ARSB_MOUSE
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 03-AUG-2022, entry version 170.
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 GlyGen; P50429; 6 sites, 4 N-linked glycans (2 sites).
DR PhosphoSitePlus; P50429; -.
DR EPD; P50429; -.
DR jPOST; P50429; -.
DR MaxQB; P50429; -.
DR PaxDb; P50429; -.
DR PeptideAtlas; P50429; -.
DR PRIDE; P50429; -.
DR ProteomicsDB; 281906; -. [P50429-1]
DR ProteomicsDB; 281907; -. [P50429-2]
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 CTD; 411; -.
DR MGI; MGI:88075; Arsb.
DR eggNOG; KOG3867; Eukaryota.
DR InParanoid; P50429; -.
DR OrthoDB; 515367at2759; -.
DR PhylomeDB; P50429; -.
DR TreeFam; TF314186; -.
DR BRENDA; 3.1.6.12; 3474.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
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 SABIO-RK; P50429; -.
DR BioGRID-ORCS; 11881; 1 hit in 75 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:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO: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: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:0007417; P:central nervous system development; ISO:MGI.
DR GO; GO:0061580; P:colon epithelial cell migration; ISS:UniProtKB.
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 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 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
