IDS_MOUSE
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 03-AUG-2022, entry version 146.
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 GlyGen; Q08890; 6 sites, 7 N-linked glycans (3 sites).
DR iPTMnet; Q08890; -.
DR PhosphoSitePlus; Q08890; -.
DR MaxQB; Q08890; -.
DR PaxDb; Q08890; -.
DR PeptideAtlas; Q08890; -.
DR PRIDE; Q08890; -.
DR ProteomicsDB; 273266; -.
DR DNASU; 15931; -.
DR Ensembl; ENSMUST00000101509; ENSMUSP00000099046; ENSMUSG00000035847.
DR GeneID; 15931; -.
DR KEGG; mmu:15931; -.
DR UCSC; uc012hjl.1; mouse.
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; PHLDAFA; -.
DR OrthoDB; 1353742at2759; -.
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 71 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 223 other tissues.
DR ExpressionAtlas; Q08890; baseline and differential.
DR Genevisible; Q08890; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IDA:MGI.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; ISS:UniProtKB.
DR CDD; cd16030; iduronate-2-sulfatase; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035874; IDS.
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; 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
