SULF1_CAEEL
ID SULF1_CAEEL Reviewed; 709 AA.
AC Q21376;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Putative extracellular sulfatase Sulf-1 homolog;
DE Short=CeSulf-1;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=sul-1; ORFNames=K09C4.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus, Golgi stack {ECO:0000250}. Cell surface {ECO:0000250}.
CC Note=Also localized on the cell surface. {ECO:0000250}.
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}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; FO081118; CCD69246.1; -; Genomic_DNA.
DR PIR; T16584; T16584.
DR RefSeq; NP_508560.1; NM_076159.3.
DR AlphaFoldDB; Q21376; -.
DR SMR; Q21376; -.
DR STRING; 6239.K09C4.8; -.
DR PaxDb; Q21376; -.
DR EnsemblMetazoa; K09C4.8.1; K09C4.8.1; WBGene00006308.
DR GeneID; 180619; -.
DR KEGG; cel:CELE_K09C4.8; -.
DR UCSC; K09C4.8; c. elegans.
DR CTD; 180619; -.
DR WormBase; K09C4.8; CE04736; WBGene00006308; sul-1.
DR eggNOG; KOG3731; Eukaryota.
DR GeneTree; ENSGT00940000169254; -.
DR HOGENOM; CLU_006332_2_0_1; -.
DR InParanoid; Q21376; -.
DR OMA; WDEWHAI; -.
DR OrthoDB; 1273622at2759; -.
DR PhylomeDB; Q21376; -.
DR PRO; PR:Q21376; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006308; Expressed in embryo and 2 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IMP:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IBA:GO_Central.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IMP:WormBase.
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.
PE 3: Inferred from homology;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..709
FT /note="Putative extracellular sulfatase Sulf-1 homolog"
FT /id="PRO_0000033438"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 79
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 709 AA; 83784 MW; 0F919517DDC7E892 CRC64;
MISNLRISNY FIIFYVLFLI IPIKVTSIHF VDSQHNVILI LTDDQDIELG SMDFMPKTSQ
IMKERGTEFT SGYVTTPICC PSRSTILTGL YVHNHHVHTN NQNCTGVEWR KVHEKKSIGV
YLQEAGYRTA YLGKYLNEYD GSYIPPGWDE WHAIVKNSKF YNYTMNSNGE REKFGSEYEK
DYFTDLVTNR SLKFIDKHIK IRAWQPFALI ISYPAPHGPE DPAPQFAHMF ENEISHRTGS
WNFAPNPDKQ WLLQRTGKMN DVHISFTDLL HRRRLQTLQS VDEGIERLFN LLRELNQLWN
TYAIYTSDHG YHLGQFGLLK GKNMPYEFDI RVPFFMRGPG IPRNVTFNEI VTNVDIAPTM
LHIAGVPKPA RMNGRSLLEL VALKKKKKKH MTALKPWRDT ILIERGKMPK LKKIRDRYIK
QKKKFNKENR LSKECKRRKW QRDCVHGQLW KCYYTVEDRW RIYKCRDNWS DQCSCRKKRE
ISNYDDDDID EFLTYADREN FSEGHEWYQG EFEDSGEVGE ELDGHRSKRG ILSKCSCSRN
VSHPIKLLEQ KMSKKHYLKY KKKPQNGSLK PKDCSLPQMN CFTHTASHWK TPPLWPEELG
EFCFCQNCNN NTYWCLRTKN ETHNFLYCEF VTEFISFYDF NTDPDQLINA VYSLDIGVLE
QLSEQLRNLR KCKNRQCEIW STSQMLRSPK LVDLRVNEKS FLTYQPEKT
