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Protein

Iduronate 2-sulfatase

Gene

Ids

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Required for the lysosomal degradation of heparan sulfate and dermatan sulfate.1 Publication

Catalytic activityi

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

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471CalciumBy similarity
Metal bindingi48 – 481CalciumBy similarity
Metal bindingi86 – 861Calcium; via 3-oxoalanineBy similarity
Metal bindingi336 – 3361CalciumBy similarity
Metal bindingi337 – 3371CalciumBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_294584. CS/DS degradation.
REACT_343711. HS-GAG degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Iduronate 2-sulfatase (EC:3.1.6.13)
Alternative name(s):
Alpha-L-iduronate sulfate sulfatase
Gene namesi
Name:Ids
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:96417. Ids.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Propeptidei30 – 356By similarityPRO_0000033431
Chaini36 – 552517Iduronate 2-sulfatasePRO_0000033432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 8613-oxoalanine (Cys)By similarity
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ08890.
PaxDbiQ08890.
PRIDEiQ08890.

PTM databases

PhosphoSiteiQ08890.

Expressioni

Tissue specificityi

Found to be expressed in alpha and beta pancreatic cells.1 Publication

Inductioni

By glucose, in a dose dependent manner.1 Publication

Gene expression databases

BgeeiQ08890.
CleanExiMM_IDS.
ExpressionAtlasiQ08890. baseline and differential.
GenevisibleiQ08890. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099046.

Structurei

3D structure databases

ProteinModelPortaliQ08890.
SMRiQ08890. Positions 40-413.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00730000110906.
HOVERGENiHBG006120.
InParanoidiQ08890.
KOiK01136.
OMAiDHNMYND.
OrthoDBiEOG7PK8ZR.
TreeFamiTF323156.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 2 hits.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q08890-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPPPPPPIW RQLSFSLLLG SFCIALESAA QGNSATDALN ILLIIVDDLR
60 70 80 90 100
PSLGCYGDKL VRSPNIDQLA SHSVLFQNAF AQQAVCAPSR VSFLTGRRPD
110 120 130 140 150
TTRLYDFNSY WRVHSGNFST IPQYFKENGY VTMSVGKVFH PGISSNHSDD
160 170 180 190 200
YPYSWSFPPY HPSSEKYENT KTCKGQDGKL HANLLCPVDV ADVPEGTLPD
210 220 230 240 250
KQSTEEAIRL LEKMKTSASP FFLAVGYHKP HIPFRYPKEF QKLYPLENIT
260 270 280 290 300
LAPDPHVPDS LPPVAYNPWM DIREREDVQA LNISVPYGPI PEDFQRKIRQ
310 320 330 340 350
SYFASVSYLD TQVGHVLSAL DDLRLAHNTI IAFTSDHGWA LGEHGEWAKY
360 370 380 390 400
SNFDVATRVP LMLYVPGRTA PLPAAGQKLF PYRDPFDPAS DWMDAGRHTE
410 420 430 440 450
DLVELVSLFP TLAGLAGLPV PPRCPIPSFH VELCREGQNL QKHLQLHDLE
460 470 480 490 500
EEPDLFGNPR ELIAYSQYPR PADFPQWNSD KPSLNDIKVM GYSIRTVDYR
510 520 530 540 550
YTVWVGFDPS EFLANFSDIH AGELYFVDSD PLQDHNVYND SQHGGLLHSL

RP
Length:552
Mass (Da):62,186
Last modified:July 27, 2011 - v3
Checksum:i3E3D819A823AFDE5
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411I → V in BAE38612 (PubMed:16141072).Curated
Sequence conflicti218 – 2181A → G in AAA37880 (PubMed:8325651).Curated
Sequence conflicti483 – 4831S → T in AAA37880 (PubMed:8325651).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK166178 mRNA. Translation: BAE38612.1.
BX294168 Genomic DNA. Translation: CAM20128.1.
L07921 mRNA. Translation: AAA37880.1. Frameshift.
BN000750 mRNA. Translation: CAI84996.1.
CCDSiCCDS40996.1.
PIRiA47153.
RefSeqiNP_034628.2. NM_010498.3.
UniGeneiMm.233083.

Genome annotation databases

EnsembliENSMUST00000101509; ENSMUSP00000099046; ENSMUSG00000035847.
GeneIDi15931.
KEGGimmu:15931.
UCSCiuc012hjl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK166178 mRNA. Translation: BAE38612.1.
BX294168 Genomic DNA. Translation: CAM20128.1.
L07921 mRNA. Translation: AAA37880.1. Frameshift.
BN000750 mRNA. Translation: CAI84996.1.
CCDSiCCDS40996.1.
PIRiA47153.
RefSeqiNP_034628.2. NM_010498.3.
UniGeneiMm.233083.

3D structure databases

ProteinModelPortaliQ08890.
SMRiQ08890. Positions 40-413.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000099046.

PTM databases

PhosphoSiteiQ08890.

Proteomic databases

MaxQBiQ08890.
PaxDbiQ08890.
PRIDEiQ08890.

Protocols and materials databases

DNASUi15931.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000101509; ENSMUSP00000099046; ENSMUSG00000035847.
GeneIDi15931.
KEGGimmu:15931.
UCSCiuc012hjl.1. mouse.

Organism-specific databases

CTDi3423.
MGIiMGI:96417. Ids.

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00730000110906.
HOVERGENiHBG006120.
InParanoidiQ08890.
KOiK01136.
OMAiDHNMYND.
OrthoDBiEOG7PK8ZR.
TreeFamiTF323156.

Enzyme and pathway databases

ReactomeiREACT_294584. CS/DS degradation.
REACT_343711. HS-GAG degradation.

Miscellaneous databases

ChiTaRSiIds. mouse.
NextBioi288652.
PROiQ08890.
SOURCEiSearch...

Gene expression databases

BgeeiQ08890.
CleanExiMM_IDS.
ExpressionAtlasiQ08890. baseline and differential.
GenevisibleiQ08890. MM.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 2 hits.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiIDS_MOUSE
AccessioniPrimary (citable) accession number: Q08890
Secondary accession number(s): Q32KI7, Q3TM30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.