ARSJ_HUMAN
ID ARSJ_HUMAN Reviewed; 599 AA.
AC Q5FYB0; A2RUG0; B7ZM45; Q1HA39; Q5FWE4; Q6UWT9;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Arylsulfatase J;
DE Short=ASJ;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=ARSJ; ORFNames=UNQ372/PRO708;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16500042; DOI=10.1016/j.gene.2005.12.023;
RA Obaya A.J.;
RT "Molecular cloning and initial characterization of three novel human
RT sulfatases.";
RL Gene 372:110-117(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Chondrosarcoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAQ89010.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY875938; AAW66666.1; -; mRNA.
DR EMBL; AM049401; CAJ18095.1; -; mRNA.
DR EMBL; AY358647; AAQ89010.1; ALT_FRAME; mRNA.
DR EMBL; AC104779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089445; AAH89445.1; -; mRNA.
DR EMBL; BC132879; AAI32880.1; -; mRNA.
DR EMBL; BC132881; AAI32882.1; -; mRNA.
DR EMBL; BC144265; AAI44266.1; -; mRNA.
DR CCDS; CCDS43264.1; -.
DR RefSeq; NP_078866.3; NM_024590.3.
DR RefSeq; XP_005263269.1; XM_005263212.4.
DR RefSeq; XP_016864081.1; XM_017008592.1.
DR AlphaFoldDB; Q5FYB0; -.
DR SMR; Q5FYB0; -.
DR BioGRID; 122770; 5.
DR IntAct; Q5FYB0; 1.
DR MINT; Q5FYB0; -.
DR STRING; 9606.ENSP00000320219; -.
DR GlyGen; Q5FYB0; 6 sites.
DR iPTMnet; Q5FYB0; -.
DR PhosphoSitePlus; Q5FYB0; -.
DR BioMuta; ARSJ; -.
DR DMDM; 74722580; -.
DR MassIVE; Q5FYB0; -.
DR PaxDb; Q5FYB0; -.
DR PeptideAtlas; Q5FYB0; -.
DR PRIDE; Q5FYB0; -.
DR ProteomicsDB; 62820; -.
DR Antibodypedia; 48673; 39 antibodies from 20 providers.
DR DNASU; 79642; -.
DR Ensembl; ENST00000315366.8; ENSP00000320219.7; ENSG00000180801.14.
DR GeneID; 79642; -.
DR KEGG; hsa:79642; -.
DR MANE-Select; ENST00000315366.8; ENSP00000320219.7; NM_024590.4; NP_078866.3.
DR UCSC; uc003ibq.2; human.
DR CTD; 79642; -.
DR DisGeNET; 79642; -.
DR GeneCards; ARSJ; -.
DR HGNC; HGNC:26286; ARSJ.
DR HPA; ENSG00000180801; Low tissue specificity.
DR MalaCards; ARSJ; -.
DR MIM; 610010; gene.
DR neXtProt; NX_Q5FYB0; -.
DR OpenTargets; ENSG00000180801; -.
DR PharmGKB; PA143485310; -.
DR VEuPathDB; HostDB:ENSG00000180801; -.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000159954; -.
DR HOGENOM; CLU_006332_10_1_1; -.
DR InParanoid; Q5FYB0; -.
DR OMA; GPWFKED; -.
DR OrthoDB; 875384at2759; -.
DR PhylomeDB; Q5FYB0; -.
DR TreeFam; TF314186; -.
DR PathwayCommons; Q5FYB0; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-HSA-1663150; The activation of arylsulfatases.
DR SignaLink; Q5FYB0; -.
DR BioGRID-ORCS; 79642; 4 hits in 1068 CRISPR screens.
DR ChiTaRS; ARSJ; human.
DR GenomeRNAi; 79642; -.
DR Pharos; Q5FYB0; Tdark.
DR PRO; PR:Q5FYB0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q5FYB0; protein.
DR Bgee; ENSG00000180801; Expressed in stromal cell of endometrium and 118 other tissues.
DR ExpressionAtlas; Q5FYB0; baseline and differential.
DR Genevisible; Q5FYB0; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004065; F:arylsulfatase activity; TAS:HGNC-UCL.
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; Glycoprotein; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..49
FT /evidence="ECO:0000255"
FT CHAIN 50..599
FT /note="Arylsulfatase J"
FT /id="PRO_0000042217"
FT REGION 531..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..586
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 178
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 122
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 565
FT /note="S -> R (in dbSNP:rs17046588)"
FT /id="VAR_052515"
FT CONFLICT 182
FT /note="Y -> N (in Ref. 3; AAQ89010)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="I -> T (in Ref. 3; AAQ89010)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="L -> P (in Ref. 5; AAH89445)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="S -> K (in Ref. 5; AAH89445)"
FT /evidence="ECO:0000305"
FT CONFLICT 590..599
FT /note="STCHSGVTCG -> KPANLAR (in Ref. 2; CAJ18095 and 3;
FT AAQ89010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 67235 MW; 1548898E95C43A7A CRC64;
MAPRGCAGHP PPPSPQACVC PGKMLAMGAL AGFWILCLLT YGYLSWGQAL EEEEEGALLA
QAGEKLEPST TSTSQPHLIF ILADDQGFRD VGYHGSEIKT PTLDKLAAEG VKLENYYVQP
ICTPSRSQFI TGKYQIHTGL QHSIIRPTQP NCLPLDNATL PQKLKEVGYS THMVGKWHLG
FYRKECMPTR RGFDTFFGSL LGSGDYYTHY KCDSPGMCGY DLYENDNAAW DYDNGIYSTQ
MYTQRVQQIL ASHNPTKPIF LYIAYQAVHS PLQAPGRYFE HYRSIININR RRYAAMLSCL
DEAINNVTLA LKTYGFYNNS IIIYSSDNGG QPTAGGSNWP LRGSKGTYWE GGIRAVGFVH
SPLLKNKGTV CKELVHITDW YPTLISLAEG QIDEDIQLDG YDIWETISEG LRSPRVDILH
NIDPIYTKAK NGSWAAGYGI WNTAIQSAIR VQHWKLLTGN PGYSDWVPPQ SFSNLGPNRW
HNERITLSTG KSVWLFNITA DPYERVDLSN RYPGIVKKLL RRLSQFNKTA VPVRYPPKDP
RSNPRLNGGV WGPWYKEETK KKKPSKNQAE KKQKKSKKKK KKQQKAVSGS TCHSGVTCG
