ID F6RR89_HORSE Unreviewed; 857 AA.
AC F6RR89;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 3.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Arylsulfatase {ECO:0000256|ARBA:ARBA00035041};
DE EC=3.1.6.1 {ECO:0000256|ARBA:ARBA00035026};
DE EC=3.1.6.14 {ECO:0000256|ARBA:ARBA00035027};
DE AltName: Full=N-acetylglucosamine-6-sulfatase {ECO:0000256|ARBA:ARBA00035044};
GN Name=SULF1 {ECO:0000313|Ensembl:ENSECAP00000015670.3,
GN ECO:0000313|VGNC:VGNC:23753};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000015670.3, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000015670.3, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000015670.3,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000015670.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000015670.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 6-sulfate groups of the N-acetyl-D-
CC glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.;
CC EC=3.1.6.14; Evidence={ECO:0000256|ARBA:ARBA00034997};
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:0000256|ARBA:ARBA00034984};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR036665-52};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR036665-
CC 52};
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}.
CC Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus,
CC Golgi stack {ECO:0000256|ARBA:ARBA00004348}.
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:0000256|PIRSR:PIRSR036665-50}.
CC -!- SIMILARITY: Belongs to the sulfatase family.
CC {ECO:0000256|ARBA:ARBA00008779}.
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DR AlphaFoldDB; F6RR89; -.
DR STRING; 9796.ENSECAP00000015670; -.
DR PaxDb; 9796-ENSECAP00000015670; -.
DR Ensembl; ENSECAT00000019160.3; ENSECAP00000015670.3; ENSECAG00000016927.4.
DR VGNC; VGNC:23753; SULF1.
DR GeneTree; ENSGT00940000157544; -.
DR HOGENOM; CLU_006332_2_0_1; -.
DR InParanoid; F6RR89; -.
DR OMA; GCRGRNC; -.
DR Proteomes; UP000002281; Chromosome 9.
DR Bgee; ENSECAG00000016927; Expressed in synovial membrane of synovial joint and 21 other cell types or tissues.
DR ExpressionAtlas; F6RR89; baseline.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IBA:GO_Central.
DR GO; GO:0032836; P:glomerular basement membrane development; IBA:GO_Central.
DR GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; IBA:GO_Central.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IBA:GO_Central.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IBA:GO_Central.
DR CDD; cd16147; G6S; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR014615; Extracellular_sulfatase.
DR InterPro; IPR024609; Extracellular_sulfatase_C.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR43108:SF1; EXTRACELLULAR SULFATASE SULF-1; 1.
DR PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR Pfam; PF12548; DUF3740; 2.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF036665; Sulf1; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 2.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR036665-52};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036665-52};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..857
FT /note="Arylsulfatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040365457"
FT DOMAIN 43..373
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT DOMAIN 534..676
FT /note="Extracellular sulfatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12548"
FT DOMAIN 679..737
FT /note="Extracellular sulfatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12548"
FT REGION 508..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 640..667
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-51"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT MOD_RES 87
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-50"
SQ SEQUENCE 857 AA; 99316 MW; 502230ED6E2D9156 CRC64;
MKYSCCALVL AVLGTELLGS LCSNVRSPRF RGRLQQERKN IRPNIILVLT DDQDVELGSL
QVMNKTRKIM EHGGATFTNA FVTTPMCCPS RSSMLTGKYV HNHNVYTNNE NCSSPSWQAM
HEPRTFAVYL NNTGYRTAFF GKYLNEYNGS YIPPGWREWL GLIKNSRFYN YTVCRNGIKE
KHGFDYAKDY FTDLITNESI NYFKMSKRMY PHRPIMMVIS HAAPHGPEDS APQFSKLYPN
ASQHITPSYN YAPNMDKHWI MQYTGPMLPI HMEFTNVLHR KRLQTLMSVD DSVERLYNML
VETRELENTY IIYTADHGYH IGQFGLVKGK SMPYDFDIRV PFFIRGPSVE PGSIVPQIVL
NIDLAPTILD IAGLDTPPDV DGKSVLKLLD PERPGNRFRT NKKAKIWRDT FLVERGKFLR
KKEDSSKNIQ QSNHLPKYER VKELCQQARY QTACEQPGQK WQCIEDTAGK LRIHKCKGSG
DLLAVRQSTR HLYSRGFHDK DRECHCGEPG YRASRGQRKS QRQFLRNQGT PKYKPRFVHT
RQTRSLSVEF EGEIYDINLE EEELQVLRPR SIAKRHDEGR RGPGGRQAAG DGAAMLAGGD
NAVGLPATVR VTHKCFILPN DTIHCERELY QSARAWKDHK AYIDKEIEAL QDKIKNLREV
RGHLKRRKPE ECGCNKQSYY NKEKGVKKQE KLKSHLHPFK EAAQEVDSKL QLFKEKRRRK
KERKEKKRQR KGEECSLPGL TCFTHDNHHW QTAPFWNLGS FCACTSSNNN TYWCLRTVNE
THNFLFCEFA TGFLEYFDMN TDPYQLTNTV HAVERGILNQ LHIQLMELRS CQGYKQCNPR
PKGLEVAHVR QSRRTRS
//
