ARSI_MOUSE
ID ARSI_MOUSE Reviewed; 573 AA.
AC Q32KI9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Arylsulfatase I;
DE Short=ASI;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=Arsi;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION.
RX PubMed=16174644; DOI=10.1093/hmg/ddi351;
RA Sardiello M., Annunziata I., Roma G., Ballabio A.;
RT "Sulfatases and sulfatase modifying factors: an exclusive and promiscuous
RT relationship.";
RL Hum. Mol. Genet. 14:3203-3217(2005).
CC -!- FUNCTION: Displays arylsulfatase activity at neutral pH, when co-
CC expressed with SUMF1; arylsulfatase activity is measured in the
CC secretion medium of retinal cell line, but no activity is recorded when
CC measured in cell extracts. {ECO:0000250|UniProtKB:Q5FYB1}.
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: Secreted {ECO:0000250|UniProtKB:Q5FYB1}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q5FYB1}. Note=Localized in
CC the intracellular granular structures. {ECO:0000250|UniProtKB:Q5FYB1}.
CC -!- PTM: The oxidation of Cys-93 residue to 3-oxoalanine (also known as
CC C(alpha)-formylglycine) by SUMF1/Sulfatase-modifying factor 1, seems
CC critical for catalytic activity. {ECO:0000250|UniProtKB:Q5FYB1}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; CH466528; EDL09797.1; -; Genomic_DNA.
DR EMBL; BC138970; AAI38971.1; -; mRNA.
DR EMBL; BC141169; AAI41170.1; -; mRNA.
DR EMBL; BN000748; CAI84994.1; -; mRNA.
DR CCDS; CCDS29275.1; -.
DR RefSeq; NP_001033588.1; NM_001038499.1.
DR AlphaFoldDB; Q32KI9; -.
DR SMR; Q32KI9; -.
DR STRING; 10090.ENSMUSP00000043966; -.
DR GlyGen; Q32KI9; 4 sites.
DR iPTMnet; Q32KI9; -.
DR PhosphoSitePlus; Q32KI9; -.
DR MaxQB; Q32KI9; -.
DR PaxDb; Q32KI9; -.
DR PRIDE; Q32KI9; -.
DR Antibodypedia; 50254; 188 antibodies from 26 providers.
DR Ensembl; ENSMUST00000040359; ENSMUSP00000043966; ENSMUSG00000036412.
DR GeneID; 545260; -.
DR KEGG; mmu:545260; -.
DR UCSC; uc008fbe.1; mouse.
DR CTD; 340075; -.
DR MGI; MGI:2670959; Arsi.
DR VEuPathDB; HostDB:ENSMUSG00000036412; -.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000157656; -.
DR HOGENOM; CLU_006332_10_1_1; -.
DR InParanoid; Q32KI9; -.
DR OMA; WGPWASE; -.
DR OrthoDB; 515367at2759; -.
DR PhylomeDB; Q32KI9; -.
DR TreeFam; TF314186; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-1663150; The activation of arylsulfatases.
DR BioGRID-ORCS; 545260; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q32KI9; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q32KI9; protein.
DR Bgee; ENSMUSG00000036412; Expressed in epithelium of lens and 114 other tissues.
DR Genevisible; Q32KI9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
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; Endoplasmic reticulum; Glycoprotein; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..573
FT /note="Arylsulfatase I"
FT /id="PRO_0000356284"
FT REGION 515..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 149
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 93
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:Q5FYB1"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 573 AA; 64367 MW; C12EF772465AA21E CRC64;
MHALSGFSLV SLLSLGYLSW DWAKPGLVAD GPAEAGDQPS VAPPQPPHII FILTDDQGYH
DVGYHGSDIE TPTLDRLAAE GVKLENYYIQ PICTPSRSQL LTGRYQIHTG LQHSIIRPRQ
PNCLPLDQVT LPQKLQEAGY STHMVGKWHL GFYRKECLPT RRGFDTFLGS LTGNVDYYTY
DNCDGPGVCG FDLHEGESVA WGLSGQYSTM LYAQRASHIL ASHNPQNPLF LYVAFQAVHT
PLQSPREYLY RYRTMGNVAR RKYAAMVTCM DEAVRNITWA LKRYGFYNNS VIIFSSDNGG
QTFSGGSNWP LRGRKGTYWE GGVRGLGFVH SPLLKKKRRT SRALVHITDW YPTLVGLAGG
TTSAADGLDG YDVWPAISEG RASPRTEILH NIDPLYNHAR HGSLEGGFGI WNTAVQAAIR
VGEWKLLTGD PGYGDWIPPQ TLASFPGSWW NLERMASIRQ AVWLFNISAD PYEREDLAGQ
RPDVVRTLLA RLADYNRTAI PVRYPAANPR AHPDFNGGAW GPWASEEEEE EEEEEEEGRA
RSFSRGRRKK KCKICKLRSF FRKLNTRLMS HRI
