ID   ARS_HEMPU               Reviewed;         551 AA.
AC   P14000;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Hemicentrotus pulcherrimus (Sea urchin) (Strongylocentrotus pulcherrimus).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Hemicentrotus.
OX   NCBI_TaxID=7650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Pluteus;
RX   PubMed=3181160; DOI=10.1111/j.1432-1033.1988.tb14338.x;
RA   Sasaki H., Yamada K., Akasaka H., Suzuki K., Saito A., Sato M., Shimada H.;
RT   "cDNA cloning, nucleotide sequence and expression of the gene for
RT   arylsulfatase in the sea urchin (Hemicentrotus pulcherrimus) embryo.";
RL   Eur. J. Biochem. 177:9-13(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2598936; DOI=10.1111/j.1432-1033.1989.tb15223.x;
RA   Yamada K., Akasaka K., Shimada H.;
RT   "Structure of sea-urchin arylsulfatase gene.";
RL   Eur. J. Biochem. 186:405-410(1989).
CC   -!- FUNCTION: May be a structural component of the extracellular matrices
CC       involved in cell movement during morphogenesis.
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: Cytoplasm. Secreted, extracellular space,
CC       extracellular matrix.
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; X17015; CAA34881.1; -; mRNA.
DR   PIR; S01793; S01793.
DR   PIR; S07089; S07089.
DR   AlphaFoldDB; P14000; -.
DR   SMR; P14000; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-EC.
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   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Direct protein sequencing; Extracellular matrix;
KW   Glycoprotein; Hydrolase; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..551
FT                   /note="Arylsulfatase"
FT                   /id="PRO_0000033442"
FT   ACT_SITE        100
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         21
FT                   /note="Blocked amino end (Gln)"
FT   MOD_RES         100
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   551 AA;  60952 MW;  54C1AAC14D6710C9 CRC64;
     MKSAPFLFLL GLLGLVTAQT QDPALLDLLR ENPDLLSLLL QSNEHRAPLV KPNVVLLVAD
     HMGSGDLTSY GHPTQEAGFI DKMAAEGLRF TNGYVGDAVC TPSRSAIMTG RLPVRIGTFG
     ETRVFLPWTK TGLPKSELTI AEAMKEAGYA TGMVGKWHLG INENSSTDGA HLPFNHGFDF
     VGHNLPFTNS WSCDDTGLHK DFPDSQRCYL YVNATLVSQP YQHKGLTQLF TDDALGFIED
     NHADPFFLYV AFAHMHTSLF SSDDFSCTSR RGRYGDNLLE MHDAVQKIVD KLEENNISEN
     TIIFFISDHG PHREYCEEGG DASIFRGGKS HSWEGGHRIP YIVYWPGTIS PGISNEIVTS
     MDIIATAADL GGTTLPTDRI YDGKSIKDVL LEGSASPHSS FFYYCKDNLM AVRVGKYKAH
     FRTQRVRSQD EYGLECAGGF PLEDYFDCND CEGDCVTEHD PPLLFDLHRD PGEAYPLEAC
     GHEDVFLTVK STVEEHKAAL VKGTPLLDSF DHSIVPCCNP ANGCICNYVH EPGMPECYQD
     QVATAARHYR P