ID   IDS_MOUSE               Reviewed;         552 AA.
AC   Q08890; Q32KI7; Q3TM30;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Iduronate 2-sulfatase;
DE            EC=3.1.6.13;
DE   AltName: Full=Alpha-L-iduronate sulfate sulfatase;
DE   Flags: Precursor;
GN   Name=Ids;
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 MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-552.
RC   TISSUE=Thymus;
RX   PubMed=8325651; DOI=10.1006/geno.1993.1259;
RA   Daniele A., Faust C.J., Herman G.E., di Natale P., Ballabio A.;
RT   "Cloning and characterization of the cDNA for the murine iduronate
RT   sulfatase gene.";
RL   Genomics 16:755-757(1993).
RN   [4]
RP   TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15149955; DOI=10.1152/ajpendo.00528.2003;
RA   Coronado-Pons I., Novials A., Casas S., Clark A., Gomis R.;
RT   "Identification of iduronate-2-sulfatase in mouse pancreatic islets.";
RL   Am. J. Physiol. 287:E983-E990(2004).
RN   [5]
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: Lysosomal enzyme involved in the degradation pathway of
CC       dermatan sulfate and heparan sulfate. {ECO:0000250|UniProtKB:P22304}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of the 2-sulfate groups of the L-iduronate 2-
CC         sulfate units of dermatan sulfate, heparan sulfate and heparin.;
CC         EC=3.1.6.13; Evidence={ECO:0000250|UniProtKB:P22304};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P22304};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P22304};
CC   -!- SUBUNIT: Monomer. The 58-kDa mature form is composed of two chains
CC       resulting from proteolitic processing, the 42-kDa chain and the 14-kDa
CC       chain that remain stably associated and form the 58-kDa intermediate
CC       form which is enzymatically active. {ECO:0000250|UniProtKB:P22304}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:15149955}.
CC   -!- TISSUE SPECIFICITY: Found to be expressed in alpha and beta pancreatic
CC       cells. {ECO:0000269|PubMed:15149955}.
CC   -!- INDUCTION: By glucose, in a dose dependent manner.
CC       {ECO:0000269|PubMed:15149955}.
CC   -!- PTM: Synthesized as a 75-kDa precursor form in the endoplasmic
CC       reticulum (ER), and then processed by proteolytic cleavage through
CC       various intermediates to yield a 55-kDa mature form, with the release
CC       of an 18 kDa polypeptide. {ECO:0000250|UniProtKB:P22304}.
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|UniProtKB:P15289}.
CC   -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37880.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK166178; BAE38612.1; -; mRNA.
DR   EMBL; BX294168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L07921; AAA37880.1; ALT_FRAME; mRNA.
DR   EMBL; BN000750; CAI84996.1; -; mRNA.
DR   CCDS; CCDS40996.1; -.
DR   PIR; A47153; A47153.
DR   RefSeq; NP_034628.2; NM_010498.3.
DR   AlphaFoldDB; Q08890; -.
DR   SMR; Q08890; -.
DR   STRING; 10090.ENSMUSP00000099046; -.
DR   GlyConnect; 2377; 7 N-Linked glycans (3 sites).
DR   GlyCosmos; Q08890; 6 sites, 7 glycans.
DR   GlyGen; Q08890; 6 sites, 7 N-linked glycans (3 sites).
DR   iPTMnet; Q08890; -.
DR   PhosphoSitePlus; Q08890; -.
DR   MaxQB; Q08890; -.
DR   PaxDb; 10090-ENSMUSP00000099046; -.
DR   PeptideAtlas; Q08890; -.
DR   ProteomicsDB; 273266; -.
DR   DNASU; 15931; -.
DR   Ensembl; ENSMUST00000101509.9; ENSMUSP00000099046.3; ENSMUSG00000035847.16.
DR   GeneID; 15931; -.
DR   KEGG; mmu:15931; -.
DR   UCSC; uc012hjl.1; mouse.
DR   AGR; MGI:96417; -.
DR   CTD; 3423; -.
DR   MGI; MGI:96417; Ids.
DR   VEuPathDB; HostDB:ENSMUSG00000035847; -.
DR   eggNOG; KOG3867; Eukaryota.
DR   GeneTree; ENSGT00940000156803; -.
DR   HOGENOM; CLU_006332_9_0_1; -.
DR   InParanoid; Q08890; -.
DR   OMA; HVFTRAY; -.
DR   OrthoDB; 2964021at2759; -.
DR   PhylomeDB; Q08890; -.
DR   TreeFam; TF323156; -.
DR   Reactome; R-MMU-2024096; HS-GAG degradation.
DR   Reactome; R-MMU-2024101; CS/DS degradation.
DR   BioGRID-ORCS; 15931; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Ids; mouse.
DR   PRO; PR:Q08890; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q08890; Protein.
DR   Bgee; ENSMUSG00000035847; Expressed in subparaventricular zone and 225 other cell types or tissues.
DR   ExpressionAtlas; Q08890; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043202; C:lysosomal lumen; IDA:MGI.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0004423; F:iduronate-2-sulfatase activity; IMP:MGI.
DR   GO; GO:0008484; F:sulfuric ester hydrolase activity; IDA:MGI.
DR   GO; GO:0030209; P:dermatan sulfate catabolic process; IMP:MGI.
DR   GO; GO:0006027; P:glycosaminoglycan catabolic process; ISS:UniProtKB.
DR   GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IMP:MGI.
DR   CDD; cd16030; iduronate-2-sulfatase; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR035874; IDS.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR45953; IDURONATE 2-SULFATASE; 1.
DR   PANTHER; PTHR45953:SF1; IDURONATE 2-SULFATASE; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
DR   PROSITE; PS00149; SULFATASE_2; 1.
DR   Genevisible; Q08890; MM.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Metal-binding;
KW   Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..35
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT                   /id="PRO_0000033431"
FT   CHAIN           36..552
FT                   /note="Iduronate 2-sulfatase"
FT                   /id="PRO_0000033432"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   BINDING         48
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   BINDING         86
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   BINDING         336
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   BINDING         337
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   MOD_RES         86
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        539
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        173..186
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   DISULFID        424..434
FT                   /evidence="ECO:0000250|UniProtKB:P22304"
FT   CONFLICT        41
FT                   /note="I -> V (in Ref. 1; BAE38612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="A -> G (in Ref. 3; AAA37880)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        483
FT                   /note="S -> T (in Ref. 3; AAA37880)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   552 AA;  62186 MW;  3E3D819A823AFDE5 CRC64;
     MSPPPPPPIW RQLSFSLLLG SFCIALESAA QGNSATDALN ILLIIVDDLR PSLGCYGDKL
     VRSPNIDQLA SHSVLFQNAF AQQAVCAPSR VSFLTGRRPD TTRLYDFNSY WRVHSGNFST
     IPQYFKENGY VTMSVGKVFH PGISSNHSDD YPYSWSFPPY HPSSEKYENT KTCKGQDGKL
     HANLLCPVDV ADVPEGTLPD KQSTEEAIRL LEKMKTSASP FFLAVGYHKP HIPFRYPKEF
     QKLYPLENIT LAPDPHVPDS LPPVAYNPWM DIREREDVQA LNISVPYGPI PEDFQRKIRQ
     SYFASVSYLD TQVGHVLSAL DDLRLAHNTI IAFTSDHGWA LGEHGEWAKY SNFDVATRVP
     LMLYVPGRTA PLPAAGQKLF PYRDPFDPAS DWMDAGRHTE DLVELVSLFP TLAGLAGLPV
     PPRCPIPSFH VELCREGQNL QKHLQLHDLE EEPDLFGNPR ELIAYSQYPR PADFPQWNSD
     KPSLNDIKVM GYSIRTVDYR YTVWVGFDPS EFLANFSDIH AGELYFVDSD PLQDHNVYND
     SQHGGLLHSL RP
//