SULF1_RAT
ID SULF1_RAT Reviewed; 870 AA.
AC Q8VI60;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Extracellular sulfatase Sulf-1;
DE EC=3.1.6.-;
DE AltName: Full=RSulfFP1;
DE AltName: Full=Sulfatase FP;
DE Flags: Precursor;
GN Name=Sulf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Embryo;
RX PubMed=11895481; DOI=10.1046/j.1356-9597.2001.00502.x;
RA Ohto T., Uchida H., Yamazaki H., Keino-Masu K., Matsui A., Masu M.;
RT "Identification of a novel nonlysosomal sulphatase expressed in the floor
RT plate, choroid plexus and cartilage.";
RL Genes Cells 7:173-185(2002).
RN [2]
RP ERRATUM OF PUBMED:11895481.
RA Ohto T., Uchida H., Yamazaki H., Keino-Masu K., Matsui A., Masu M.;
RL Genes Cells 7:521-522(2002).
CC -!- FUNCTION: May be involved in the desulfation of sulfated
CC glycosaminoglycans in the biosynthetic pathway and may play a role as
CC an extracellular regulator of proteoglycan mediated signaling.
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. Golgi apparatus, Golgi
CC stack. Cell surface. Note=Also localized on the cell surface.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the floor plate, choroid
CC plexus and cartilage. Weaker expression seen in the eye, lung brain,
CC spinal cord, urinary bladder, testis, ovary and uterus.
CC -!- DEVELOPMENTAL STAGE: Abundantly and specifically expressed in the floor
CC plate region of the spinal cord at embryonic day 13 (E13) and E15 and
CC at lower levels at postnatal day 1 (P1). A high level expression was
CC also observed in the ventral hindbrain and midbrain. No expression was
CC seen in the notochord at these stages. Prominent expression in the
CC nervous system was also seen in the choroid plexus. At E13, expression
CC was also seen in the dorsomedial forebrain and roof of the hind brain.
CC Robust and specific expression was detected in the choroid plexus
CC epithelium of the lateral, 3rd and 4th ventricles at E15 and P1 and
CC persisted into adulthood. In the CNS, expression was detected in
CC thalamic and hypothalamic regions at E13, E15 and P1. In embryos, it
CC was highly expressed in the limb buds, face region, large blood
CC vessels, olfactory pits and pleural epithelium. In particular,
CC expression was robust and specific in bone-forming regions of the face
CC and in the mesenchymal cells surrounding the developing cartilages of
CC the extremities.
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; AF230072; AAL71906.1; -; mRNA.
DR RefSeq; NP_599205.1; NM_134378.2.
DR AlphaFoldDB; Q8VI60; -.
DR SMR; Q8VI60; -.
DR STRING; 10116.ENSRNOP00000012611; -.
DR GlyGen; Q8VI60; 10 sites.
DR PaxDb; Q8VI60; -.
DR GeneID; 171396; -.
DR KEGG; rno:171396; -.
DR UCSC; RGD:708554; rat.
DR CTD; 23213; -.
DR RGD; 708554; Sulf1.
DR eggNOG; KOG3731; Eukaryota.
DR InParanoid; Q8VI60; -.
DR OrthoDB; 1273622at2759; -.
DR PhylomeDB; Q8VI60; -.
DR PRO; PR:Q8VI60; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0004065; F:arylsulfatase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR GO; GO:0001502; P:cartilage condensation; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS: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:0032836; P:glomerular basement membrane development; ISO:RGD.
DR GO; GO:0003094; P:glomerular filtration; ISO:RGD.
DR GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; ISS: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; ISS: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:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; ISO:RGD.
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; 1.
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; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..870
FT /note="Extracellular sulfatase Sulf-1"
FT /id="PRO_0000033436"
FT REGION 506..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..527
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 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 870 AA; 100860 MW; 037813868C08967F CRC64;
MKNSCWALLL AVLGAELLGG FCSTMRSQRF RGRVQQERKN IRPNIILVLT DDQDVELGSL
QVMNKTRKIM EHGGATFTNA FVTTPMCCPS RSSMLTGKYV HNHNVYTNNE NCSSPSWQAL
HEPRTFAVYL NNTGYRTAFF GKYLNEYNGS YIPPGWREWL GLIKNSRFYN YTVCRNGIKE
KHGFDYAKDY FTDLITNESI NYFKMSKRMY PHRPVMMVIS HAAPHGPEDS APQFSKLYPN
ASQHITPSYN YAPNMDKHWI MQYTGPMLPI HMEFTNVLQR KRLQTLMSVD DSVERLYNML
VETGELGNTY IIYTADHGYH IGQFGLVKGK SMPYDFDIRV PFFIRGPSIE PGSIVPQIVL
NIDLAPTILD IAGLDTPSDV DGKSVLKLLD LEKPGNRFRT NKKAKIWRDT FLVERGKFLR
KKEESSKNIQ QSNHLPKYER VKELCQQARY QTACEQPGQN WQCIEDTSGK LRIHKCKGPS
DLLTVRQNAR NLYSRGLQDK DKECHCRESG YRPSRSQRKK ERQFLRNQGT PKYKPRFVHT
RQTRSLSVEF EGEIYDINLE EEELQVLPPR SVAKRHDEGH QGFGGHQAAA GDFRNEMLAD
SNSAVGLPTT VRVTHKCFIL PNDTIHCERE LYQSARAWKD HKAYIDKEIE VLQDKIKNLR
EVRGHLKKRK PEECSCGKQS YYNKEKGVKR QEKLKSHLHP FKEAAAQEVD SKLQLFKEHR
RRKKERKEKK RQRKGEECSL PGLTCFTHDN NHWQTAPFWN LGSFCACTSS NNNTYWCLRT
VNETHNFLFC EFATGFLEYF DMNTDPYQLT NTVHTVERGI LNQLHIQLME LRSCQGYKQC
NPRPKSLDVG TKEGGNYDPH RGQLWDGWEG
