ARSH_HUMAN
ID ARSH_HUMAN Reviewed; 562 AA.
AC Q5FYA8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Arylsulfatase H;
DE Short=ASH;
DE EC=3.1.6.-;
GN Name=ARSH;
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).
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: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {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; AY875940; AAW66668.1; -; mRNA.
DR CCDS; CCDS35198.1; -.
DR RefSeq; NP_001011719.1; NM_001011719.1.
DR AlphaFoldDB; Q5FYA8; -.
DR SMR; Q5FYA8; -.
DR BioGRID; 131447; 3.
DR STRING; 9606.ENSP00000370522; -.
DR iPTMnet; Q5FYA8; -.
DR PhosphoSitePlus; Q5FYA8; -.
DR BioMuta; ARSH; -.
DR DMDM; 74722579; -.
DR jPOST; Q5FYA8; -.
DR MassIVE; Q5FYA8; -.
DR PaxDb; Q5FYA8; -.
DR PeptideAtlas; Q5FYA8; -.
DR PRIDE; Q5FYA8; -.
DR ProteomicsDB; 62819; -.
DR Antibodypedia; 23512; 150 antibodies from 25 providers.
DR DNASU; 347527; -.
DR Ensembl; ENST00000381130.3; ENSP00000370522.3; ENSG00000205667.3.
DR GeneID; 347527; -.
DR KEGG; hsa:347527; -.
DR MANE-Select; ENST00000381130.3; ENSP00000370522.3; NM_001011719.2; NP_001011719.1.
DR UCSC; uc011mhj.3; human.
DR CTD; 347527; -.
DR DisGeNET; 347527; -.
DR GeneCards; ARSH; -.
DR HGNC; HGNC:32488; ARSH.
DR HPA; ENSG00000205667; Not detected.
DR MIM; 300586; gene.
DR neXtProt; NX_Q5FYA8; -.
DR OpenTargets; ENSG00000205667; -.
DR PharmGKB; PA143485308; -.
DR VEuPathDB; HostDB:ENSG00000205667; -.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000162925; -.
DR HOGENOM; CLU_006332_13_4_1; -.
DR InParanoid; Q5FYA8; -.
DR OMA; RNDHCYH; -.
DR OrthoDB; 873694at2759; -.
DR PhylomeDB; Q5FYA8; -.
DR TreeFam; TF314186; -.
DR PathwayCommons; Q5FYA8; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-HSA-1663150; The activation of arylsulfatases.
DR SignaLink; Q5FYA8; -.
DR BioGRID-ORCS; 347527; 6 hits in 688 CRISPR screens.
DR GenomeRNAi; 347527; -.
DR Pharos; Q5FYA8; Tbio.
DR PRO; PR:Q5FYA8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5FYA8; protein.
DR Bgee; ENSG00000205667; Expressed in gall bladder and 18 other tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
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; Hydrolase; Membrane; Metal-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..562
FT /note="Arylsulfatase H"
FT /id="PRO_0000295623"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 117
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 16
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 55
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
SQ SEQUENCE 562 AA; 63525 MW; E7428B679C76E78F CRC64;
MTRNARPNIV LLMADDLGVG DLCCYGNNSV STPNIDRLAS EGVRLTQHLA AASMCTPSRA
AFLTGRYPIR SGMVSAYNLN RAFTWLGGSG GLPTNETTFA KLLQHRGYRT GLIGKWHLGL
SCASRNDHCY HPLNHGFHYF YGVPFGLLSD CQASKTPELH RWLRIKLWIS TVALALVPFL
LLIPKFARWF SVPWKVIFVF ALLAFLFFTS WYSSYGFTRR WNCILMRNHE IIQQPMKEEK
VASLMLKEAL AFIERYKREP FLLFFSFLHV HTPLISKKKF VGRSKYGRYG DNVEEMDWMV
GKILDALDQE RLANHTLVYF TSDNGGHLEP LDGAVQLGGW NGIYKGGKGM GGWEGGIRVP
GIFRWPSVLE AGRVINEPTS LMDIYPTLSY IGGGILSQDR VIDGQNLMPL LEGRASHSDH
EFLFHYCGVY LHTVRWHQKD CATVWKAHYV TPKFYPEGTG ACYGSGICSC SGDVTYHDPP
LLFDISRDPS EALPLNPDNE PLFDSVIKKM EAAIREHRRT LTPVPQQFSV FNTIWKPWLQ
PCCGTFPFCG CDKEDDILPM AP
