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Q08890 (IDS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Iduronate 2-sulfatase

EC=3.1.6.13
Alternative name(s):
Alpha-L-iduronate sulfate sulfatase
Gene names
Name:Ids
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Required for the lysosomal degradation of heparan sulfate and dermatan sulfate. Ref.4

Catalytic activity

Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Lysosome.

Tissue specificity

Found to be expressed in alpha and beta pancreatic cells. Ref.4

Induction

By glucose, in a dose dependent manner. Ref.4

Post-translational modification

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 By similarity.

Sequence similarities

Belongs to the sulfatase family.

Sequence caution

The sequence AAA37880.1 differs from that shown. Reason: Frameshift at positions 420, 458, 488, 493 and 497.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMGlycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioniduronate-2-sulfatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sulfuric ester hydrolase activity

Inferred from direct assay PubMed 15962010. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Propeptide30 – 356 By similarity
PRO_0000033431
Chain36 – 552517Iduronate 2-sulfatase
PRO_0000033432

Sites

Metal binding471Calcium By similarity
Metal binding481Calcium By similarity
Metal binding861Calcium; via 3-oxoalanine By similarity
Metal binding3361Calcium By similarity
Metal binding3371Calcium By similarity

Amino acid modifications

Modified residue8613-oxoalanine (Cys) By similarity
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation2481N-linked (GlcNAc...) Potential
Glycosylation2821N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation5391N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict411I → V in BAE38612. Ref.1
Sequence conflict2181A → G in AAA37880. Ref.3
Sequence conflict4831S → T in AAA37880. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q08890 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 3E3D819A823AFDE5

FASTA55262,186
        10         20         30         40         50         60 
MSPPPPPPIW RQLSFSLLLG SFCIALESAA QGNSATDALN ILLIIVDDLR PSLGCYGDKL 

        70         80         90        100        110        120 
VRSPNIDQLA SHSVLFQNAF AQQAVCAPSR VSFLTGRRPD TTRLYDFNSY WRVHSGNFST 

       130        140        150        160        170        180 
IPQYFKENGY VTMSVGKVFH PGISSNHSDD YPYSWSFPPY HPSSEKYENT KTCKGQDGKL 

       190        200        210        220        230        240 
HANLLCPVDV ADVPEGTLPD KQSTEEAIRL LEKMKTSASP FFLAVGYHKP HIPFRYPKEF 

       250        260        270        280        290        300 
QKLYPLENIT LAPDPHVPDS LPPVAYNPWM DIREREDVQA LNISVPYGPI PEDFQRKIRQ 

       310        320        330        340        350        360 
SYFASVSYLD TQVGHVLSAL DDLRLAHNTI IAFTSDHGWA LGEHGEWAKY SNFDVATRVP 

       370        380        390        400        410        420 
LMLYVPGRTA PLPAAGQKLF PYRDPFDPAS DWMDAGRHTE DLVELVSLFP TLAGLAGLPV 

       430        440        450        460        470        480 
PPRCPIPSFH VELCREGQNL QKHLQLHDLE EEPDLFGNPR ELIAYSQYPR PADFPQWNSD 

       490        500        510        520        530        540 
KPSLNDIKVM GYSIRTVDYR YTVWVGFDPS EFLANFSDIH AGELYFVDSD PLQDHNVYND 

       550 
SQHGGLLHSL RP 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Cloning and characterization of the cDNA for the murine iduronate sulfatase gene."
Daniele A., Faust C.J., Herman G.E., di Natale P., Ballabio A.
Genomics 16:755-757(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-552.
Tissue: Thymus.
[4]"Identification of iduronate-2-sulfatase in mouse pancreatic islets."
Coronado-Pons I., Novials A., Casas S., Clark A., Gomis R.
Am. J. Physiol. 287:E983-E990(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[5]"Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship."
Sardiello M., Annunziata I., Roma G., Ballabio A.
Hum. Mol. Genet. 14:3203-3217(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK166178 mRNA. Translation: BAE38612.1.
BX294168 Genomic DNA. Translation: CAM20128.1.
L07921 mRNA. Translation: AAA37880.1. Frameshift.
BN000750 mRNA. Translation: CAI84996.1.
PIRA47153.
RefSeqNP_034628.2. NM_010498.3.
UniGeneMm.233083.

3D structure databases

ProteinModelPortalQ08890.
SMRQ08890. Positions 40-413.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ08890.

Proteomic databases

PaxDbQ08890.
PRIDEQ08890.

Protocols and materials databases

DNASU15931.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000101509; ENSMUSP00000099046; ENSMUSG00000035847.
GeneID15931.
KEGGmmu:15931.
UCSCuc012hjl.1. mouse.

Organism-specific databases

CTD3423.
MGIMGI:96417. Ids.

Phylogenomic databases

eggNOGCOG3119.
GeneTreeENSGT00730000110906.
HOVERGENHBG006120.
InParanoidQ32KI7.
KOK01136.
OMADHNMYND.
OrthoDBEOG7PK8ZR.
TreeFamTF323156.

Gene expression databases

ArrayExpressQ08890.
BgeeQ08890.
CleanExMM_IDS.
GenevestigatorQ08890.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 2 hits.
PROSITEPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIDS. mouse.
NextBio288652.
PROQ08890.
SOURCESearch...

Entry information

Entry nameIDS_MOUSE
AccessionPrimary (citable) accession number: Q08890
Secondary accession number(s): Q32KI7, Q3TM30
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: February 19, 2014
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot