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Arylsulfatase I (ASI) (EC 3.1.6.-)

 ARSI_HUMAN              Reviewed;         569 AA.
Q5FYB1; A1L3B0; B3KV22; B7XD03;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 1.
05-DEC-2018, entry version 122.
RecName: Full=Arylsulfatase I;
Short=ASI;
EC=3.1.6.-;
Flags: Precursor;
Name=ARSI;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=16174644; DOI=10.1093/hmg/ddi351;
Sardiello M., Annunziata I., Roma G., Ballabio A.;
"Sulfatases and sulfatase modifying factors: an exclusive and
promiscuous relationship.";
Hum. Mol. Genet. 14:3203-3217(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
FUNCTION.
PubMed=16500042; DOI=10.1016/j.gene.2005.12.023;
Obaya A.J.;
"Molecular cloning and initial characterization of three novel human
sulfatases.";
Gene 372:110-117(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, MUTAGENESIS OF CYS-93, OXOALANINE AT CYS-93, AND TISSUE
SPECIFICITY.
PubMed=19262745;
Oshikawa M., Usami R., Kato S.;
"Characterization of the arylsulfatase I (ARSI) gene preferentially
expressed in the human retinal pigment epithelium cell line ARPE-19.";
Mol. Vis. 15:482-494(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Displays arylsulfatase activity at neutral pH, when co-
expressed with SUMF1; arylsulfatase activity is measured in the
secretion medium of retinal cell line, but no activity is recorded
when measured in cell extracts. {ECO:0000269|PubMed:16500042,
ECO:0000269|PubMed:19262745}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- INTERACTION:
Q6A162:KRT40; NbExp=3; IntAct=EBI-10243706, EBI-10171697;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19262745}.
Endoplasmic reticulum {ECO:0000269|PubMed:19262745}.
Note=Localized in the intracellular granular structures.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5FYB1-1; Sequence=Displayed;
Name=2;
IsoId=Q5FYB1-2; Sequence=VSP_036022;
-!- TISSUE SPECIFICITY: Expressed in placenta, in embryonic stem
cells, fetal eyes and lens. {ECO:0000269|PubMed:16500042,
ECO:0000269|PubMed:19262745}.
-!- PTM: The oxidation of Cys-93 residue to 3-oxoalanine (also known
as C(alpha)-formylglycine) by SUMF1/Sulfatase-modifying factor 1,
seems critical for catalytic activity.
{ECO:0000269|PubMed:19262745}.
-!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
-!- CAUTION: According to PubMed:16500042, has no arylsulfatase
activity. {ECO:0000305}.
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EMBL; AY875937; AAW66665.1; -; mRNA.
EMBL; AB448735; BAH11166.1; -; mRNA.
EMBL; AK122641; BAG53634.1; -; mRNA.
EMBL; BC129995; AAI29996.1; -; mRNA.
EMBL; BC129996; AAI29997.1; -; mRNA.
CCDS; CCDS34275.1; -. [Q5FYB1-1]
RefSeq; NP_001012301.1; NM_001012301.3. [Q5FYB1-1]
UniGene; Hs.591252; -.
ProteinModelPortal; Q5FYB1; -.
SMR; Q5FYB1; -.
BioGrid; 130992; 6.
IntAct; Q5FYB1; 1.
STRING; 9606.ENSP00000333395; -.
iPTMnet; Q5FYB1; -.
PhosphoSitePlus; Q5FYB1; -.
BioMuta; ARSI; -.
DMDM; 74722581; -.
PaxDb; Q5FYB1; -.
PeptideAtlas; Q5FYB1; -.
PRIDE; Q5FYB1; -.
ProteomicsDB; 62821; -.
ProteomicsDB; 62822; -. [Q5FYB1-2]
Ensembl; ENST00000328668; ENSP00000333395; ENSG00000183876. [Q5FYB1-1]
Ensembl; ENST00000515301; ENSP00000426879; ENSG00000183876. [Q5FYB1-2]
GeneID; 340075; -.
KEGG; hsa:340075; -.
UCSC; uc003lrv.3; human. [Q5FYB1-1]
CTD; 340075; -.
DisGeNET; 340075; -.
EuPathDB; HostDB:ENSG00000183876.8; -.
GeneCards; ARSI; -.
HGNC; HGNC:32521; ARSI.
HPA; HPA038386; -.
HPA; HPA038398; -.
MalaCards; ARSI; -.
MIM; 610009; gene.
neXtProt; NX_Q5FYB1; -.
OpenTargets; ENSG00000183876; -.
Orphanet; 401815; Autosomal recessive spastic paraplegia type 66.
PharmGKB; PA143485309; -.
eggNOG; KOG3867; Eukaryota.
eggNOG; COG3119; LUCA.
GeneTree; ENSGT00940000157656; -.
HOGENOM; HOG000135354; -.
HOVERGEN; HBG004282; -.
InParanoid; Q5FYB1; -.
KO; K12375; -.
OMA; QPNCLPF; -.
OrthoDB; EOG091G06C3; -.
PhylomeDB; Q5FYB1; -.
TreeFam; TF314186; -.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-1663150; The activation of arylsulfatases.
GenomeRNAi; 340075; -.
PRO; PR:Q5FYB1; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000183876; Expressed in 94 organ(s), highest expression level in tibia.
CleanEx; HS_ARSI; -.
ExpressionAtlas; Q5FYB1; baseline and differential.
Genevisible; Q5FYB1; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004065; F:arylsulfatase activity; TAS:HGNC.
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;
Alternative splicing; Calcium; Complete proteome;
Endoplasmic reticulum; Glycoprotein; Hydrolase; Metal-binding;
Oxidation; Reference proteome; Secreted; Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 569 Arylsulfatase I.
/FTId=PRO_0000042216.
COMPBIAS 527 533 Poly-Glu.
ACT_SITE 93 93 Nucleophile.
{ECO:0000269|PubMed:19262745}.
ACT_SITE 149 149 {ECO:0000250|UniProtKB:P15289}.
METAL 55 55 Calcium. {ECO:0000250}.
METAL 56 56 Calcium. {ECO:0000250}.
METAL 93 93 Calcium; via 3-oxoalanine. {ECO:0000250}.
METAL 297 297 Calcium. {ECO:0000250}.
METAL 298 298 Calcium. {ECO:0000250}.
BINDING 147 147 Substrate. {ECO:0000250}.
BINDING 239 239 Substrate. {ECO:0000250}.
BINDING 315 315 Substrate. {ECO:0000250}.
MOD_RES 93 93 3-oxoalanine (Cys).
{ECO:0000269|PubMed:19262745}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 466 466 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 496 496 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 143 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036022.
MUTAGEN 93 93 C->S: No arylsulfatase activity in the
media of retinal epithelium cell.
{ECO:0000269|PubMed:19262745}.
CONFLICT 171 171 L -> F (in Ref. 4; BAG53634).
{ECO:0000305}.
CONFLICT 211 211 L -> P (in Ref. 4; BAG53634).
{ECO:0000305}.
SEQUENCE 569 AA; 64030 MW; D2F33EDD33ED211C CRC64;
MHTLTGFSLV SLLSFGYLSW DWAKPSFVAD GPGEAGEQPS AAPPQPPHII FILTDDQGYH
DVGYHGSDIE TPTLDRLAAK GVKLENYYIQ PICTPSRSQL LTGRYQIHTG LQHSIIRPQQ
PNCLPLDQVT LPQKLQEAGY STHMVGKWHL GFYRKECLPT RRGFDTFLGS LTGNVDYYTY
DNCDGPGVCG FDLHEGENVA WGLSGQYSTM LYAQRASHIL ASHSPQRPLF LYVAFQAVHT
PLQSPREYLY RYRTMGNVAR RKYAAMVTCM DEAVRNITWA LKRYGFYNNS VIIFSSDNGG
QTFSGGSNWP LRGRKGTYWE GGVRGLGFVH SPLLKRKQRT SRALMHITDW YPTLVGLAGG
TTSAADGLDG YDVWPAISEG RASPRTEILH NIDPLYNHAQ HGSLEGGFGI WNTAVQAAIR
VGEWKLLTGD PGYGDWIPPQ TLATFPGSWW NLERMASVRQ AVWLFNISAD PYEREDLAGQ
RPDVVRTLLA RLAEYNRTAI PVRYPAENPR AHPDFNGGAW GPWASDEEEE EEEGRARSFS
RGRRKKKCKI CKLRSFFRKL NTRLMSQRI


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