ARSG_RAT
ID ARSG_RAT Reviewed; 526 AA.
AC Q32KJ9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Arylsulfatase G;
DE Short=ASG;
DE EC=3.1.6.1 {ECO:0000250|UniProtKB:Q96EG1};
DE AltName: Full=N-sulfoglucosamine-3-sulfatase;
DE EC=3.1.6.15 {ECO:0000250|UniProtKB:Q96EG1};
DE Flags: Precursor;
GN Name=Arsg;
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: Displays arylsulfatase activity at acidic pH towards the
CC artificial substrate p-nitrocatechol sulfate (By similarity). Catalyzes
CC the hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-
CC O-sulfate units of heparin (By similarity).
CC {ECO:0000250|UniProtKB:Q96EG1}.
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:Q96EG1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 3-sulfate groups of the N-sulfo-D-
CC glucosamine 3-O-sulfate units of heparin.; EC=3.1.6.15;
CC Evidence={ECO:0000250|UniProtKB:Q96EG1};
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: Lysosome {ECO:0000250|UniProtKB:Q3TYD4}. Note=The
CC 63-kDa precursor protein localizes to pre-lysosomal compartments and
CC tightly associates with organelle membranes, most likely the
CC endoplasmic reticulum. In contrast, proteolytically processed fragments
CC of 34-, 18- and 10-kDa are found in lysosomal fractions and lose their
CC membrane association. {ECO:0000250|UniProtKB:Q3TYD4}.
CC -!- PTM: N-glycosylated with both high mannose and complex type sugars.
CC {ECO:0000250|UniProtKB:Q3TYD4}.
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:P15289}.
CC -!- PTM: 63-kDa precursor undergoes proteolytic processing in two steps,
CC yielding two fragments in the first step (apparent molecular masses of
CC 44 and 18 kDa) (By similarity). In the second step, the 44-kDa fragment
CC is processed further to the 34- and 10-kDa chains. The 10-kDa chain is
CC a cleavage product of the 44-kDa fragment but linked to the 18-kDa
CC chain through a disulfide bridge (By similarity).
CC {ECO:0000250|UniProtKB:Q3TYD4}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; AABR03073953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03074766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03075952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03076519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03076696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000738; CAI84984.1; -; mRNA.
DR RefSeq; NP_001041342.1; NM_001047877.1.
DR RefSeq; XP_006247661.1; XM_006247599.3.
DR RefSeq; XP_006247662.1; XM_006247600.3.
DR RefSeq; XP_006247663.1; XM_006247601.3.
DR RefSeq; XP_006247664.1; XM_006247602.3.
DR RefSeq; XP_006247665.1; XM_006247603.2.
DR RefSeq; XP_006247666.1; XM_006247604.3.
DR RefSeq; XP_006247668.1; XM_006247606.3.
DR RefSeq; XP_006247669.1; XM_006247607.3.
DR RefSeq; XP_006247670.1; XM_006247608.3.
DR RefSeq; XP_008766590.1; XM_008768368.2.
DR RefSeq; XP_008766591.1; XM_008768369.1.
DR AlphaFoldDB; Q32KJ9; -.
DR SMR; Q32KJ9; -.
DR STRING; 10116.ENSRNOP00000005257; -.
DR GlyGen; Q32KJ9; 1 site.
DR PhosphoSitePlus; Q32KJ9; -.
DR PaxDb; Q32KJ9; -.
DR Ensembl; ENSRNOT00000113597; ENSRNOP00000086727; ENSRNOG00000003931.
DR GeneID; 303631; -.
DR KEGG; rno:303631; -.
DR CTD; 22901; -.
DR RGD; 1306571; Arsg.
DR VEuPathDB; HostDB:ENSRNOG00000003827; -.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000159093; -.
DR HOGENOM; CLU_006332_13_6_1; -.
DR InParanoid; Q32KJ9; -.
DR OMA; PFTGLWQ; -.
DR PhylomeDB; Q32KJ9; -.
DR TreeFam; TF314186; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-RNO-1663150; The activation of arylsulfatases.
DR PRO; PR:Q32KJ9; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003931; Expressed in heart and 18 other tissues.
DR Genevisible; Q32KJ9; RN.
DR GO; GO:0000421; C:autophagosome membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0004065; F:arylsulfatase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033889; F:N-sulfoglucosamine-3-sulfatase activity; ISO:RGD.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IEA:Ensembl.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IEA:Ensembl.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IEA:Ensembl.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:RGD.
DR GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; IEA:Ensembl.
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 Reference proteome; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..526
FT /note="Arylsulfatase G"
FT /id="PRO_0000238664"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 139
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 84
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q3TYD4"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q3TYD4"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q3TYD4"
SQ SEQUENCE 526 AA; 57269 MW; 95C5F00354AE84A4 CRC64;
MGWLFLKVLL VGMVFSGLLY PFVDFSISGE TRAPRPNIVI ILADDMGWGD LGANWAETKD
TTNLDKMASE GMRFVDFHAA ASTCSPSRAS LLTGRLGLRN GVTHNFAVTS VGGLPLNETT
LAEVLQQAGY VTAMIGKWHL GHHGSYHPSF RGFDYYFGIP YSNDMGCTDN PGYNYPPCPA
CPQSDGRWRN PDRDCYTDVA LPLYENLNIV EQPVNLSGLA QKYAERAVEF IEQASTSGRP
FLLYVGLAHM HVPLSVTPPL ANPQSQRLYR ASLQEMDSLV GQIKDKVDHV AKENTLLWFA
GDNGPWAQKC ELAGSMGPFS GLWQTHQGGS PAKQTTWEGG HRVPALAYWP GRVPVNVTST
ALLSLLDIFP TVIALAGASL PPNRKFDGVD VSEVLFGKSQ TGHRVLFHPN SGAAGEYGAL
QTVRLDRYKA FYITGGAKAC DGGVGPEQHH VSPLIFNLED DAAESSPLQK GSPEYQELLP
KVTRVLADVL QDIADDNSSQ ADYTQDPSVT PCCNPYQITC RCQPGE
