ARSG_CANLF
ID ARSG_CANLF Reviewed; 535 AA.
AC Q32KH9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
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 with pseudosubstrates at
CC acidic pH, such as 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: The 63-kDa precursor undergoes proteolytic processing in two
CC steps, yielding two fragments in the first step (apparent molecular
CC masses of 44 and 18 kDa) (By similarity). In the second step, the 44-
CC kDa fragment is processed further to the 34- and 10-kDa chains. The 10-
CC kDa chain is a cleavage product of the 44-kDa fragment but linked to
CC the 18-kDa 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; AAEX02034846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000758; CAI85004.1; -; mRNA.
DR RefSeq; NP_001041563.1; NM_001048098.1.
DR AlphaFoldDB; Q32KH9; -.
DR SMR; Q32KH9; -.
DR STRING; 9612.ENSCAFP00000016319; -.
DR PaxDb; Q32KH9; -.
DR GeneID; 480460; -.
DR KEGG; cfa:480460; -.
DR CTD; 22901; -.
DR eggNOG; KOG3867; Eukaryota.
DR HOGENOM; CLU_006332_13_6_1; -.
DR InParanoid; Q32KH9; -.
DR OMA; PFTGLWQ; -.
DR OrthoDB; 515367at2759; -.
DR TreeFam; TF314186; -.
DR Reactome; R-CFA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-CFA-1663150; The activation of arylsulfatases.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000011070; Expressed in granulocyte and 49 other tissues.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0004065; F:arylsulfatase 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; 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..535
FT /note="Arylsulfatase G"
FT /id="PRO_0000238662"
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:0000255"
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 535 AA; 58250 MW; D71E87A22A83575B CRC64;
MGWLFLKVLF LGVTFLGCLY PLVDFCPSGE TRGQKPNFVI ILADDMGWGD LGANWAETKD
TANLDKMAAE GMRFVDFHAA ASTCSPSRAS LLTGRLGLRN GVTHNFAVTS VGGLPLNETT
LAEVLQQAGY VTGMIGKWHL GHHGPYHPNF RGFDYYFGIP YSHDMGCTDT PGYNHPPCPA
CPRGDRPSRS LERDCYTDVA LPLYENLNIV EQPVNLSSLA HKYAEKAIQF IQHASASGRP
FLLYMGLAHM HVPISRTQLS AVLRGRRPYG AGLREMDSLV GQIKDKVDRT AKENTFLWFT
GDNGPWAQKC ELAGSVGPFT GLWQTHQGGS PAKQTTWEGG HRVPALAYWP GRVPVNVTST
ALLSVLDIFP TVVALAGASL PQDRHFDGLD ASEVLFGWSQ TGHRVLFHPN SGAAGEFGAL
QTVRLGSYKA FYVSGGAKAC DGDVGREQHH DPPLIFNLED DVAEAVPLDR GSAEYQGVLP
KVREILADVL LDIAGDNTSR ADYTRHPSVT PCCNPHHVAC RCQATGWTDF PTGRC
