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Arylsulfatase J (ASJ) (EC 3.1.6.-)

 ARSJ_HUMAN              Reviewed;         599 AA.
Q5FYB0; A2RUG0; B7ZM45; Q1HA39; Q5FWE4; Q6UWT9;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 1.
23-MAY-2018, entry version 114.
RecName: Full=Arylsulfatase J;
Short=ASJ;
EC=3.1.6.-;
Flags: Precursor;
Name=ARSJ; ORFNames=UNQ372/PRO708;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16500042; DOI=10.1016/j.gene.2005.12.023;
Obaya A.J.;
"Molecular cloning and initial characterization of three novel human
sulfatases.";
Gene 372:110-117(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Chondrosarcoma;
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).
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- 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}.
-!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAQ89010.1; Type=Frameshift; Positions=425; Evidence={ECO:0000305};
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EMBL; AY875938; AAW66666.1; -; mRNA.
EMBL; AM049401; CAJ18095.1; -; mRNA.
EMBL; AY358647; AAQ89010.1; ALT_FRAME; mRNA.
EMBL; AC104779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC089445; AAH89445.1; -; mRNA.
EMBL; BC132879; AAI32880.1; -; mRNA.
EMBL; BC132881; AAI32882.1; -; mRNA.
EMBL; BC144265; AAI44266.1; -; mRNA.
CCDS; CCDS43264.1; -.
RefSeq; NP_078866.3; NM_024590.3.
RefSeq; XP_005263269.1; XM_005263212.4.
RefSeq; XP_016864081.1; XM_017008592.1.
UniGene; Hs.22895; -.
UniGene; Hs.700496; -.
UniGene; Hs.712042; -.
ProteinModelPortal; Q5FYB0; -.
SMR; Q5FYB0; -.
BioGrid; 122770; 4.
IntAct; Q5FYB0; 1.
MINT; Q5FYB0; -.
STRING; 9606.ENSP00000320219; -.
iPTMnet; Q5FYB0; -.
PhosphoSitePlus; Q5FYB0; -.
BioMuta; ARSJ; -.
DMDM; 74722580; -.
PaxDb; Q5FYB0; -.
PeptideAtlas; Q5FYB0; -.
PRIDE; Q5FYB0; -.
Ensembl; ENST00000315366; ENSP00000320219; ENSG00000180801.
GeneID; 79642; -.
KEGG; hsa:79642; -.
UCSC; uc003ibq.2; human.
CTD; 79642; -.
DisGeNET; 79642; -.
EuPathDB; HostDB:ENSG00000180801.12; -.
GeneCards; ARSJ; -.
HGNC; HGNC:26286; ARSJ.
HPA; HPA036481; -.
HPA; HPA036482; -.
MIM; 610010; gene.
neXtProt; NX_Q5FYB0; -.
OpenTargets; ENSG00000180801; -.
PharmGKB; PA143485310; -.
eggNOG; KOG3867; Eukaryota.
eggNOG; COG3119; LUCA.
GeneTree; ENSGT00760000119062; -.
HOGENOM; HOG000135354; -.
HOVERGEN; HBG004282; -.
InParanoid; Q5FYB0; -.
KO; K12375; -.
OMA; AIRVQHW; -.
OrthoDB; EOG091G06C3; -.
PhylomeDB; Q5FYB0; -.
TreeFam; TF314186; -.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-1663150; The activation of arylsulfatases.
ChiTaRS; ARSJ; human.
GenomeRNAi; 79642; -.
PRO; PR:Q5FYB0; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000180801; -.
CleanEx; HS_ARSJ; -.
ExpressionAtlas; Q5FYB0; baseline and differential.
Genevisible; Q5FYB0; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004065; F:arylsulfatase activity; TAS:HGNC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008152; P:metabolic process; IEA:InterPro.
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;
Calcium; Complete proteome; Glycoprotein; Hydrolase; Metal-binding;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 49 {ECO:0000255}.
CHAIN 50 599 Arylsulfatase J.
/FTId=PRO_0000042217.
ACT_SITE 122 122 Nucleophile.
{ECO:0000250|UniProtKB:P15289}.
ACT_SITE 178 178 {ECO:0000250|UniProtKB:P15289}.
METAL 84 84 Calcium. {ECO:0000250}.
METAL 85 85 Calcium. {ECO:0000250}.
METAL 122 122 Calcium; via 3-oxoalanine. {ECO:0000250}.
METAL 327 327 Calcium. {ECO:0000250}.
METAL 328 328 Calcium. {ECO:0000250}.
BINDING 176 176 Substrate. {ECO:0000250}.
BINDING 269 269 Substrate. {ECO:0000250}.
BINDING 345 345 Substrate. {ECO:0000250}.
MOD_RES 122 122 3-oxoalanine (Cys).
{ECO:0000250|UniProtKB:P15289}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 497 497 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 527 527 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 565 565 S -> R (in dbSNP:rs17046588).
/FTId=VAR_052515.
CONFLICT 182 182 Y -> N (in Ref. 3; AAQ89010).
{ECO:0000305}.
CONFLICT 263 263 I -> T (in Ref. 3; AAQ89010).
{ECO:0000305}.
CONFLICT 495 495 L -> P (in Ref. 5; AAH89445).
{ECO:0000305}.
CONFLICT 576 576 S -> K (in Ref. 5; AAH89445).
{ECO:0000305}.
CONFLICT 590 599 STCHSGVTCG -> KPANLAR (in Ref. 2;
CAJ18095 and 3; AAQ89010). {ECO:0000305}.
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


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