ARSL_MACFA
ID ARSL_MACFA Reviewed; 588 AA.
AC Q60HH5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Arylsulfatase L;
DE EC=3.1.6.1 {ECO:0000250|UniProtKB:P51690};
DE AltName: Full=Arylsulfatase E;
DE Short=ASE;
DE Flags: Precursor;
GN Name=ARSL; Synonyms=ARSE; ORFNames=QtrA-14484;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exhibits arylsulfatase activity towards the artificial
CC substrate 4-methylumbelliferyl sulfate (By similarity). May be
CC essential for the correct composition of cartilage and bone matrix
CC during development (By similarity). Has no activity toward steroid
CC sulfates (By similarity). {ECO:0000250|UniProtKB:P51690}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aryl sulfate + H2O = a phenol + H(+) + sulfate;
CC Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317; EC=3.1.6.1;
CC Evidence={ECO:0000250|UniProtKB:P51690};
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 -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack
CC {ECO:0000250|UniProtKB:P51690}.
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|UniProtKB:P15289}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; AB125152; BAD51940.1; -; mRNA.
DR RefSeq; NP_001270146.1; NM_001283217.1.
DR AlphaFoldDB; Q60HH5; -.
DR SMR; Q60HH5; -.
DR STRING; 9541.XP_005592946.1; -.
DR PRIDE; Q60HH5; -.
DR GeneID; 102138132; -.
DR CTD; 415; -.
DR eggNOG; KOG3867; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0004065; F:arylsulfatase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; 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; Glycoprotein; Golgi apparatus; Hydrolase; Metal-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..588
FT /note="Arylsulfatase L"
FT /id="PRO_0000033426"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 147
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 86
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 588 AA; 65480 MW; 3457C6286AA7CA19 CRC64;
MLHLHHSWLC FRSWLAGMLS VLLGLVPSAS SNISTSRPNI LLLMADDLGI GDIGCYGNNT
MRTPNIDRLA EDGVKLTQHI SAASLCTPSR AAFLTGRYPV RSGMVSSIGY RVLQWTGASG
GLPTNETTFA KILKEKGYAT GLIGKWHLGL NCESASDHCH HPLHHGFDHF YGMPFSLMGD
CAHWELSEKR VNLEQKLNFL FQVLALVALT LVAGKLTHLI PVSWTPVIWS ALWAVLLLTG
SYFVGALIVH AGCLLMRNHT ITEQPMRFQK TTPLILQEVA SFLKRNKHGP FLLFVSFLHV
HIPLITMENF LGKSLHGLYG DNVEEMDWMV GQILDTLDME GLTNSTLIYF TSDHGGSLEN
QLGRTQYGGW NGIYKGGKGM GGWEGGIRVP GIFRWPGVLP AGQVIGEPTS LMDVFPTVVQ
LAGGEVPQDR VIDGQDLLPL LLGTAQHSDH EFLMHYCEGF LHAARWHQRD RTTWKVHFVT
PVFQPEGAGA CYGRKVCPCF GEKVLHHDPP LLFDLSRDPS ETHVLTPASE PVFYQVMERV
QRAVREHQRT LSPVPLQLDR LGNIWRPWLQ PSCGPFPLCW CLREDGPQ
