ARSB_FELCA
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 03-AUG-2022, entry version 101.
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}.
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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.ENSFCAP00000021800; -.
DR GeneID; 100216331; -.
DR KEGG; fca:100216331; -.
DR CTD; 411; -.
DR eggNOG; KOG3867; Eukaryota.
DR InParanoid; P33727; -.
DR OrthoDB; 515367at2759; -.
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 Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
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.
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
