ARSB_RAT
ID ARSB_RAT Reviewed; 528 AA.
AC P50430; Q32KK1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Arylsulfatase B;
DE Short=ASB;
DE EC=3.1.6.12;
DE AltName: Full=N-acetylgalactosamine-4-sulfatase;
DE Short=G4S;
GN Name=Arsb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-55, AND DISEASE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8575749; DOI=10.1006/geno.1995.9962;
RA Kunieda T.;
RT "Mucopolysaccharidosis type VI in rats: isolation of cDNAs encoding
RT arylsulfatase B, chromosomal localization of the gene, and identification
RT of the mutation.";
RL Genomics 29:582-587(1995).
RN [3]
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).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=19536613; DOI=10.1007/s00795-009-0447-x;
RA Mitsunaga-Nakatsubo K., Kusunoki S., Kawakami H., Akasaka K., Akimoto Y.;
RT "Cell-surface arylsulfatase A and B on sinusoidal endothelial cells,
RT hepatocytes, and Kupffer cells in mammalian livers.";
RL Med. Mol. Morphol. 42:63-69(2009).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=24311516; DOI=10.1002/glia.22604;
RA Zhang X., Bhattacharyya S., Kusumo H., Goodlett C.R., Tobacman J.K.,
RA Guizzetti M.;
RT "Arylsulfatase B modulates neurite outgrowth via astrocyte chondroitin-4-
RT sulfate: dysregulation by ethanol.";
RL Glia 62:259-271(2014).
CC -!- FUNCTION: Removes sulfate groups from chondroitin-4-sulfate (C4S) and
CC regulates its degradation (PubMed:24311516). In the central nervous
CC system, is a regulator of neurite outgrowth and neuronal plasticity,
CC acting through the control of sulfate glycosaminoglycans and neurocan
CC levels (PubMed:24311516). Involved in the regulation of cell adhesion,
CC cell migration and invasion in colonic epithelium (By similarity).
CC {ECO:0000250|UniProtKB:P15848, ECO:0000269|PubMed:24311516}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 4-sulfate groups of the N-acetyl-D-
CC galactosamine 4-sulfate units of chondroitin sulfate and dermatan
CC sulfate.; EC=3.1.6.12;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by ethanol.
CC {ECO:0000269|PubMed:24311516}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome. Cell surface
CC {ECO:0000269|PubMed:19536613}.
CC -!- DISEASE: Note=Defects in Arsb are the cause of mucopolysaccharidosis
CC type VI (MPS-VI) (PubMed:8575749). {ECO:0000269|PubMed:8575749}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; AABR03012149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03015281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03016930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03021723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D49434; BAA08412.1; -; mRNA.
DR EMBL; BN000736; CAI84982.1; -; mRNA.
DR PIR; I54210; I54210.
DR RefSeq; NP_254278.1; NM_033443.1.
DR AlphaFoldDB; P50430; -.
DR SMR; P50430; -.
DR BioGRID; 247268; 1.
DR IntAct; P50430; 1.
DR STRING; 10116.ENSRNOP00000014860; -.
DR GlyGen; P50430; 6 sites.
DR PhosphoSitePlus; P50430; -.
DR jPOST; P50430; -.
DR PaxDb; P50430; -.
DR PRIDE; P50430; -.
DR Ensembl; ENSRNOT00000014860; ENSRNOP00000014860; ENSRNOG00000011150.
DR GeneID; 25227; -.
DR KEGG; rno:25227; -.
DR UCSC; RGD:2158; rat.
DR CTD; 411; -.
DR RGD; 2158; Arsb.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000158270; -.
DR HOGENOM; CLU_006332_10_1_1; -.
DR InParanoid; P50430; -.
DR OMA; CDPAATG; -.
DR OrthoDB; 515367at2759; -.
DR PhylomeDB; P50430; -.
DR TreeFam; TF314186; -.
DR BRENDA; 3.1.6.12; 5301.
DR BRENDA; 3.1.6.4; 5301.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-RNO-1663150; The activation of arylsulfatases.
DR Reactome; R-RNO-2024101; CS/DS degradation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P50430; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011150; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; P50430; baseline and differential.
DR Genevisible; P50430; RN.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0004065; F:arylsulfatase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003943; F:N-acetylgalactosamine-4-sulfatase activity; ISS:UniProtKB.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IDA:RGD.
DR GO; GO:0097065; P:anterior head development; ISO:RGD.
DR GO; GO:0006914; P:autophagy; IDA:RGD.
DR GO; GO:0007417; P:central nervous system development; IDA:RGD.
DR GO; GO:0061580; P:colon epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0010632; P:regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0051597; P:response to methylmercury; IDA:RGD.
DR GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR GO; GO:0009268; P:response to pH; IDA:RGD.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
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 Mucopolysaccharidosis; Reference proteome.
FT CHAIN 1..528
FT /note="Arylsulfatase B"
FT /id="PRO_0000192682"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 142
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 86
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 112..516
FT /evidence="ECO:0000250"
FT DISULFID 116..150
FT /evidence="ECO:0000250"
FT DISULFID 176..187
FT /evidence="ECO:0000250"
FT DISULFID 400..442
FT /evidence="ECO:0000250"
FT CONFLICT 56..57
FT /note="GF -> IR (in Ref. 1; AABR03012149)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..134
FT /note="YA -> SS (in Ref. 1; AABR03012149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 58959 MW; 1F02425E858E5A00 CRC64;
MGELSGCTGG SRAGGPGPRL PLLLLLLLWP ARASDAAPPP HVVFVLADDL GWNDLGFHGS
VIRTPHLDAL AAGGVVLDNY YVQPLCTPSR SQLLTGRYQI HMGLQHYLIM TCQPNCVPLD
EKLLPQLLKD AGYATHMVGK WHLGMYRKEC LPTRRGFDTY FGYLLGSEDY YTHEACAPIE
CLNGTRCALD LRDGEEPAKE YTDIYSTNIF TKRATTLIAN HPPEKPLFLY LAFQSVHDPL
QVPEEYMEPY DFIQDKHRRI YAGMVSLLDE AVGNVTKALK SRGLWNNTVL IFSTDNGGQT
RSGGNNWPLR GRKGTLWEGG IRGAGFVASP LLKQKGVKSR ELMHITDWLP TLVNLAGGST
HGTKPLDGFD VWETISEGSP SPRVELLLNI DPDFFDGLPC PGKNTTPEKN DSFPLEHSAF
NTSIHAGIRY KNWKLLTGYP GCGYWFPPPS QSNISEVPSV DSPTKTLWLF DINRDPEERH
DVSREHPHIV QNLLSRLQYY HEHSVPSYFP PLDPRCDPKG TGVWSPWM
