ARSK_RAT
ID ARSK_RAT Reviewed; 563 AA.
AC Q32KJ2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Arylsulfatase K;
DE Short=ASK;
DE EC=3.1.6.1 {ECO:0000250|UniProtKB:Q6UWY0};
DE AltName: Full=Glucuronate-2-sulfatase;
DE EC=3.1.6.18 {ECO:0000250|UniProtKB:Q6UWY0};
DE Flags: Precursor;
GN Name=Arsk;
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 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).
CC -!- FUNCTION: Catalyzes the hydrolysis of pseudosubstrates such as p-
CC nitrocatechol sulfate and p-nitrophenyl sulfate (By similarity).
CC Catalyzes the hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-
CC glucuronate residues of chondroitin sulfate, heparin and heparitin
CC sulfate (By similarity). Acts selectively on 2-sulfoglucuronate and
CC lacks activity against 2-sulfoiduronate (By similarity).
CC {ECO:0000250|UniProtKB:Q6UWY0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aryl sulfate + H2O = a phenol + H(+) + sulfate;
CC Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317; EC=3.1.6.1;
CC Evidence={ECO:0000250|UniProtKB:Q6UWY0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-
CC glucuronate residues of chondroitin sulfate, heparin and heparitin
CC sulfate.; EC=3.1.6.18; Evidence={ECO:0000250|UniProtKB:Q6UWY0};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P15289};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15289};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6UWY0}. Lysosome
CC {ECO:0000250|UniProtKB:Q6UWY0}.
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|UniProtKB:Q6UWY0}.
CC -!- PTM: The 75-kDa precursor undergoes proteolytic processing to yield a
CC 23 kDa form. {ECO:0000250|UniProtKB:Q6UWY0}.
CC -!- PTM: N-glycosylated with both high mannose and complex type sugars.
CC {ECO:0000250|UniProtKB:Q6UWY0}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; AABR03012430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03016345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03016385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000745; CAI84991.1; -; mRNA.
DR RefSeq; NP_001041382.1; NM_001047917.1.
DR AlphaFoldDB; Q32KJ2; -.
DR SMR; Q32KJ2; -.
DR STRING; 10116.ENSRNOP00000029855; -.
DR GlyGen; Q32KJ2; 6 sites.
DR PaxDb; Q32KJ2; -.
DR PRIDE; Q32KJ2; -.
DR Ensembl; ENSRNOT00000029250; ENSRNOP00000029855; ENSRNOG00000026937.
DR GeneID; 365619; -.
DR KEGG; rno:365619; -.
DR UCSC; RGD:1310182; rat.
DR CTD; 153642; -.
DR RGD; 1310182; Arsk.
DR eggNOG; KOG3731; Eukaryota.
DR GeneTree; ENSGT00940000158982; -.
DR HOGENOM; CLU_006332_6_0_1; -.
DR InParanoid; Q32KJ2; -.
DR OMA; YGWAVNW; -.
DR OrthoDB; 349944at2759; -.
DR PhylomeDB; Q32KJ2; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-RNO-1663150; The activation of arylsulfatases.
DR PRO; PR:Q32KJ2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000026937; Expressed in ovary and 19 other tissues.
DR Genevisible; Q32KJ2; RN.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0004065; F:arylsulfatase activity; ISS:UniProtKB.
DR GO; GO:0015024; F:glucuronate-2-sulfatase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 2: Evidence at transcript level;
KW Calcium; Glycoprotein; Hydrolase; Lysosome; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..563
FT /note="Arylsulfatase K"
FT /id="PRO_0000356287"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 80
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:Q6UWY0"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 563 AA; 64273 MW; 1B784F33678AC5A8 CRC64;
MLLLLVSVIV ALALVAPAPE TQEKRLQVAQ APNVVLVASD SFDGRLTFQP GSQVVKLPFI
NFMRARGTTF LNAYTNSPIC CPSRAAMWSG LFTHLTESWN NFKGLDPNYT TWMDVMEKHG
YQTQKFGKLD YSSGHHSISN RVEAWTRDVA FLLRQEGRPI INLIPDKNRR RVMDKDWQNT
DKAIAWLRQV NSTKPFVLYL GLNLPHPYPS PSSGENFGSS TFHTSLYWLE KVAYDAIKIP
KWLALSEMHP VDYYSSYTKN CTGKFTENEI KNIRAFYYAM CAETDAMLGE IILALHKLNL
LQKTIVIYTS DHGEMAMEHR QFYKMSMYEA SAHVPILMMG PGIKANLQVP SLVSLVDIYP
TMLDIAGIPL PLNLSGYSLL PLSSNTSAND QAFRVHHPPW ILSEFHGCNA NASTYMLRTG
QWKYIAYSDG TLVQPQLFDL SLDPDELTNI ATEFPEITYS LDQQLRSVIN YPKVSASVHR
YNKEQFIMWK QSVAQNYSNY IAHLRWHQDW QKDPRKYENA IQRWLAIHSS PPTHSPLSLV
HQWLTTHSSP IAVDNKKTFS SYT
