ARSA_BOVIN
ID ARSA_BOVIN Reviewed; 507 AA.
AC Q08DD1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Arylsulfatase A;
DE Short=ASA;
DE EC=3.1.6.8 {ECO:0000250|UniProtKB:P15289};
DE AltName: Full=Cerebroside-sulfatase;
DE Flags: Precursor;
GN Name=ARSA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes cerebroside sulfate.
CC {ECO:0000250|UniProtKB:P15289}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine =
CC a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H(+) + sulfate;
CC Xref=Rhea:RHEA:21300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:18390, ChEBI:CHEBI:75956; EC=3.1.6.8;
CC Evidence={ECO:0000250|UniProtKB:P15289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21301;
CC Evidence={ECO:0000250|UniProtKB:P15289};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P15289};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15289};
CC -!- SUBUNIT: Homodimer at neutral pH and homooctamer at acidic pH. Exists
CC both as a single chain of 58 kDa (component A) or as a chain of 50 kDa
CC (component B) linked by disulfide bond(s) to a 7 kDa chain (component
CC C). Interacts with SUMF1 (By similarity).
CC {ECO:0000250|UniProtKB:P15289}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P15289}. Lysosome
CC {ECO:0000250|UniProtKB:P15289}.
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. This post-
CC translational modification is severely defective in multiple sulfatase
CC deficiency (MSD). {ECO:0000250|UniProtKB:P15289}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; BC123816; AAI23817.1; -; mRNA.
DR RefSeq; NP_001068673.1; NM_001075205.1.
DR RefSeq; XP_005207557.1; XM_005207500.3.
DR AlphaFoldDB; Q08DD1; -.
DR SMR; Q08DD1; -.
DR STRING; 9913.ENSBTAP00000021364; -.
DR PaxDb; Q08DD1; -.
DR PRIDE; Q08DD1; -.
DR Ensembl; ENSBTAT00000021364; ENSBTAP00000021364; ENSBTAG00000016053.
DR GeneID; 505514; -.
DR KEGG; bta:505514; -.
DR CTD; 410; -.
DR VEuPathDB; HostDB:ENSBTAG00000016053; -.
DR VGNC; VGNC:50217; ARSA.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000157610; -.
DR HOGENOM; CLU_006332_13_7_1; -.
DR InParanoid; Q08DD1; -.
DR OMA; PALEPCC; -.
DR OrthoDB; 515367at2759; -.
DR TreeFam; TF314186; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000016053; Expressed in pigment epithelium of eye and 104 other tissues.
DR ExpressionAtlas; Q08DD1; baseline.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004098; F:cerebroside-sulfatase activity; IEA:UniProtKB-EC.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid metabolism; Lysosome; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CHAIN 19..507
FT /note="Arylsulfatase A"
FT /id="PRO_0000273636"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 125
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 69
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 156..172
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT DISULFID 161..168
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT DISULFID 300..414
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT DISULFID 488..500
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT DISULFID 489..502
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT DISULFID 493..499
FT /evidence="ECO:0000250|UniProtKB:P15289"
SQ SEQUENCE 507 AA; 53807 MW; CFE35552A9A4992A CRC64;
MEALWTLTLA LAAGLAAASP PNILLIFADD LGYGDLGSYG HPSSTTPNLD QLAAGGLRFT
DFYVPVSLCT PSRAALLTGR LPVRMGLYPG VLEPSSRGGL PLDEVTLAEV LAAQGYLTGI
AGKWHLGVGP EGAFLPPHHG FHRFLGIPYS HDQGPCQNLT CFPPATPCEG ICDQGLVPIP
LLANLSVEAQ PPWLPGLEAR YVAFARDLMT DAQHQGRPFF LYYASHHTHY PQFSGQSFPG
HSGRGPFGDS LMELDAAVGA LMTAVGDLGL LGETLVFFTA DNGPETMRMS HGGCSGLLRC
GKGTTFEGGV REPALAFWPG HIAPGVTHEL ASSLDLLPTL AALAGAQLPN ITLDGVDLSP
LLLGTGKSPR HTLFFYSAYP DEVRGVFAVR SGKYKAHFFT QGSVHSDTTA DPACHASNPL
TAHEPPLLFD LSEDPGENYN LLDSVDEVAP EALQAVKQLE LLKAQFDAAM TFGPSQMAQG
EDPTLQVCCQ PSCTPRPSCC HCPEFQP
