SULF1_COTCO
ID SULF1_COTCO Reviewed; 867 AA.
AC Q90XB6;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Extracellular sulfatase Sulf-1;
DE Short=qSulf1;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=SULF1;
OS Coturnix coturnix (Common quail) (Tetrao coturnix).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=9091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF 87-CYS-CYS-88.
RX PubMed=11533491; DOI=10.1126/science.293.5535.1663;
RA Dhoot G.K., Gustafsson M.K., Ai X., Sun W., Standiford D.M.,
RA Emerson C.P. Jr.;
RT "Regulation of Wnt signaling and embryo patterning by an extracellular
RT sulfatase.";
RL Science 293:1663-1666(2001).
CC -!- FUNCTION: Regulates Wnt signaling through desulfation of cell surface
CC heparan sulfate proteoglycans.
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. Note=Also localized
CC on the cell surface.
CC -!- TISSUE SPECIFICITY: Expressed in the ventral spinal cord and paraxial
CC mesoderm as well as in the floor plate.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF410802; AAK98515.1; -; mRNA.
DR AlphaFoldDB; Q90XB6; -.
DR SMR; Q90XB6; -.
DR PRIDE; Q90XB6; -.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0004065; F:arylsulfatase activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IDA:UniProtKB.
DR GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR GO; GO:0001502; P:cartilage condensation; IDA:UniProtKB.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0002063; P:chondrocyte development; ISS:UniProtKB.
DR GO; GO:0048706; P:embryonic skeletal system development; ISS:UniProtKB.
DR GO; GO:0014846; P:esophagus smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:0035860; P:glial cell-derived neurotrophic factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; IDA:UniProtKB.
DR GO; GO:0060384; P:innervation; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0036022; P:limb joint morphogenesis; IDA:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060686; P:negative regulation of prostatic bud formation; ISS:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.40.720.10; -; 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 Pfam; PF12548; DUF3740; 2.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF036665; Sulf1; 1.
DR SUPFAM; SSF53649; SSF53649; 2.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 1: Evidence at protein level;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase;
KW Metal-binding; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..867
FT /note="Extracellular sulfatase Sulf-1"
FT /id="PRO_0000033437"
FT REGION 494..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 87
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 87..88
FT /note="CC->AA: Acts as a dominant negative inhibitor of Wnt
FT signaling."
FT /evidence="ECO:0000269|PubMed:11533491"
SQ SEQUENCE 867 AA; 100603 MW; 6DA4499EB134A01C CRC64;
MKTSWFALFL AVLSTELLTS HSSTLKSLRF RGRVQQERKN IRPNIILVLT DDQDVELGSL
QVMNKTRRIM ENGGASFINA FVTTPMCCPS RSSMLTGKYV HNHNIYTNNE NCSSPSWQAT
HEPRTFAVYL NNTGYRTAFF GKYLNEYNGS YIPPGWREWV GLVKNSRFYN YTISRNGNKE
KHGFDYAKDY FTDLITNESI NYFRMSKRIY PHRPIMMVIS HAAPHGPEDS APQFSELYPN
ASQHITPSYN YAPNMDKHWI MQYTGPMLPI HMEFTNVLQR KRLQTLMSVD DSMERLYQML
AEMGELENTY IIYTADHGYH IGQFGLVKGK SMPYDFDIRV PFFIRGPSVE PGSVVPQIVL
NIDLAPTILD IAGLDTPPDM DGKSVLKLLD LERPGNRFRT NKKTKIWRDT FLVERGKFLR
KKEEANKNTQ QSNQLPKYER VKELCQQARY QTACEQPGQK WQCTEDASGK LRIHKCKVSS
DILAIRKRTR SIHSRGYSGK DKDCNCGDTD FRNSRTQRKN QRQFLRNPSA QKYKPRFVHT
RQTRSLSVEF EGEIYDINLE EEELQVLKTR SITKRHNAEN DKKAEETDGA PGDTMVADGT
DVIGQPSSVR VTHKCFILPN DTIRCERELY QSARAWKDHK AYIDKEIEAL QDKIKNLREV
RGHLKRRKPD ECDCTKQSYY NKEKGVKTQE KIKSHLHPFK EAAQEVDSKL QLFKENRRRK
KERKGKKRQK KGDECSLPGL TCFTHDNNHW QTAPFWNLGS FCACTSSNNN TYWCLRTVND
THNFLFCEFA TGFLEFFDMN TDPYQLTNTV HTVERGILNQ LHVQLMELRS CQGYKQCNPR
PKGLETGNKD GGSYDPHRGQ LWDGWEG
