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Extracellular sulfatase Sulf-1 (EC 3.1.6.-) (RSulfFP1) (Sulfatase FP)

 SULF1_RAT               Reviewed;         870 AA.
Q8VI60;
19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
23-MAY-2018, entry version 94.
RecName: Full=Extracellular sulfatase Sulf-1;
EC=3.1.6.-;
AltName: Full=RSulfFP1;
AltName: Full=Sulfatase FP;
Flags: Precursor;
Name=Sulf1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Embryo;
PubMed=11895481; DOI=10.1046/j.1356-9597.2001.00502.x;
Ohto T., Uchida H., Yamazaki H., Keino-Masu K., Matsui A., Masu M.;
"Identification of a novel nonlysosomal sulphatase expressed in the
floor plate, choroid plexus and cartilage.";
Genes Cells 7:173-185(2002).
[2]
ERRATUM.
Ohto T., Uchida H., Yamazaki H., Keino-Masu K., Matsui A., Masu M.;
Genes Cells 7:521-522(2002).
-!- FUNCTION: May be involved in the desulfation of sulfated
glycosaminoglycans in the biosynthetic pathway and may play a role
as an extracellular regulator of proteoglycan mediated signaling.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus,
Golgi stack. Cell surface. Note=Also localized on the cell
surface.
-!- TISSUE SPECIFICITY: Strongly expressed in the floor plate, choroid
plexus and cartilage. Weaker expression seen in the eye, lung
brain, spinal cord, urinary bladder, testis, ovary and uterus.
-!- DEVELOPMENTAL STAGE: Abundantly and specifically expressed in the
floor plate region of the spinal cord at embryonic day 13 (E13)
and E15 and at lower levels at postnatal day 1 (P1). A high level
expression was also observed in the ventral hindbrain and
midbrain. No expression was seen in the notochord at these stages.
Prominent expression in the nervous system was also seen in the
choroid plexus. At E13, expression was also seen in the
dorsomedial forebrain and roof of the hind brain. Robust and
specific expression was detected in the choroid plexus epithelium
of the lateral, 3rd and 4th ventricles at E15 and P1 and persisted
into adulthood. In the CNS, expression was detected in thalamic
and hypothalamic regions at E13, E15 and P1. In embryos, it was
highly expressed in the limb buds, face region, large blood
vessels, olfactory pits and pleural epithelium. In particular,
expression was robust and specific in bone-forming regions of the
face and in the mesenchymal cells surrounding the developing
cartilages of the extremities.
-!- PTM: The conversion to 3-oxoalanine (also known as C-
formylglycine, FGly), of a serine or cysteine residue in
prokaryotes and of a cysteine residue in eukaryotes, is critical
for catalytic activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF230072; AAL71906.1; -; mRNA.
RefSeq; NP_599205.1; NM_134378.2.
UniGene; Rn.161961; -.
ProteinModelPortal; Q8VI60; -.
STRING; 10116.ENSRNOP00000012611; -.
PaxDb; Q8VI60; -.
PRIDE; Q8VI60; -.
GeneID; 171396; -.
KEGG; rno:171396; -.
UCSC; RGD:708554; rat.
CTD; 23213; -.
RGD; 708554; Sulf1.
eggNOG; KOG3731; Eukaryota.
eggNOG; COG3119; LUCA.
HOGENOM; HOG000290161; -.
HOVERGEN; HBG056431; -.
InParanoid; Q8VI60; -.
KO; K14607; -.
PhylomeDB; Q8VI60; -.
PRO; PR:Q8VI60; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0004065; F:arylsulfatase activity; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; ISS:UniProtKB.
GO; GO:0060348; P:bone development; ISS:UniProtKB.
GO; GO:0001502; P:cartilage condensation; ISS:UniProtKB.
GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0002063; P:chondrocyte development; ISS:UniProtKB.
GO; GO:0048706; P:embryonic skeletal system development; ISS:UniProtKB.
GO; GO:0014846; P:esophagus smooth muscle contraction; ISS:UniProtKB.
GO; GO:0035860; P:glial cell-derived neurotrophic factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; ISS:UniProtKB.
GO; GO:0060384; P:innervation; ISS:UniProtKB.
GO; GO:0001822; P:kidney development; ISS:UniProtKB.
GO; GO:0036022; P:limb joint morphogenesis; ISS:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0060686; P:negative regulation of prostatic bud formation; ISS:UniProtKB.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR014615; Extracellular_sulfatase.
InterPro; IPR024609; Extracellular_sulfatase_C.
InterPro; IPR024607; Sulfatase_CS.
InterPro; IPR000917; Sulfatase_N.
Pfam; PF12548; DUF3740; 1.
Pfam; PF00884; Sulfatase; 1.
PIRSF; PIRSF036665; Sulf1; 1.
SUPFAM; SSF53649; SSF53649; 3.
PROSITE; PS00523; SULFATASE_1; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Endoplasmic reticulum; Glycoprotein;
Golgi apparatus; Hydrolase; Metal-binding; Reference proteome; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 870 Extracellular sulfatase Sulf-1.
/FTId=PRO_0000033436.
ACT_SITE 87 87 Nucleophile.
{ECO:0000250|UniProtKB:P15289}.
METAL 51 51 Calcium. {ECO:0000250}.
METAL 52 52 Calcium. {ECO:0000250}.
METAL 87 87 Calcium; via 3-oxoalanine. {ECO:0000250}.
METAL 316 316 Calcium. {ECO:0000250}.
METAL 317 317 Calcium. {ECO:0000250}.
MOD_RES 87 87 3-oxoalanine (Cys).
{ECO:0000250|UniProtKB:P15289}.
CARBOHYD 64 64 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 131 131 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 170 170 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 772 772 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 782 782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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