ID   ARSB_MOUSE              Reviewed;         534 AA.
AC   P50429; Q32KJ1; Q3TYV7; Q3U4Q6; Q8C404;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 176.
DE   RecName: Full=Arylsulfatase B;
DE            Short=ASB;
DE            EC=3.1.6.12;
DE   AltName: Full=N-acetylgalactosamine-4-sulfatase;
DE            Short=G4S;
DE   Flags: Precursor;
GN   Name=Arsb; Synonyms=As1, As1-s;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Inner ear, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 58-90 (ISOFORM 1).
RX   PubMed=1572648; DOI=10.1016/0888-7543(92)90306-d;
RA   Grompe M., Pieretti M., Caskey C.T., Ballabio A.;
RT   "The sulfatase gene family: cross-species PCR cloning using the MOPAC
RT   technique.";
RL   Genomics 12:755-760(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 137-388 (ISOFORM 1).
RX   PubMed=8710849; DOI=10.1073/pnas.93.16.8214;
RA   Evers M., Saftig P., Schmidt P., Hafner A., McLoghlin D.B., Schmahl W.,
RA   Hess B., von Figura K., Peters C.;
RT   "Targeted disruption of the arylsulfatase B gene results in mice resembling
RT   the phenotype of mucopolysaccharidosis VI.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:8214-8219(1996).
RN   [5]
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   [6]
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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Removes sulfate groups from chondroitin-4-sulfate (C4S) and
CC       regulates its degradation (By similarity). Involved in the regulation
CC       of cell adhesion, cell migration and invasion in colonic epithelium (By
CC       similarity). In the central nervous system, is a regulator of neurite
CC       outgrowth and neuronal plasticity, acting through the control of
CC       sulfate glycosaminoglycans and neurocan levels (By similarity).
CC       {ECO:0000250|UniProtKB:P15848, ECO:0000250|UniProtKB:P50430}.
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P50430}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19536613}. Cell
CC       surface {ECO:0000269|PubMed:19536613}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P50429-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P50429-2; Sequence=VSP_007881, VSP_022249;
CC   -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC       FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC       residue in eukaryotes, is critical for catalytic activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR   EMBL; AK083309; BAC38859.1; -; mRNA.
DR   EMBL; AK154098; BAE32375.1; -; mRNA.
DR   EMBL; AK158312; BAE34455.1; -; mRNA.
DR   EMBL; AC131739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC136976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M82877; AAA37261.1; -; mRNA.
DR   EMBL; X92096; CAA63067.1; -; mRNA.
DR   EMBL; BN000746; CAI84992.1; -; mRNA.
DR   CCDS; CCDS36749.1; -. [P50429-1]
DR   RefSeq; NP_033842.3; NM_009712.3.
DR   AlphaFoldDB; P50429; -.
DR   SMR; P50429; -.
DR   BioGRID; 198216; 9.
DR   STRING; 10090.ENSMUSP00000088964; -.
DR   GlyConnect; 2134; 4 N-Linked glycans (2 sites).
DR   GlyCosmos; P50429; 6 sites, 4 glycans.
DR   GlyGen; P50429; 6 sites, 4 N-linked glycans (2 sites).
DR   iPTMnet; P50429; -.
DR   PhosphoSitePlus; P50429; -.
DR   SwissPalm; P50429; -.
DR   EPD; P50429; -.
DR   jPOST; P50429; -.
DR   MaxQB; P50429; -.
DR   PaxDb; 10090-ENSMUSP00000088964; -.
DR   PeptideAtlas; P50429; -.
DR   ProteomicsDB; 281906; -. [P50429-1]
DR   ProteomicsDB; 281907; -. [P50429-2]
DR   Pumba; P50429; -.
DR   DNASU; 11881; -.
DR   GeneID; 11881; -.
DR   KEGG; mmu:11881; -.
DR   UCSC; uc007rlo.1; mouse. [P50429-1]
DR   UCSC; uc011zcv.1; mouse. [P50429-2]
DR   AGR; MGI:88075; -.
DR   CTD; 411; -.
DR   MGI; MGI:88075; Arsb.
DR   eggNOG; KOG3867; Eukaryota.
DR   InParanoid; P50429; -.
DR   OrthoDB; 2913702at2759; -.
DR   PhylomeDB; P50429; -.
DR   TreeFam; TF314186; -.
DR   BRENDA; 3.1.6.12; 3474.
DR   Reactome; R-MMU-1663150; The activation of arylsulfatases.
DR   Reactome; R-MMU-2024101; CS/DS degradation.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-9840310; Glycosphingolipid catabolism.
DR   SABIO-RK; P50429; -.
DR   BioGRID-ORCS; 11881; 1 hit in 80 CRISPR screens.
DR   ChiTaRS; Arsb; mouse.
DR   PRO; PR:P50429; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P50429; Protein.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0004065; F:arylsulfatase activity; IDA:MGI.
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:0043890; F:N-acetylgalactosamine-6-sulfatase activity; IMP:MGI.
DR   GO; GO:0008484; F:sulfuric ester hydrolase activity; ISO:MGI.
DR   GO; GO:0097065; P:anterior head development; IMP:MGI.
DR   GO; GO:0006914; P:autophagy; ISO:MGI.
DR   GO; GO:0030207; P:chondroitin sulfate catabolic process; ISO:MGI.
DR   GO; GO:0061580; P:colon epithelial cell migration; ISS:UniProtKB.
DR   GO; GO:0030209; P:dermatan sulfate catabolic process; IMP:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0010632; P:regulation of epithelial cell migration; ISS:UniProtKB.
DR   GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR   GO; GO:0051597; P:response to methylmercury; ISO:MGI.
DR   GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR   GO; GO:0009268; P:response to pH; ISO:MGI.
DR   CDD; cd16029; 4-S; 1.
DR   Gene3D; 3.30.1120.10; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR047115; ARSB.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR10342; ARYLSULFATASE; 1.
DR   PANTHER; PTHR10342:SF272; ARYLSULFATASE B; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
DR   PROSITE; PS00149; SULFATASE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW   Lysosome; Metal-binding; Reference proteome; Signal.
FT   SIGNAL          1..41
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..534
FT                   /note="Arylsulfatase B"
FT                   /id="PRO_0000033423"
FT   ACT_SITE        92
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         92
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   CARBOHYD        189
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        427
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        118..522
FT                   /evidence="ECO:0000250"
FT   DISULFID        122..156
FT                   /evidence="ECO:0000250"
FT   DISULFID        182..193
FT                   /evidence="ECO:0000250"
FT   DISULFID        406..448
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         383..431
FT                   /note="EGHPSPRVELLHNIDQDFFDGLPCPGKNMTPAKDDSFPLEHSAFNTSIH ->
FT                   PVTGDHWHAEGELGCSFRTASAAEEEPTYKLREKKRRKSPDCGRARWFL (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_007881"
FT   VAR_SEQ         432..534
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022249"
FT   CONFLICT        60
FT                   /note="D -> A (in Ref. 3; AAA37261)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        352
FT                   /note="T -> S (in Ref. 1; BAE34455 and 4; CAA63067)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        467
FT                   /note="G -> D (in Ref. 2; CAI84992)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   534 AA;  59647 MW;  78DAB2D65C71E97D CRC64;
     MGKLSPCTGR SRPGGPGPQL PLLLLLLQLL LLLLSPARAS GATQPPHVVF VLADDLGWND
     LGFHGSVIRT PHLDALAAGG VVLDNYYVQP LCTPSRSQLL TGRYQIHLGL QHYLIMTCQP
     SCVPLDEKLL PQLLKEAGYA THMVGKWHLG MYRKECLPTR RGFDTYFGYL LGSEDYYTHE
     ACAPIESLNG TRCALDLRDG EEPAKEYNNI YSTNIFTKRA TTVIANHPPE KPLFLYLAFQ
     SVHDPLQVPE EYMEPYGFIQ DKHRRIYAGM VSLMDEAVGN VTKALKSHGL WNNTVFIFST
     DNGGQTRSGG NNWPLRGRKG TLWEGGIRGT GFVASPLLKQ KGVKSRELMH ITDWLPTLVD
     LAGGSTNGTK PLDGFNMWKT ISEGHPSPRV ELLHNIDQDF FDGLPCPGKN MTPAKDDSFP
     LEHSAFNTSI HAGIRYKNWK LLTGHPGCGY WFPPPSQSNV SEIPPVGPPT KTLWLFDINQ
     DPEERHDVSR EHPHIVQNLL SRLQYYHEHS VPSHFPPLDP RCDPKSTGVW SPWM
//