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Protein

Arylsulfatase B

Gene

Arsb

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

Functioni

Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (By similarity). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (By similarity). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity, acting through the control of sulfate glycosaminoglycans and neurocan levels (By similarity).By similarity

Catalytic activityi

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

Cofactori

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

Enzyme regulationi

Inhibited by ethanol (By similarity).By similarity

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_294584. CS/DS degradation.
REACT_320139. The activation of arylsulfatases.
REACT_339900. 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 Componenti: Unplaced

Organism-specific databases

MGIiMGI:88075. Arsb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Sequence AnalysisAdd
BLAST
Chaini42 – 534493Arylsulfatase BPRO_0000033423Add
BLAST

Amino acid modifications

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

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP50429.
PaxDbiP50429.
PRIDEiP50429.

PTM databases

PhosphoSiteiP50429.

Expressioni

Gene expression databases

BgeeiP50429.
CleanExiMM_ARSB.
GenevisibleiP50429. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000088964.

Structurei

3D structure databases

ProteinModelPortaliP50429.
SMRiP50429. Positions 43-534.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
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. AlignAdd to basket

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

        10         20         30         40         50
MGKLSPCTGR SRPGGPGPQL PLLLLLLQLL LLLLSPARAS GATQPPHVVF
60 70 80 90 100
VLADDLGWND LGFHGSVIRT PHLDALAAGG VVLDNYYVQP LCTPSRSQLL
110 120 130 140 150
TGRYQIHLGL QHYLIMTCQP SCVPLDEKLL PQLLKEAGYA THMVGKWHLG
160 170 180 190 200
MYRKECLPTR RGFDTYFGYL LGSEDYYTHE ACAPIESLNG TRCALDLRDG
210 220 230 240 250
EEPAKEYNNI YSTNIFTKRA TTVIANHPPE KPLFLYLAFQ SVHDPLQVPE
260 270 280 290 300
EYMEPYGFIQ DKHRRIYAGM VSLMDEAVGN VTKALKSHGL WNNTVFIFST
310 320 330 340 350
DNGGQTRSGG NNWPLRGRKG TLWEGGIRGT GFVASPLLKQ KGVKSRELMH
360 370 380 390 400
ITDWLPTLVD LAGGSTNGTK PLDGFNMWKT ISEGHPSPRV ELLHNIDQDF
410 420 430 440 450
FDGLPCPGKN MTPAKDDSFP LEHSAFNTSI HAGIRYKNWK LLTGHPGCGY
460 470 480 490 500
WFPPPSQSNV SEIPPVGPPT KTLWLFDINQ DPEERHDVSR EHPHIVQNLL
510 520 530
SRLQYYHEHS VPSHFPPLDP RCDPKSTGVW SPWM
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601D → A in AAA37261 (PubMed:1572648).Curated
Sequence conflicti352 – 3521T → S in BAE34455 (PubMed:16141072).Curated
Sequence conflicti352 – 3521T → S in CAA63067 (PubMed:8710849).Curated
Sequence conflicti467 – 4671G → D in CAI84992 (PubMed:19468303).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei383 – 43149EGHPS…NTSIH → PVTGDHWHAEGELGCSFRTA SAAEEEPTYKLREKKRRKSP DCGRARWFL in isoform 2. 1 PublicationVSP_007881Add
BLAST
Alternative sequencei432 – 534103Missing in isoform 2. 1 PublicationVSP_022249Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP50429.
SMRiP50429. Positions 43-534.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000088964.

PTM databases

PhosphoSiteiP50429.

Proteomic databases

MaxQBiP50429.
PaxDbiP50429.
PRIDEiP50429.

Protocols and materials databases

DNASUi11881.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi11881.
KEGGimmu:11881.
UCSCiuc007rlo.1. mouse. [P50429-1]
uc011zcv.1. mouse. [P50429-2]

Organism-specific databases

CTDi411.
MGIiMGI:88075. Arsb.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_294584. CS/DS degradation.
REACT_320139. The activation of arylsulfatases.
REACT_339900. Glycosphingolipid metabolism.
SABIO-RKP50429.

Miscellaneous databases

NextBioi279911.
PROiP50429.
SOURCEiSearch...

Gene expression databases

BgeeiP50429.
CleanExiMM_ARSB.
GenevisibleiP50429. 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. 1 hit.
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] (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.
  6. "Cell-surface arylsulfatase A and B on sinusoidal endothelial cells, hepatocytes, and Kupffer cells in mammalian livers."
    Mitsunaga-Nakatsubo K., Kusunoki S., Kawakami H., Akasaka K., Akimoto Y.
    Med. Mol. Morphol. 42:63-69(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

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: June 24, 2015
This is version 133 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.