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Arylsulfatase G (ASG) (EC 3.1.6.-)

 ARSG_MOUSE              Reviewed;         525 AA.
Q3TYD4; B1AT67; B1AT68; Q5XFU5; Q69ZT6; Q8CHS3; Q8VBZ5; Q9D3B4;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
28-MAR-2018, entry version 100.
RecName: Full=Arylsulfatase G;
Short=ASG;
EC=3.1.6.-;
Flags: Precursor;
Name=Arsg; Synonyms=Kiaa1001;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Visual cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Kidney, and Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-525 (ISOFORM 1).
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[5]
IDENTIFICATION.
PubMed=16174644; DOI=10.1093/hmg/ddi351;
Sardiello M., Annunziata I., Roma G., Ballabio A.;
"Sulfatases and sulfatase modifying factors: an exclusive and
promiscuous relationship.";
Hum. Mol. Genet. 14:3203-3217(2005).
-!- FUNCTION: Displays arylsulfatase activity with pseudosubstrates at
acidic pH, such as p-nitrocatechol sulfate. {ECO:0000250}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Lysosome. Note=Previously observed
endoplasmic reticulum localization is most likely due to
folding/maturation problems for overexpressed proteins.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3TYD4-1; Sequence=Displayed;
Name=2;
IsoId=Q3TYD4-2; Sequence=VSP_018628, VSP_018629;
Note=No experimental confirmation available.;
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: The conversion to 3-oxoalanine (also known as C-
formylglycine, FGly), of a serine or cysteine residue in
prokaryotes and of a cysteine residue in eukaryotes, is critical
for catalytic activity. {ECO:0000250}.
-!- PTM: Glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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EMBL; AK018132; BAB31086.1; -; mRNA.
EMBL; AK158726; BAE34629.1; -; mRNA.
EMBL; AL645791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC022158; AAH22158.1; -; mRNA.
EMBL; BC039629; AAH39629.1; -; mRNA.
EMBL; BC084731; AAH84731.1; -; mRNA.
EMBL; AK173082; BAD32360.1; -; mRNA.
EMBL; BN000747; CAI84993.1; -; mRNA.
CCDS; CCDS25581.1; -. [Q3TYD4-1]
CCDS; CCDS48971.1; -. [Q3TYD4-2]
RefSeq; NP_001159649.1; NM_001166177.1. [Q3TYD4-2]
RefSeq; NP_082986.3; NM_028710.3. [Q3TYD4-1]
RefSeq; XP_006534411.1; XM_006534348.2. [Q3TYD4-1]
RefSeq; XP_006534412.1; XM_006534349.3. [Q3TYD4-1]
RefSeq; XP_006534413.1; XM_006534350.3. [Q3TYD4-1]
RefSeq; XP_017170289.1; XM_017314800.1. [Q3TYD4-1]
RefSeq; XP_017170290.1; XM_017314801.1. [Q3TYD4-1]
UniGene; Mm.482224; -.
ProteinModelPortal; Q3TYD4; -.
STRING; 10090.ENSMUSP00000020928; -.
PhosphoSitePlus; Q3TYD4; -.
MaxQB; Q3TYD4; -.
PaxDb; Q3TYD4; -.
PeptideAtlas; Q3TYD4; -.
PRIDE; Q3TYD4; -.
Ensembl; ENSMUST00000020928; ENSMUSP00000020928; ENSMUSG00000020604. [Q3TYD4-1]
Ensembl; ENSMUST00000106696; ENSMUSP00000102307; ENSMUSG00000020604. [Q3TYD4-2]
Ensembl; ENSMUST00000106697; ENSMUSP00000102308; ENSMUSG00000020604. [Q3TYD4-1]
GeneID; 74008; -.
KEGG; mmu:74008; -.
UCSC; uc007mcn.1; mouse. [Q3TYD4-1]
UCSC; uc007mcp.2; mouse. [Q3TYD4-2]
CTD; 22901; -.
MGI; MGI:1921258; Arsg.
eggNOG; KOG3867; Eukaryota.
eggNOG; COG3119; LUCA.
GeneTree; ENSGT00760000119062; -.
HOVERGEN; HBG004283; -.
InParanoid; Q3TYD4; -.
KO; K12381; -.
OMA; KAFYITG; -.
OrthoDB; EOG091G041Y; -.
PhylomeDB; Q3TYD4; -.
Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
Reactome; R-MMU-1663150; The activation of arylsulfatases.
PRO; PR:Q3TYD4; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020604; -.
CleanEx; MM_ARSG; -.
Genevisible; Q3TYD4; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0004065; F:arylsulfatase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006790; P:sulfur compound metabolic process; ISO:MGI.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR024607; Sulfatase_CS.
InterPro; IPR000917; Sulfatase_N.
Pfam; PF00884; Sulfatase; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00523; SULFATASE_1; 1.
PROSITE; PS00149; SULFATASE_2; 1.
2: Evidence at transcript level;
Alternative splicing; Calcium; Complete proteome; Glycoprotein;
Hydrolase; Lysosome; Metal-binding; Reference proteome; Signal.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 525 Arylsulfatase G.
/FTId=PRO_0000238663.
ACT_SITE 84 84 Nucleophile.
{ECO:0000250|UniProtKB:P15289}.
ACT_SITE 139 139 {ECO:0000250|UniProtKB:P15289}.
METAL 44 44 Calcium. {ECO:0000250}.
METAL 45 45 Calcium. {ECO:0000250}.
METAL 84 84 Calcium; via 3-oxoalanine. {ECO:0000250}.
METAL 302 302 Calcium. {ECO:0000250}.
METAL 303 303 Calcium. {ECO:0000250}.
BINDING 137 137 Substrate. {ECO:0000250}.
BINDING 162 162 Substrate. {ECO:0000250}.
BINDING 251 251 Substrate. {ECO:0000250}.
MOD_RES 84 84 3-oxoalanine (Cys).
{ECO:0000250|UniProtKB:P15289}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 323 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_018628.
VAR_SEQ 324 327 QTHQ -> MIKI (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_018629.
CONFLICT 122 122 A -> V (in Ref. 3; AAH84731).
{ECO:0000305}.
CONFLICT 247 247 L -> Q (in Ref. 1; BAB31086).
{ECO:0000305}.
SEQUENCE 525 AA; 57434 MW; FA319206459D1B2B CRC64;
MGWLFLKVLL VGMAFSGFFY PLVDFSISGK TRAPQPNIVI ILADDMGWGD LGANWAETKD
TTNLDKMASE GMRFVDFHAA ASTCSPSRAS LLTGRLGLRN GVTHNFAVTS VGGLPVNETT
LAEVLRQEGY VTAMIGKWHL GHHGSYHPNF RGFDYYFGIP YSNDMGCTDA PGYNYPPCPA
CPQRDGLWRN PGRDCYTDVA LPLYENLNIV EQPVNLSGLA QKYAERAVEF IEQASTSGRP
FLLYVGLAHM HVPLSVTPPL AHPQRQSLYR ASLREMDSLV GQIKDKVDHV ARENTLLWFT
GDNGPWAQKC ELAGSVGPFF GLWQTHQGGS PTKQTTWEGG HRVPALAYWP GRVPANVTST
ALLSLLDIFP TVIALAGASL PPNRKFDGRD VSEVLFGKSQ MGHRVLFHPN SGAAGEYGAL
QTVRLNHYKA FYITGGAKAC DGSVGPEQHH VAPLIFNLED AADEGMPLQK GSPEYQEVLQ
QVTRALADVL QDIADDNSSR ADYTQDPSVI PCCNPYQTTC RCQPV


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