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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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