ARSF_HUMAN
ID ARSF_HUMAN Reviewed; 590 AA.
AC P54793; Q8TCC5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Arylsulfatase F;
DE Short=ASF;
DE EC=3.1.6.1 {ECO:0000269|PubMed:9192838};
DE Flags: Precursor;
GN Name=ARSF;
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], VARIANT TYR-527, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC TISSUE=Fetal brain;
RX PubMed=9192838; DOI=10.1006/geno.1997.4716;
RA Puca A.A., Zollo M., Repetto M., Andolfi G., Guffanti A., Simon G.,
RA Ballabio A., Franco B.;
RT "Identification by shotgun sequencing, genomic organization, and functional
RT analysis of a fourth arylsulfatase gene (ARSF) from the Xp22.3 region.";
RL Genomics 42:192-199(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-527.
RC TISSUE=Kidney;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 369-422.
RC TISSUE=Kidney;
RX PubMed=7720070; DOI=10.1016/0092-8674(95)90367-4;
RA Franco B., Meroni G., Parenti G., Levilliers J., Bernard L., Gebbia M.,
RA Cox L., Maroteaux P., Sheffield L., Rappold G.A., Andria G., Petit C.,
RA Ballabio A.;
RT "A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia
RT punctata (CDPX) and implications for warfarin embryopathy.";
RL Cell 81:15-25(1995).
CC -!- FUNCTION: Exhibits arylsulfatase activity towards the artificial
CC substrate 4-methylumbelliferyl sulfate. {ECO:0000269|PubMed:9192838}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aryl sulfate + H2O = a phenol + H(+) + sulfate;
CC Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317; EC=3.1.6.1;
CC Evidence={ECO:0000269|PubMed:9192838};
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 -!- ACTIVITY REGULATION: Not inhibited by DHEAS or warfarin.
CC {ECO:0000269|PubMed:9192838}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:9192838};
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; X97868; CAA66462.1; -; mRNA.
DR EMBL; AC112653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022389; AAH22389.1; -; mRNA.
DR CCDS; CCDS14123.1; -.
DR PIR; A56217; A56217.
DR RefSeq; NP_001188467.1; NM_001201538.1.
DR RefSeq; NP_001188468.1; NM_001201539.1.
DR RefSeq; NP_004033.2; NM_004042.4.
DR AlphaFoldDB; P54793; -.
DR SMR; P54793; -.
DR BioGRID; 106909; 77.
DR IntAct; P54793; 3.
DR STRING; 9606.ENSP00000370519; -.
DR GlyGen; P54793; 3 sites.
DR iPTMnet; P54793; -.
DR PhosphoSitePlus; P54793; -.
DR BioMuta; ARSF; -.
DR DMDM; 259016386; -.
DR jPOST; P54793; -.
DR MassIVE; P54793; -.
DR PaxDb; P54793; -.
DR PeptideAtlas; P54793; -.
DR PRIDE; P54793; -.
DR ProteomicsDB; 56720; -.
DR Antibodypedia; 406; 202 antibodies from 22 providers.
DR DNASU; 416; -.
DR Ensembl; ENST00000359361.2; ENSP00000352319.2; ENSG00000062096.15.
DR Ensembl; ENST00000381127.6; ENSP00000370519.1; ENSG00000062096.15.
DR GeneID; 416; -.
DR KEGG; hsa:416; -.
DR MANE-Select; ENST00000381127.6; ENSP00000370519.1; NM_001201539.2; NP_001188468.1.
DR UCSC; uc004cre.3; human.
DR CTD; 416; -.
DR DisGeNET; 416; -.
DR GeneCards; ARSF; -.
DR HGNC; HGNC:721; ARSF.
DR HPA; ENSG00000062096; Tissue enhanced (brain, kidney, skin).
DR MIM; 300003; gene.
DR neXtProt; NX_P54793; -.
DR OpenTargets; ENSG00000062096; -.
DR PharmGKB; PA25012; -.
DR VEuPathDB; HostDB:ENSG00000062096; -.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000163432; -.
DR HOGENOM; CLU_006332_13_4_1; -.
DR InParanoid; P54793; -.
DR OMA; FCLCDTE; -.
DR PhylomeDB; P54793; -.
DR TreeFam; TF314186; -.
DR PathwayCommons; P54793; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-HSA-1663150; The activation of arylsulfatases.
DR SignaLink; P54793; -.
DR BioGRID-ORCS; 416; 19 hits in 690 CRISPR screens.
DR ChiTaRS; ARSF; human.
DR GenomeRNAi; 416; -.
DR Pharos; P54793; Tbio.
DR PRO; PR:P54793; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P54793; protein.
DR Bgee; ENSG00000062096; Expressed in mammalian vulva and 71 other tissues.
DR Genevisible; P54793; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004065; F:arylsulfatase activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Calcium; Glycoprotein; Hydrolase; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..590
FT /note="Arylsulfatase F"
FT /id="PRO_0000033427"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 139
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 78
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 527
FT /note="H -> Y (in dbSNP:rs1052638)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9192838"
FT /id="VAR_058846"
FT CONFLICT 20..29
FT /note="CQAHRVHDDK -> WPGHTGCMTTR (in Ref. 1; CAA66462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 65940 MW; EA9B7289040AE79A CRC64;
MRPRRPLVFM SLVCALLNTC QAHRVHDDKP NIVLIMVDDL GIGDLGCYGN DTMRTPHIDR
LAREGVRLTQ HISAASLCSP SRSAFLTGRY PIRSGMVSSG NRRVIQNLAV PAGLPLNETT
LAALLKKQGY STGLIGKWHQ GLNCDSRSDQ CHHPYNYGFD YYYGMPFTLV DSCWPDPSRN
TELAFESQLW LCVQLVAIAI LTLTFGKLSG WVSVPWLLIF SMILFIFLLG YAWFSSHTSP
LYWDCLLMRG HEITEQPMKA ERAGSIMVKE AISFLERHSK ETFLLFFSFL HVHTPLPTTD
DFTGTSKHGL YGDNVEEMDS MVGKILDAID DFGLRNNTLV YFTSDHGGHL EARRGHAQLG
GWNGIYKGGK GMGGWEGGIR VPGIVRWPGK VPAGRLIKEP TSLMDILPTV ASVSGGSLPQ
DRVIDGRDLM PLLQGNVRHS EHEFLFHYCG SYLHAVRWIP KDDSGSVWKA HYVTPVFQPP
ASGGCYVTSL CRCFGEQVTY HNPPLLFDLS RDPSESTPLT PATEPLHDFV IKKVANALKE
HQETIVPVTY QLSELNQGRT WLKPCCGVFP FCLCDKEEEV SQPRGPNEKR
