ARSB_HUMAN
ID ARSB_HUMAN Reviewed; 533 AA.
AC P15848; B2RC20; Q8N322; Q9UDI9;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 212.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 103-119;
RP 135-158; 161-168; 286-295; 319-337; 379-387; 389-410; 440-450; 490-501;
RP 508-520 AND 525-533.
RC TISSUE=Placenta, and Testis;
RX PubMed=2303452; DOI=10.1016/s0021-9258(19)39778-9;
RA Peters C., Schmidt B., Rommerskirch W., Rupp K., Zuehlsdorf M., Vingron M.,
RA Meyer H.E., Pohlmann R., von Figura K.;
RT "Phylogenetic conservation of arylsulfatases. cDNA cloning and expression
RT of human arylsulfatase B.";
RL J. Biol. Chem. 265:3374-3381(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1968043; DOI=10.1016/0888-7543(90)90460-c;
RA Schuchman E.H., Jackson C.E., Desnick R.J.;
RT "Human arylsulfatase B: MOPAC cloning, nucleotide sequence of a full-length
RT cDNA, and regions of amino acid identity with arylsulfatases A and C.";
RL Genomics 6:149-158(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-358.
RX PubMed=7687847; DOI=10.1515/bchm3.1993.374.1-6.327;
RA Modaressi S., Rupp K., von Figura K., Peters C.;
RT "Structure of the human arylsulfatase B gene.";
RL Biol. Chem. Hoppe-Seyler 374:327-335(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-358.
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
RX PubMed=1930244;
RA Litjens T., Morris C.P., Gibson G.J., Beckmann K.R., Hopwood J.J.;
RT "Human N-acetylgalactosamine-4-sulphatase: protein maturation and isolation
RT of genomic clones.";
RL Biochem. Int. 24:209-215(1991).
RN [9]
RP PROTEIN SEQUENCE OF 41-55; 424-454 AND 466-483.
RC TISSUE=Placenta;
RX PubMed=1390929; DOI=10.1016/0167-4838(92)90051-e;
RA Kobayashi T., Honke K., Jin T., Gasa S., Miyazaki T., Makita A.;
RT "Components and proteolytic processing sites of arylsulfatase B from human
RT placenta.";
RL Biochim. Biophys. Acta 1159:243-247(1992).
RN [10]
RP OXOALANINE AT CYS-91, IDENTIFICATION BY MASS SPECTROMETRY, AND ABSENCE OF
RP OXOALANINE IN MSD.
RX PubMed=7628016; DOI=10.1016/0092-8674(95)90314-3;
RA Schmidt B., Selmer T., Ingendoh A., von Figura K.;
RT "A novel amino acid modification in sulfatases that is defective in
RT multiple sulfatase deficiency.";
RL Cell 82:271-278(1995).
RN [11]
RP INVOLVEMENT IN MSD.
RX PubMed=15146462; DOI=10.1002/humu.20040;
RA Cosma M.P., Pepe S., Parenti G., Settembre C., Annunziata I.,
RA Wade-Martins R., Domenico C.D., Natale P.D., Mankad A., Cox B., Uziel G.,
RA Mancini G.M., Zammarchi E., Donati M.A., Kleijer W.J., Filocamo M.,
RA Carrozzo R., Carella M., Ballabio A.;
RT "Molecular and functional analysis of SUMF1 mutations in multiple sulfatase
RT deficiency.";
RL Hum. Mutat. 23:576-581(2004).
RN [12]
RP FUNCTION.
RX PubMed=19306108; DOI=10.1007/s10585-009-9253-z;
RA Bhattacharyya S., Tobacman J.K.;
RT "Arylsulfatase B regulates colonic epithelial cell migration by effects on
RT MMP9 expression and RhoA activation.";
RL Clin. Exp. Metastasis 26:535-545(2009).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-366.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9032078; DOI=10.1016/s0969-2126(97)00185-8;
RA Bond C.S., Clements P.R., Ashby S.J., Collyer C.A., Harrop S.J.,
RA Hopwood J.J., Guss J.M.;
RT "Structure of a human lysosomal sulfatase.";
RL Structure 5:277-289(1997).
RN [16]
RP VARIANT MPS6 VAL-137, AND VARIANT MET-376.
RX PubMed=1718978; DOI=10.1016/s0021-9258(18)54649-4;
RA Wicker G., Prill V., Brooks D.A., Gibson G.J., Hopwood J.J., von Figura K.,
RA Peters C.;
RT "Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). An intermediate
RT clinical phenotype caused by substitution of valine for glycine at position
RT 137 of arylsulfatase B.";
RL J. Biol. Chem. 266:21386-21391(1991).
RN [17]
RP VARIANTS MPS6 ARG-117; PRO-236 AND TYR-405.
RX PubMed=1550123;
RA Jin W.-D., Jackson C.E., Desnick R.J., Schuchman E.H.;
RT "Mucopolysaccharidosis type VI: identification of three mutations in the
RT arylsulfatase B gene of patients with the severe and mild phenotypes
RT provides molecular evidence for genetic heterogeneity.";
RL Am. J. Hum. Genet. 50:795-800(1992).
RN [18]
RP VARIANTS MPS6 ARG-144; ARG-192; PRO-321 AND TYR-521, AND CHARACTERIZATION
RP OF VARIANTS MPS6.
RX PubMed=8116615;
RA Isbrandt D., Arlt G., Brooks D.A., Hopwood J.J., von Figura K., Peters C.;
RT "Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome): six unique
RT arylsulfatase B gene alleles causing variable disease phenotypes.";
RL Am. J. Hum. Genet. 54:454-463(1994).
RN [19]
RP VARIANTS MPS6 TRP-152 AND GLN-160.
RX PubMed=8125475; DOI=10.1007/bf00212019;
RA Voskoboeva E., Isbrandt D., von Figura K., Krasnopolskaya X., Peters C.;
RT "Four novel mutant alleles of the arylsulfatase B gene in two patients with
RT intermediate form of mucopolysaccharidosis VI (Maroteaux-Lamy syndrome).";
RL Hum. Genet. 93:259-264(1994).
RN [20]
RP VARIANTS MPS6 ILE-142; ARG-146; LEU-146 AND SER-146.
RX PubMed=8541342; DOI=10.1016/0925-4439(95)00070-4;
RA Simonaro C.M., Schuchman E.H.;
RT "N-acetylgalactosamine-4-sulfatase: identification of four new mutations
RT within the conserved sulfatase region causing mucopolysaccharidosis type
RT VI.";
RL Biochim. Biophys. Acta 1272:129-132(1995).
RN [21]
RP VARIANTS MPS6 MET-92; GLN-95; CYS-210; PRO-393 AND PRO-498.
RX PubMed=8651289;
RA Litjens T., Brooks D.A., Peters C., Gibson G.J., Hopwood J.J.;
RT "Identification, expression, and biochemical characterization of N-
RT acetylgalactosamine-4-sulfatase mutations and relationship with clinical
RT phenotype in MPS6 patients.";
RL Am. J. Hum. Genet. 58:1127-1134(1996).
RN [22]
RP VARIANT MPS-IV ARG-302.
RX PubMed=10206678;
RX DOI=10.1002/(sici)1098-1004(1998)11:5<410::aid-humu9>3.0.co;2-q;
RA Villani G.R.D., Balzano N., Di Natale P.;
RT "Two novel mutations of the arylsulfatase B gene in two Italian patients
RT with severe form of mucopolysaccharidosis.";
RL Hum. Mutat. 11:410-410(1998).
RN [23]
RP VARIANT MET-358.
RX PubMed=9582121; DOI=10.1126/science.280.5366.1077;
RA Wang D.G., Fan J.-B., Siao C.-J., Berno A., Young P., Sapolsky R.,
RA Ghandour G., Perkins N., Winchester E., Spencer J., Kruglyak L., Stein L.,
RA Hsie L., Topaloglou T., Hubbell E., Robinson E., Mittmann M., Morris M.S.,
RA Shen N., Kilburn D., Rioux J., Nusbaum C., Rozen S., Hudson T.J.,
RA Lipshutz R., Chee M., Lander E.S.;
RT "Large-scale identification, mapping, and genotyping of single-nucleotide
RT polymorphisms in the human genome.";
RL Science 280:1077-1082(1998).
RN [24]
RP VARIANTS MPS6 PHE-65; HIS-116; GLN-315 AND ARG-531, AND VARIANT MET-358.
RX PubMed=10036316; DOI=10.1016/s0925-4439(98)00099-4;
RA Villani G.R.D., Balzano N., Vitale D., Saviano M., Pavone V., Di Natale P.;
RT "Maroteaux-Lamy syndrome: five novel mutations and their structural
RT localization.";
RL Biochim. Biophys. Acta 1453:185-192(1999).
RN [25]
RP VARIANTS MPS6 ARG-192 AND ARG-239.
RX PubMed=10738004;
RX DOI=10.1002/(sici)1098-1004(200004)15:4<389::aid-humu31>3.0.co;2-0;
RA Wu J.-Y., Yang C.-F., Lee C.-C., Chang J.-G., Tsai F.-J.;
RT "A novel mutation (Q239R) identified in a Taiwan Chinese patient with type
RT VI mucopolysaccharidosis (Maroteaux-Lamy syndrome).";
RL Hum. Mutat. 15:389-390(2000).
RN [26]
RP VARIANTS MPS6 ARG-192; ARG-239 AND LEU-399, AND VARIANT MET-358.
RX PubMed=11802522;
RA Yang C.-F., Wu J.-Y., Lin S.-P., Tsai F.-J.;
RT "Mucopolysaccharidosis type VI: report of two Taiwanese patients and
RT identification of one novel mutation.";
RL J. Formos. Med. Assoc. 100:820-823(2001).
RN [27]
RP VARIANTS MPS6 TYR-86 DEL; CYS-210; PRO-236; CYS-312; GLN-315; PRO-321 AND
RP GLY-484, VARIANTS MET-358; MET-376 AND ASN-384, AND CHARACTERIZATION OF
RP VARIANTS MPS6 TYR-86 DEL AND CYS-312.
RX PubMed=14974081; DOI=10.1002/humu.10313;
RA Karageorgos L., Harmatz P., Simon J., Pollard A., Clements P.R.,
RA Brooks D.A., Hopwood J.J.;
RT "Mutational analysis of mucopolysaccharidosis type VI patients undergoing a
RT trial of enzyme replacement therapy.";
RL Hum. Mutat. 23:229-233(2004).
RN [28]
RP VARIANTS MPS6 ARG-82 AND GLN-315, AND VARIANT ASN-384.
RX PubMed=19259130; DOI=10.1038/ejhg.2009.19;
RA Zanetti A., Ferraresi E., Picci L., Filocamo M., Parini R., Rosano C.,
RA Tomanin R., Scarpa M.;
RT "Segregation analysis in a family at risk for the Maroteaux-Lamy syndrome
RT conclusively reveals c.1151G>A (p.S384N) as to be a polymorphism.";
RL Eur. J. Hum. Genet. 17:1160-1164(2009).
CC -!- FUNCTION: Removes sulfate groups from chondroitin-4-sulfate (C4S) and
CC regulates its degradation (PubMed:19306108). Involved in the regulation
CC of cell adhesion, cell migration and invasion in colonic epithelium
CC (PubMed:19306108). In the central nervous system, is a regulator of
CC neurite outgrowth and neuronal plasticity, acting through the control
CC of sulfate glycosaminoglycans and neurocan levels (By similarity).
CC {ECO:0000250|UniProtKB:P50430, ECO:0000269|PubMed:19306108}.
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;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by ethanol (By similarity).
CC {ECO:0000250|UniProtKB:P50430}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P50429}. Cell
CC surface {ECO:0000250|UniProtKB:P50429}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15848-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15848-2; Sequence=VSP_042721;
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. This post-
CC translational modification is severely defective in multiple sulfatase
CC deficiency (MSD). {ECO:0000269|PubMed:7628016}.
CC -!- DISEASE: Mucopolysaccharidosis 6 (MPS6) [MIM:253200]: A form of
CC mucopolysaccharidosis, a group of lysosomal storage diseases
CC characterized by defective degradation of glycosaminoglycans, resulting
CC in their excessive accumulation and secretion. The diseases are
CC progressive and often display a wide spectrum of clinical severity.
CC MPS6 is an autosomal recessive form characterized by intracellular
CC accumulation of dermatan sulfate. Clinical features can include
CC abnormal growth, short stature, stiff joints, skeletal malformations,
CC corneal clouding, hepatosplenomegaly, and cardiac abnormalities.
CC {ECO:0000269|PubMed:10036316, ECO:0000269|PubMed:10738004,
CC ECO:0000269|PubMed:11802522, ECO:0000269|PubMed:14974081,
CC ECO:0000269|PubMed:1550123, ECO:0000269|PubMed:1718978,
CC ECO:0000269|PubMed:19259130, ECO:0000269|PubMed:8116615,
CC ECO:0000269|PubMed:8125475, ECO:0000269|PubMed:8541342,
CC ECO:0000269|PubMed:8651289}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Multiple sulfatase deficiency (MSD) [MIM:272200]: A clinically
CC and biochemically heterogeneous disorder caused by the simultaneous
CC impairment of all sulfatases, due to defective post-translational
CC modification and activation. It combines features of individual
CC sulfatase deficiencies such as metachromatic leukodystrophy,
CC mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus,
CC ichthyosis, neurologic deterioration and developmental delay.
CC {ECO:0000269|PubMed:15146462}. Note=The protein represented in this
CC entry is involved in disease pathogenesis. Arylsulfatase B activity is
CC impaired in multiple sulfatase deficiency due to mutations in SUMF1.
CC SUMF1 mutations result in defective post-translational modification of
CC ARSB at residue Cys-91 that is not converted to 3-oxoalanine.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; J05225; AAA51784.1; -; mRNA.
DR EMBL; M32373; AAA51779.1; -; mRNA.
DR EMBL; X72735; CAA51272.1; -; Genomic_DNA.
DR EMBL; X72736; CAA51272.1; JOINED; Genomic_DNA.
DR EMBL; X72737; CAA51272.1; JOINED; Genomic_DNA.
DR EMBL; X72738; CAA51272.1; JOINED; Genomic_DNA.
DR EMBL; X72739; CAA51272.1; JOINED; Genomic_DNA.
DR EMBL; X72740; CAA51272.1; JOINED; Genomic_DNA.
DR EMBL; X72741; CAA51272.1; JOINED; Genomic_DNA.
DR EMBL; X72742; CAA51272.1; JOINED; Genomic_DNA.
DR EMBL; AK314903; BAG37417.1; -; mRNA.
DR EMBL; AC020937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95822.1; -; Genomic_DNA.
DR EMBL; BC029051; AAH29051.1; -; mRNA.
DR EMBL; S57777; AAB19988.1; -; Genomic_DNA.
DR CCDS; CCDS4043.1; -. [P15848-1]
DR CCDS; CCDS43334.1; -. [P15848-2]
DR PIR; S35990; KJHUAB.
DR RefSeq; NP_000037.2; NM_000046.3. [P15848-1]
DR RefSeq; NP_942002.1; NM_198709.2. [P15848-2]
DR RefSeq; XP_011541692.1; XM_011543390.1. [P15848-1]
DR PDB; 1FSU; X-ray; 2.50 A; A=42-533.
DR PDBsum; 1FSU; -.
DR AlphaFoldDB; P15848; -.
DR SMR; P15848; -.
DR BioGRID; 106904; 42.
DR IntAct; P15848; 12.
DR STRING; 9606.ENSP00000264914; -.
DR ChEMBL; CHEMBL2399; -.
DR DrugBank; DB09301; Chondroitin sulfate.
DR GlyConnect; 1016; 3 N-Linked glycans (3 sites).
DR GlyGen; P15848; 7 sites, 3 N-linked glycans (3 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P15848; -.
DR PhosphoSitePlus; P15848; -.
DR BioMuta; ARSB; -.
DR EPD; P15848; -.
DR jPOST; P15848; -.
DR MassIVE; P15848; -.
DR MaxQB; P15848; -.
DR PaxDb; P15848; -.
DR PeptideAtlas; P15848; -.
DR PRIDE; P15848; -.
DR ProteomicsDB; 53228; -. [P15848-1]
DR ProteomicsDB; 53229; -. [P15848-2]
DR Antibodypedia; 24535; 315 antibodies from 37 providers.
DR DNASU; 411; -.
DR Ensembl; ENST00000264914.10; ENSP00000264914.4; ENSG00000113273.17. [P15848-1]
DR Ensembl; ENST00000396151.7; ENSP00000379455.3; ENSG00000113273.17. [P15848-2]
DR GeneID; 411; -.
DR KEGG; hsa:411; -.
DR MANE-Select; ENST00000264914.10; ENSP00000264914.4; NM_000046.5; NP_000037.2.
DR UCSC; uc003kfq.5; human. [P15848-1]
DR CTD; 411; -.
DR DisGeNET; 411; -.
DR GeneCards; ARSB; -.
DR HGNC; HGNC:714; ARSB.
DR HPA; ENSG00000113273; Low tissue specificity.
DR MalaCards; ARSB; -.
DR MIM; 253200; phenotype.
DR MIM; 272200; phenotype.
DR MIM; 611542; gene.
DR neXtProt; NX_P15848; -.
DR OpenTargets; ENSG00000113273; -.
DR Orphanet; 276212; Mucopolysaccharidosis type 6, rapidly progressing.
DR Orphanet; 276223; Mucopolysaccharidosis type 6, slowly progressing.
DR PharmGKB; PA25006; -.
DR VEuPathDB; HostDB:ENSG00000113273; -.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000158270; -.
DR HOGENOM; CLU_006332_10_1_1; -.
DR InParanoid; P15848; -.
DR OMA; CDPAATG; -.
DR PhylomeDB; P15848; -.
DR TreeFam; TF314186; -.
DR BioCyc; MetaCyc:HS03665-MON; -.
DR BRENDA; 3.1.6.1; 2681.
DR BRENDA; 3.1.6.12; 2681.
DR PathwayCommons; P15848; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-HSA-1663150; The activation of arylsulfatases.
DR Reactome; R-HSA-2024101; CS/DS degradation.
DR Reactome; R-HSA-2206285; MPS VI - Maroteaux-Lamy syndrome.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SABIO-RK; P15848; -.
DR SignaLink; P15848; -.
DR BioGRID-ORCS; 411; 16 hits in 1079 CRISPR screens.
DR ChiTaRS; ARSB; human.
DR EvolutionaryTrace; P15848; -.
DR GenomeRNAi; 411; -.
DR Pharos; P15848; Tbio.
DR PRO; PR:P15848; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P15848; protein.
DR Bgee; ENSG00000113273; Expressed in calcaneal tendon and 119 other tissues.
DR ExpressionAtlas; P15848; baseline and differential.
DR Genevisible; P15848; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; TAS:ProtInc.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0004065; F:arylsulfatase activity; TAS:ProtInc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003943; F:N-acetylgalactosamine-4-sulfatase activity; IDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0061580; P:colon epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0007041; P:lysosomal transport; TAS:ProtInc.
DR GO; GO:0007040; P:lysosome organization; TAS:ProtInc.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0010632; P:regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0051597; P:response to methylmercury; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0009268; P:response to pH; IEA:Ensembl.
DR DisProt; DP02670; -.
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 3D-structure; Alternative splicing; Calcium; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein; Hydrolase; Ichthyosis;
KW Leukodystrophy; Lysosome; Metachromatic leukodystrophy; Metal-binding;
KW Mucopolysaccharidosis; Reference proteome; Signal.
FT SIGNAL 1..36
FT /note="Or 38"
FT /evidence="ECO:0000255"
FT CHAIN 37..533
FT /note="Arylsulfatase B"
FT /id="PRO_0000033421"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:7628016"
FT ACT_SITE 147
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000269|PubMed:7628016"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 91
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000269|PubMed:7628016"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..521
FT DISULFID 121..155
FT DISULFID 181..192
FT DISULFID 405..447
FT VAR_SEQ 405..533
FT /note="CPRNSMAPAKDDSSLPEYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQ
FT YNVSEIPSSDPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFP
FT AQDPRCDPKATGVWGPWM -> YWPECSLLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042721"
FT VARIANT 65
FT /note="S -> F (in MPS6; intermediate form;
FT dbSNP:rs1233331806)"
FT /evidence="ECO:0000269|PubMed:10036316"
FT /id="VAR_019017"
FT VARIANT 82
FT /note="L -> R (in MPS6; dbSNP:rs749465732)"
FT /evidence="ECO:0000269|PubMed:19259130"
FT /id="VAR_080270"
FT VARIANT 86
FT /note="Missing (in MPS6; severe form; low protein levels
FT and activity; dbSNP:rs969231209)"
FT /evidence="ECO:0000269|PubMed:14974081"
FT /id="VAR_019018"
FT VARIANT 92
FT /note="T -> M (in MPS6; mild form; dbSNP:rs751010538)"
FT /evidence="ECO:0000269|PubMed:8651289"
FT /id="VAR_007294"
FT VARIANT 95
FT /note="R -> Q (in MPS6; mild/severe form;
FT dbSNP:rs118203942)"
FT /evidence="ECO:0000269|PubMed:8651289"
FT /id="VAR_007295"
FT VARIANT 116
FT /note="P -> H (in MPS6; severe form; dbSNP:rs775780931)"
FT /evidence="ECO:0000269|PubMed:10036316"
FT /id="VAR_019019"
FT VARIANT 117
FT /note="C -> R (in MPS6; severe form; dbSNP:rs118203939)"
FT /evidence="ECO:0000269|PubMed:1550123"
FT /id="VAR_007296"
FT VARIANT 137
FT /note="G -> V (in MPS6; intermediate form;
FT dbSNP:rs118203938)"
FT /evidence="ECO:0000269|PubMed:1718978"
FT /id="VAR_007297"
FT VARIANT 142
FT /note="M -> I (in MPS6; dbSNP:rs1554088053)"
FT /evidence="ECO:0000269|PubMed:8541342"
FT /id="VAR_019020"
FT VARIANT 144
FT /note="G -> R (in MPS6; severe form; severe reduction of
FT activity; dbSNP:rs746206847)"
FT /evidence="ECO:0000269|PubMed:8116615"
FT /id="VAR_019021"
FT VARIANT 146
FT /note="W -> L (in MPS6; dbSNP:rs1554088034)"
FT /evidence="ECO:0000269|PubMed:8541342"
FT /id="VAR_019022"
FT VARIANT 146
FT /note="W -> R (in MPS6; dbSNP:rs1554088037)"
FT /evidence="ECO:0000269|PubMed:8541342"
FT /id="VAR_019023"
FT VARIANT 146
FT /note="W -> S (in MPS6; dbSNP:rs1554088034)"
FT /evidence="ECO:0000269|PubMed:8541342"
FT /id="VAR_019024"
FT VARIANT 152
FT /note="R -> W (in MPS6; intermediate form;
FT dbSNP:rs991104525)"
FT /evidence="ECO:0000269|PubMed:8125475"
FT /id="VAR_007298"
FT VARIANT 160
FT /note="R -> Q (in MPS6; intermediate form;
FT dbSNP:rs1196325597)"
FT /evidence="ECO:0000269|PubMed:8125475"
FT /id="VAR_007299"
FT VARIANT 192
FT /note="C -> R (in MPS6; mild form; severe reduction of
FT activity; dbSNP:rs1554087423)"
FT /evidence="ECO:0000269|PubMed:10738004,
FT ECO:0000269|PubMed:11802522, ECO:0000269|PubMed:8116615"
FT /id="VAR_019025"
FT VARIANT 210
FT /note="Y -> C (in MPS6; mild/intermediate;
FT dbSNP:rs118203943)"
FT /evidence="ECO:0000269|PubMed:14974081,
FT ECO:0000269|PubMed:8651289"
FT /id="VAR_007300"
FT VARIANT 236
FT /note="L -> P (in MPS6; mild form; dbSNP:rs118203940)"
FT /evidence="ECO:0000269|PubMed:14974081,
FT ECO:0000269|PubMed:1550123"
FT /id="VAR_007301"
FT VARIANT 239
FT /note="Q -> R (in MPS6; dbSNP:rs1554086431)"
FT /evidence="ECO:0000269|PubMed:10738004,
FT ECO:0000269|PubMed:11802522"
FT /id="VAR_019026"
FT VARIANT 302
FT /note="G -> R (in MPS6; severe form; dbSNP:rs779378413)"
FT /evidence="ECO:0000269|PubMed:10206678"
FT /id="VAR_007302"
FT VARIANT 312
FT /note="W -> C (in MPS6; severe form; loss of activity;
FT dbSNP:rs759384989)"
FT /evidence="ECO:0000269|PubMed:14974081"
FT /id="VAR_019027"
FT VARIANT 315
FT /note="R -> Q (in MPS6; intermediate form;
FT dbSNP:rs727503809)"
FT /evidence="ECO:0000269|PubMed:10036316,
FT ECO:0000269|PubMed:14974081, ECO:0000269|PubMed:19259130"
FT /id="VAR_019028"
FT VARIANT 321
FT /note="L -> P (in MPS6; intermediate form; severe reduction
FT of activity; dbSNP:rs1554079320)"
FT /evidence="ECO:0000269|PubMed:14974081,
FT ECO:0000269|PubMed:8116615"
FT /id="VAR_019029"
FT VARIANT 358
FT /note="V -> L (in dbSNP:rs1065757)"
FT /id="VAR_061883"
FT VARIANT 358
FT /note="V -> M (in dbSNP:rs1065757)"
FT /evidence="ECO:0000269|PubMed:10036316,
FT ECO:0000269|PubMed:11802522, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:14974081, ECO:0000269|PubMed:7687847,
FT ECO:0000269|PubMed:9582121"
FT /id="VAR_016061"
FT VARIANT 376
FT /note="V -> M (in dbSNP:rs1071598)"
FT /evidence="ECO:0000269|PubMed:14974081,
FT ECO:0000269|PubMed:1718978"
FT /id="VAR_007303"
FT VARIANT 384
FT /note="S -> N (in dbSNP:rs25414)"
FT /evidence="ECO:0000269|PubMed:14974081,
FT ECO:0000269|PubMed:19259130"
FT /id="VAR_019030"
FT VARIANT 393
FT /note="H -> P (in MPS6; mild/severe form;
FT dbSNP:rs118203944)"
FT /evidence="ECO:0000269|PubMed:8651289"
FT /id="VAR_007304"
FT VARIANT 399
FT /note="F -> L (in MPS6; dbSNP:rs200793396)"
FT /evidence="ECO:0000269|PubMed:11802522"
FT /id="VAR_019031"
FT VARIANT 405
FT /note="C -> Y (in MPS6; mild form; dbSNP:rs118203941)"
FT /evidence="ECO:0000269|PubMed:1550123"
FT /id="VAR_007305"
FT VARIANT 484
FT /note="R -> G (in MPS6; dbSNP:rs201101343)"
FT /evidence="ECO:0000269|PubMed:14974081"
FT /id="VAR_019032"
FT VARIANT 498
FT /note="L -> P (in MPS6; mild/severe form;
FT dbSNP:rs774358117)"
FT /evidence="ECO:0000269|PubMed:8651289"
FT /id="VAR_007306"
FT VARIANT 521
FT /note="C -> Y (in MPS6; severe form; severe reduction of
FT activity; dbSNP:rs1554069661)"
FT /evidence="ECO:0000269|PubMed:8116615"
FT /id="VAR_019033"
FT VARIANT 531
FT /note="P -> R (in MPS6; mild form; dbSNP:rs1554069659)"
FT /evidence="ECO:0000269|PubMed:10036316"
FT /id="VAR_019034"
FT CONFLICT 153
FT /note="K -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 408..410
FT /note="NSM -> SPC (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:1FSU"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:1FSU"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 261..286
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:1FSU"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:1FSU"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:1FSU"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:1FSU"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 492..507
FT /evidence="ECO:0007829|PDB:1FSU"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:1FSU"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:1FSU"
SQ SEQUENCE 533 AA; 59687 MW; 5983FB6911C4789A CRC64;
MGPRGAASLP RGPGPRRLLL PVVLPLLLLL LLAPPGSGAG ASRPPHLVFL LADDLGWNDV
GFHGSRIRTP HLDALAAGGV LLDNYYTQPL CTPSRSQLLT GRYQIRTGLQ HQIIWPCQPS
CVPLDEKLLP QLLKEAGYTT HMVGKWHLGM YRKECLPTRR GFDTYFGYLL GSEDYYSHER
CTLIDALNVT RCALDFRDGE EVATGYKNMY STNIFTKRAI ALITNHPPEK PLFLYLALQS
VHEPLQVPEE YLKPYDFIQD KNRHHYAGMV SLMDEAVGNV TAALKSSGLW NNTVFIFSTD
NGGQTLAGGN NWPLRGRKWS LWEGGVRGVG FVASPLLKQK GVKNRELIHI SDWLPTLVKL
ARGHTNGTKP LDGFDVWKTI SEGSPSPRIE LLHNIDPNFV DSSPCPRNSM APAKDDSSLP
EYSAFNTSVH AAIRHGNWKL LTGYPGCGYW FPPPSQYNVS EIPSSDPPTK TLWLFDIDRD
PEERHDLSRE YPHIVTKLLS RLQFYHKHSV PVYFPAQDPR CDPKATGVWG PWM
