysaccharidosis in the Siamese RT cat."; RL Am. J. Pathol. 105:191-193(1981). CC -!- FUNCTION: Removes sulfate groups from chondroitin-4-sulfate (C4S) and CC regulates its degradation (By similarity). Involved in the regulation CC of cell adhesion, cell migration and invasion in colonic epithelium (By CC similarity). In the central nervous system, is a regulator of neurite CC outgrowth and neuronal plasticity, acting through the control of CC sulfate glycosaminoglycans and neurocan levels (By similarity). CC {ECO:0000250|UniProtKB:P15848, ECO:0000250|UniProtKB:P50430}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of the 4-sulfate groups of the N-acetyl-D- CC galactosamine 4-sulfate units of chondroitin sulfate and dermatan CC sulfate.; EC=3.1.6.12; 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 -!- ACTIVITY REGULATION: Inhibited by ethanol (By similarity). CC {ECO:0000250|UniProtKB:P50430}. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Lysosome. Cell surface CC {ECO:0000250|UniProtKB:P50429}. 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 -!- DISEASE: Note=Defects in ARSB are the cause of mucopolysaccharidosis CC type VI (MPS-VI). MPS-VI has been described in Siamese cats CC (PubMed:6794375). {ECO:0000269|PubMed:6794375}. CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S48472; AAB23941.1; -; mRNA. DR PIR; A44475; A44475. DR RefSeq; NP_001135731.1; NM_001142259.1. DR AlphaFoldDB; P33727; -. DR SMR; P33727; -. DR STRING; 9685.ENSFCAP00000054046; -. DR GlyCosmos; P33727; 5 sites, No reported glycans. DR PaxDb; 9685-ENSFCAP00000021800; -. DR GeneID; 100216331; -. DR KEGG; fca:100216331; -. DR eggNOG; KOG3867; Eukaryota. DR InParanoid; P33727; -. DR OrthoDB; 2913702at2759; -. DR Proteomes; UP000011712; Unplaced. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003943; F:N-acetylgalactosamine-4-sulfatase activity; ISS:UniProtKB. DR GO; GO:0061580; P:colon epithelial cell migration; ISS:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB. DR GO; GO:0010632; P:regulation of epithelial cell migration; ISS:UniProtKB. DR CDD; cd16029; 4-S; 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; IPR047115; ARSB. DR InterPro; IPR024607; Sulfatase_CS. DR InterPro; IPR000917; Sulfatase_N. DR PANTHER; PTHR10342; ARYLSULFATASE; 1. DR PANTHER; PTHR10342:SF272; ARYLSULFATASE B; 1. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. DR PROSITE; PS00523; SULFATASE_1; 1. DR PROSITE; PS00149; SULFATASE_2; 1. PE 2: Evidence at transcript level; KW Calcium; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Metal-binding; KW Mucopolysaccharidosis; Reference proteome; Signal. FT SIGNAL 1..41 FT /evidence="ECO:0000255" FT CHAIN 42..535 FT /note="Arylsulfatase B" FT /id="PRO_0000033422" FT ACT_SITE 93 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P15289" FT ACT_SITE 149 FT /evidence="ECO:0000250|UniProtKB:P15289" FT BINDING 55 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 56 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 93 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /note="via 3-oxoalanine" FT /evidence="ECO:0000250" FT BINDING 147 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 244 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 302 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 303 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 320 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 93 FT /note="3-oxoalanine (Cys)" FT /evidence="ECO:0000250|UniProtKB:P15289" FT CARBOHYD 190 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 281 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 293 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 428 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 460 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 119..523 FT /evidence="ECO:0000250" FT DISULFID 123..157 FT /evidence="ECO:0000250" FT DISULFID 183..194 FT /evidence="ECO:0000250" FT DISULFID 407..449 FT /evidence="ECO:0000250" SQ SEQUENCE 535 AA; 59753 MW; 43A527886A9983C4 CRC64; MGRRGAASLP RGPSPRRPLL PGVLPLLLRL LLLPSRPGAG AGADRPPHLV FVLADDLGWN DVSFHGSNIR TPHLDELAAG GVLLDNYYTQ PLCTPSRSQL LTGRYQIHTG LQHQIIWPCQ PSCVPLDEKL LPQLLKEAGY TTHMVGKWHL GMYRKECLPT RRGFDTYFGY LLGSEDYYSH ERCALIDSLN VTRCALDFRD GEQVATGYKN MYSTNIFTER ATALITSHPP EKPLFLYLAL QSVHEPLQVP EEYLKPYDFI QDKNRHYYAG MVSLMDEAVG NVTAALKSHG LWNNTVFIFS TDNGGQTLAG GNNWPLRGRK WSLWEGGIRG VGFVASPLLK QKGVKNRELI HISDWLPTLV KLARGSTKGT KPLDGFDVWK TISEGSPSPR KELLHNIDPN FVDISPCPGK SLAPAKDDSS HPAYLAFNTS LHAAIRHGNW KLLTGYPGCG CWFPPPSPYN DSAIPSSDPP TKTLWPFDID QDPEERHDLS RDYPHIVEQL LSRLQFYHKH SVPVHFPAQD PRCDPKGTGA WGPWV //