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ARSJ_MOUSE
ID   ARSJ_MOUSE              Reviewed;         598 AA.
AC   Q8BM89; Q8BKG5; Q8BL46;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Arylsulfatase J;
DE            Short=ASJ;
DE            EC=3.1.6.-;
DE   Flags: Precursor;
GN   Name=Arsj;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Diencephalon, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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:0000305}.
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   -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR   EMBL; AK034454; BAC28715.1; -; mRNA.
DR   EMBL; AK046410; BAC32714.1; -; mRNA.
DR   EMBL; AK052931; BAC35208.1; -; mRNA.
DR   CCDS; CCDS17822.1; -.
DR   RefSeq; NP_775627.1; NM_173451.3.
DR   AlphaFoldDB; Q8BM89; -.
DR   SMR; Q8BM89; -.
DR   BioGRID; 234858; 1.
DR   STRING; 10090.ENSMUSP00000091511; -.
DR   GlyGen; Q8BM89; 7 sites.
DR   iPTMnet; Q8BM89; -.
DR   PhosphoSitePlus; Q8BM89; -.
DR   PaxDb; Q8BM89; -.
DR   PRIDE; Q8BM89; -.
DR   Antibodypedia; 48673; 39 antibodies from 20 providers.
DR   DNASU; 271970; -.
DR   Ensembl; ENSMUST00000093976; ENSMUSP00000091511; ENSMUSG00000046561.
DR   GeneID; 271970; -.
DR   KEGG; mmu:271970; -.
DR   UCSC; uc008rgc.1; mouse.
DR   CTD; 79642; -.
DR   MGI; MGI:2443513; Arsj.
DR   VEuPathDB; HostDB:ENSMUSG00000046561; -.
DR   eggNOG; KOG3867; Eukaryota.
DR   GeneTree; ENSGT00940000159954; -.
DR   HOGENOM; CLU_006332_10_1_1; -.
DR   InParanoid; Q8BM89; -.
DR   OMA; GPWFKED; -.
DR   OrthoDB; 875384at2759; -.
DR   PhylomeDB; Q8BM89; -.
DR   TreeFam; TF314186; -.
DR   Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-MMU-1663150; The activation of arylsulfatases.
DR   BioGRID-ORCS; 271970; 3 hits in 74 CRISPR screens.
DR   PRO; PR:Q8BM89; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8BM89; protein.
DR   Bgee; ENSMUSG00000046561; Expressed in endothelial cell of lymphatic vessel and 73 other tissues.
DR   ExpressionAtlas; Q8BM89; baseline and differential.
DR   Genevisible; Q8BM89; MM.
DR   GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
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; Glycoprotein; Hydrolase; Metal-binding; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..47
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..598
FT                   /note="Arylsulfatase J"
FT                   /id="PRO_0000042218"
FT   REGION          532..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..585
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        120
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         82
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         83
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         120
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         325
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         326
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   MOD_RES         120
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        525
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        563
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   598 AA;  67354 MW;  34E85DAC88FDD4CF CRC64;
     MAPRDSAEPL PPLSPQAWAW SGKFLAMGAL AGFSVLSLLT YGYLCWGQDL EEEGSLKAQV
     DERPEAGTAG TSQPHLIFIL ADDQGFRDVG YHGSEIKTPT LDKLAAEGVK LENYYVQPIC
     TPSRSQFITG KYQIHTGLQH SIIRPTQPNC LPLDNATLPQ KLKEVGYSTH MVGKWHLGFY
     RKDCMPTKRG FDTFFGSLLG SGDYYTHYKC DSPGVCGYDL YENDNAAWDY DNGIYSTQMY
     TQRVQQILAT HDPTKPLFLY VAYQAVHSPL QAPGRYFEHY RSIININRRR YAAMLSCLDE
     AIHNVTLALK RYGFYNNSII IYSSDNGGQP TAGGSNWPLR GSKGTYWEGG IRAVGFVHSP
     LLKNKGTVCK ELVHITDWYP TLISLAEGQI DEDIQLDGYD IWETISEGLR SPRVDILHNI
     DPIYTKAKNG SWAAGYGIWN TAIQSAIRVQ HWKLLTGNPG YSDWVPPQAF SNLGPNRWHN
     ERITLSTGKS IWLFNITADP YERVDLSSRY PGIVKKLLRR LSQFNKTAVP VRYPPKDPRS
     NPRLNGGVWG PWYKEENKKK KSNKTKAKKM QKKKSKARMR KQLAAHSSIK CHPSVATG
 
 
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