ID   ARS_STRPU               Reviewed;         567 AA.
AC   P50473;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Arylsulfatase;
DE            Short=AS;
DE            EC=3.1.6.1;
DE   AltName: Full=Aryl-sulfate sulphohydrolase;
DE            Short=ARS;
DE   Flags: Precursor;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2767335; DOI=10.1016/0012-1606(89)90157-7;
RA   Yang Q., Angerer L.M., Angerer R.C.;
RT   "Structure and tissue-specific developmental expression of a sea urchin
RT   arylsulfatase gene.";
RL   Dev. Biol. 135:53-65(1989).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expression is confined to aboral ectoderm cells and
CC       their precursors.
CC   -!- DEVELOPMENTAL STAGE: Low levels are found at mesenchyme blastula stage
CC       (24 hours), levels increase by late gastrula stage and are maintained
CC       at pluteus stage.
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; M28404; AAA30036.1; -; mRNA.
DR   PIR; A37362; A37362.
DR   RefSeq; NP_999677.1; NM_214512.1.
DR   AlphaFoldDB; P50473; -.
DR   SMR; P50473; -.
DR   STRING; 7668.SPU_023353-tr; -.
DR   EnsemblMetazoa; NM_214512; NP_999677; GeneID_373270.
DR   GeneID; 373270; -.
DR   KEGG; spu:373270; -.
DR   CTD; 5656850; -.
DR   eggNOG; KOG3867; Eukaryota.
DR   HOGENOM; CLU_006332_13_3_1; -.
DR   OMA; NTYNDWF; -.
DR   OrthoDB; 515367at2759; -.
DR   PhylomeDB; P50473; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
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; Hydrolase; Metal-binding; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..567
FT                   /note="Arylsulfatase"
FT                   /id="PRO_0000033443"
FT   ACT_SITE        115
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         324
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         115
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   567 AA;  62478 MW;  D55B627983A4C4D6 CRC64;
     MARTLFASLF LFLVLGLVAG QGDDTDGPDA ESLASLDRTA TRRYGDGEDL LHLLGQTGQH
     RTAMTKPNVI LLLADDMGVG DLSVYGHPTQ EPGFIDQMAN QGLRFTQGYS GDSVCTPSRS
     AIVTGRQPIR TGVYGEERIF LPWTTTGLPL YEVTIAEAMK GAGYTTGMVG KWHLGINENS
     SSDGAHLPAN RGFDFVGHNL PFGNSWRCDD TGLHQDFPDT NACFLYYNST SVAQPFQHKG
     LTQLLRDDTV GFIEDNVNKP FFMYVSFAHM HTSLFSSDDF SCTSRRGRYG DNLREMDQAI
     EQIVTTLVDN DIDDNTVIFF TSDHGPHREY CGEGGDANVF RGGKGQSWEG GHRIPYIVYW
     PGTISPGVSH EIVTSMDIIA TAVNLGGSQL PTDRIYDGKC LKSVLLEGAS SPHDDFFYYC
     KDTLMAVRVG KYKAHFKTQT DSSQMKLGER CDGGFPLDDY FLCSDCEGDC VTEHNPPIMF
     DLEKDPGENY PLGPCGYEHV LLHVKDAIAR HDAEMVIGTP VLDNFDFSII PCCNPETNCV
     CNYTHEPGVA ECYQDLINIA LRNGVPK