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Arylsulfatase (AS) (EC 3.1.6.1) (Aryl-sulfate sulphohydrolase) (ARS)

 ARS_HEMPU               Reviewed;         551 AA.
P14000;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
05-DEC-2018, entry version 84.
RecName: Full=Arylsulfatase;
Short=AS;
EC=3.1.6.1;
AltName: Full=Aryl-sulfate sulphohydrolase;
Short=ARS;
Flags: Precursor;
Hemicentrotus pulcherrimus (Sea urchin) (Strongylocentrotus
pulcherrimus).
Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa;
Echinoidea; Euechinoidea; Echinacea; Echinoida; Strongylocentrotidae;
Hemicentrotus.
NCBI_TaxID=7650;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Pluteus;
PubMed=3181160; DOI=10.1111/j.1432-1033.1988.tb14338.x;
Sasaki H., Yamada K., Akasaka H., Suzuki K., Saito A., Sato M.,
Shimada H.;
"cDNA cloning, nucleotide sequence and expression of the gene for
arylsulfatase in the sea urchin (Hemicentrotus pulcherrimus) embryo.";
Eur. J. Biochem. 177:9-13(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2598936; DOI=10.1111/j.1432-1033.1989.tb15223.x;
Yamada K., Akasaka K., Shimada H.;
"Structure of sea-urchin arylsulfatase gene.";
Eur. J. Biochem. 186:405-410(1989).
-!- FUNCTION: May be a structural component of the extracellular
matrices involved in cell movement during morphogenesis.
-!- CATALYTIC ACTIVITY:
Reaction=a phenyl sulfate + H2O = a phenol + H(+) + sulfate;
Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317;
EC=3.1.6.1;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Cytoplasm. Secreted, extracellular space,
extracellular matrix.
-!- PTM: The conversion to 3-oxoalanine (also known as C-
formylglycine, FGly), of a serine or cysteine residue in
prokaryotes and of a cysteine residue in eukaryotes, is critical
for catalytic activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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EMBL; X17015; CAA34881.1; -; mRNA.
PIR; S01793; S01793.
PIR; S07089; S07089.
ProteinModelPortal; P14000; -.
SMR; P14000; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR024607; Sulfatase_CS.
InterPro; IPR000917; Sulfatase_N.
Pfam; PF00884; Sulfatase; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00523; SULFATASE_1; 1.
PROSITE; PS00149; SULFATASE_2; 1.
1: Evidence at protein level;
Calcium; Cytoplasm; Direct protein sequencing; Extracellular matrix;
Glycoprotein; Hydrolase; Metal-binding; Secreted; Signal.
SIGNAL 1 20
CHAIN 21 551 Arylsulfatase.
/FTId=PRO_0000033442.
ACT_SITE 100 100 Nucleophile.
{ECO:0000250|UniProtKB:P15289}.
ACT_SITE 158 158 {ECO:0000250|UniProtKB:P15289}.
METAL 60 60 Calcium. {ECO:0000250}.
METAL 61 61 Calcium. {ECO:0000250}.
METAL 100 100 Calcium; via 3-oxoalanine. {ECO:0000250}.
METAL 308 308 Calcium. {ECO:0000250}.
METAL 309 309 Calcium. {ECO:0000250}.
MOD_RES 21 21 Blocked amino end (Gln).
MOD_RES 100 100 3-oxoalanine (Cys).
{ECO:0000250|UniProtKB:P15289}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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