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P50429

- ARSB_MOUSE

UniProt

P50429 - ARSB_MOUSE

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Protein
Arylsulfatase B
Gene
Arsb, As1, As1-s
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate.

Cofactori

Binds 1 calcium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541Calcium By similarity
Metal bindingi55 – 551Calcium By similarity
Metal bindingi92 – 921Calcium; via 3-oxoalanine By similarity
Binding sitei146 – 1461Substrate By similarity
Active sitei148 – 1481 By similarity
Binding sitei243 – 2431Substrate By similarity
Metal bindingi301 – 3011Calcium By similarity
Metal bindingi302 – 3021Calcium By similarity
Binding sitei319 – 3191Substrate By similarity

GO - Molecular functioni

  1. N-acetylgalactosamine-4-sulfatase activity Source: UniProtKB-EC
  2. arylsulfatase activity Source: MGI
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. autophagy Source: Ensembl
  2. central nervous system development Source: Ensembl
  3. response to estrogen Source: Ensembl
  4. response to methylmercury Source: Ensembl
  5. response to nutrient Source: Ensembl
  6. response to pH Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198981. CS/DS degradation.
REACT_198990. The activation of arylsulfatases.
REACT_199008. Glycosphingolipid metabolism.
SABIO-RKP50429.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase B (EC:3.1.6.12)
Short name:
ASB
Alternative name(s):
N-acetylgalactosamine-4-sulfatase
Short name:
G4S
Gene namesi
Name:Arsb
Synonyms:As1, As1-s
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:88075. Arsb.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. lysosome Source: UniProtKB-SubCell
  3. mitochondrion Source: Ensembl
  4. rough endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141 Reviewed prediction
Add
BLAST
Chaini42 – 534493Arylsulfatase B
PRO_0000033423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei92 – 9213-oxoalanine (Cys) By similarity
Disulfide bondi118 ↔ 522 By similarity
Disulfide bondi122 ↔ 156 By similarity
Disulfide bondi182 ↔ 193 By similarity
Glycosylationi189 – 1891N-linked (GlcNAc...) Reviewed prediction
Glycosylationi280 – 2801N-linked (GlcNAc...) Reviewed prediction
Glycosylationi292 – 2921N-linked (GlcNAc...) Reviewed prediction
Glycosylationi367 – 3671N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi406 ↔ 448 By similarity
Glycosylationi427 – 4271N-linked (GlcNAc...) Reviewed prediction
Glycosylationi459 – 4591N-linked (GlcNAc...) Reviewed prediction

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

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP50429.
PaxDbiP50429.
PRIDEiP50429.

PTM databases

PhosphoSiteiP50429.

Expressioni

Gene expression databases

BgeeiP50429.
CleanExiMM_ARSB.
GenevestigatoriP50429.

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliP50429.
SMRiP50429. Positions 43-534.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00560000077076.
HOGENOMiHOG000135354.
HOVERGENiHBG004282.
InParanoidiP50429.
KOiK01135.
OrthoDBiEOG7MKW5Q.
PhylomeDBiP50429.
TreeFamiTF314186.

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. 1 hit.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P50429-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGKLSPCTGR SRPGGPGPQL PLLLLLLQLL LLLLSPARAS GATQPPHVVF    50
VLADDLGWND LGFHGSVIRT PHLDALAAGG VVLDNYYVQP LCTPSRSQLL 100
TGRYQIHLGL QHYLIMTCQP SCVPLDEKLL PQLLKEAGYA THMVGKWHLG 150
MYRKECLPTR RGFDTYFGYL LGSEDYYTHE ACAPIESLNG TRCALDLRDG 200
EEPAKEYNNI YSTNIFTKRA TTVIANHPPE KPLFLYLAFQ SVHDPLQVPE 250
EYMEPYGFIQ DKHRRIYAGM VSLMDEAVGN VTKALKSHGL WNNTVFIFST 300
DNGGQTRSGG NNWPLRGRKG TLWEGGIRGT GFVASPLLKQ KGVKSRELMH 350
ITDWLPTLVD LAGGSTNGTK PLDGFNMWKT ISEGHPSPRV ELLHNIDQDF 400
FDGLPCPGKN MTPAKDDSFP LEHSAFNTSI HAGIRYKNWK LLTGHPGCGY 450
WFPPPSQSNV SEIPPVGPPT KTLWLFDINQ DPEERHDVSR EHPHIVQNLL 500
SRLQYYHEHS VPSHFPPLDP RCDPKSTGVW SPWM 534
Length:534
Mass (Da):59,647
Last modified:January 9, 2007 - v3
Checksum:i78DAB2D65C71E97D
GO
Isoform 2 (identifier: P50429-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     383-431: EGHPSPRVEL...EHSAFNTSIH → PVTGDHWHAE...PDCGRARWFL
     432-534: Missing.

Show »
Length:431
Mass (Da):47,934
Checksum:iE3C8BBE3E0B7C6D5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei383 – 43149EGHPS…NTSIH → PVTGDHWHAEGELGCSFRTA SAAEEEPTYKLREKKRRKSP DCGRARWFL in isoform 2.
VSP_007881Add
BLAST
Alternative sequencei432 – 534103Missing in isoform 2.
VSP_022249Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601D → A in AAA37261. 1 Publication
Sequence conflicti352 – 3521T → S in BAE34455. 1 Publication
Sequence conflicti352 – 3521T → S in CAA63067. 1 Publication
Sequence conflicti467 – 4671G → D in CAI84992. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK083309 mRNA. Translation: BAC38859.1.
AK154098 mRNA. Translation: BAE32375.1.
AK158312 mRNA. Translation: BAE34455.1.
AC131739 Genomic DNA. No translation available.
AC136976 Genomic DNA. No translation available.
M82877 mRNA. Translation: AAA37261.1.
X92096 mRNA. Translation: CAA63067.1.
BN000746 mRNA. Translation: CAI84992.1.
CCDSiCCDS36749.1. [P50429-1]
RefSeqiNP_033842.3. NM_009712.3.
UniGeneiMm.300178.
Mm.472255.

Genome annotation databases

EnsembliENSMUST00000091403; ENSMUSP00000088964; ENSMUSG00000042082.
GeneIDi11881.
KEGGimmu:11881.
UCSCiuc007rlo.1. mouse. [P50429-1]
uc011zcv.1. mouse. [P50429-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK083309 mRNA. Translation: BAC38859.1 .
AK154098 mRNA. Translation: BAE32375.1 .
AK158312 mRNA. Translation: BAE34455.1 .
AC131739 Genomic DNA. No translation available.
AC136976 Genomic DNA. No translation available.
M82877 mRNA. Translation: AAA37261.1 .
X92096 mRNA. Translation: CAA63067.1 .
BN000746 mRNA. Translation: CAI84992.1 .
CCDSi CCDS36749.1. [P50429-1 ]
RefSeqi NP_033842.3. NM_009712.3.
UniGenei Mm.300178.
Mm.472255.

3D structure databases

ProteinModelPortali P50429.
SMRi P50429. Positions 43-534.
ModBasei Search...

PTM databases

PhosphoSitei P50429.

Proteomic databases

MaxQBi P50429.
PaxDbi P50429.
PRIDEi P50429.

Protocols and materials databases

DNASUi 11881.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000091403 ; ENSMUSP00000088964 ; ENSMUSG00000042082 .
GeneIDi 11881.
KEGGi mmu:11881.
UCSCi uc007rlo.1. mouse. [P50429-1 ]
uc011zcv.1. mouse. [P50429-2 ]

Organism-specific databases

CTDi 411.
MGIi MGI:88075. Arsb.

Phylogenomic databases

eggNOGi COG3119.
GeneTreei ENSGT00560000077076.
HOGENOMi HOG000135354.
HOVERGENi HBG004282.
InParanoidi P50429.
KOi K01135.
OrthoDBi EOG7MKW5Q.
PhylomeDBi P50429.
TreeFami TF314186.

Enzyme and pathway databases

Reactomei REACT_198981. CS/DS degradation.
REACT_198990. The activation of arylsulfatases.
REACT_199008. Glycosphingolipid metabolism.
SABIO-RK P50429.

Miscellaneous databases

NextBioi 279911.
PROi P50429.
SOURCEi Search...

Gene expression databases

Bgeei P50429.
CleanExi MM_ARSB.
Genevestigatori P50429.

Family and domain databases

Gene3Di 3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view ]
Pfami PF00884. Sulfatase. 1 hit.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Inner ear and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The sulfatase gene family: cross-species PCR cloning using the MOPAC technique."
    Grompe M., Pieretti M., Caskey C.T., Ballabio A.
    Genomics 12:755-760(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-90 (ISOFORM 1).
  4. "Targeted disruption of the arylsulfatase B gene results in mice resembling the phenotype of mucopolysaccharidosis VI."
    Evers M., Saftig P., Schmidt P., Hafner A., McLoghlin D.B., Schmahl W., Hess B., von Figura K., Peters C.
    Proc. Natl. Acad. Sci. U.S.A. 93:8214-8219(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 137-388 (ISOFORM 1).
  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 nameiARSB_MOUSE
AccessioniPrimary (citable) accession number: P50429
Secondary accession number(s): Q32KJ1
, Q3TYV7, Q3U4Q6, Q8C404
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 9, 2007
Last modified: September 3, 2014
This is version 124 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