SULF1_MOUSE
ID SULF1_MOUSE Reviewed; 870 AA.
AC Q8K007; Q6ZPZ0; Q8BLJ0; Q8C1D3;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Extracellular sulfatase Sulf-1;
DE Short=mSulf-1;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=Sulf1; Synonyms=Kiaa1077;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12368295; DOI=10.1074/jbc.m205131200;
RA Morimoto-Tomita M., Uchimura K., Werb Z., Hemmerich S., Rosen S.D.;
RT "Cloning and characterization of two extracellular heparin-degrading
RT endosulfatases in mice and humans.";
RL J. Biol. Chem. 277:49175-49185(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, Eye, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Exhibits arylsulfatase activity and highly specific
CC endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-
CC 6 position of glucosamine within specific subregions of intact heparin.
CC Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits
CC signaling by heparin-dependent growth factors, diminishes
CC proliferation, and facilitates apoptosis in response to exogenous
CC stimulation (By similarity). {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32179.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC98088.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98088.1; Type=Miscellaneous discrepancy; Note=Intron retention. The sequence is a pre-RNA and intronic sequences remain.; Evidence={ECO:0000305};
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DR EMBL; AY101178; AAM76863.1; -; mRNA.
DR EMBL; AK129278; BAC98088.1; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK028285; BAC25858.1; -; mRNA.
DR EMBL; AK045002; BAC32179.1; ALT_SEQ; mRNA.
DR EMBL; BC034547; AAH34547.1; -; mRNA.
DR EMBL; BC049276; AAH49276.1; -; mRNA.
DR CCDS; CCDS14820.1; -.
DR RefSeq; NP_001185494.1; NM_001198565.1.
DR RefSeq; NP_001185495.1; NM_001198566.1.
DR RefSeq; NP_758498.1; NM_172294.1.
DR AlphaFoldDB; Q8K007; -.
DR SMR; Q8K007; -.
DR BioGRID; 232231; 3.
DR STRING; 10090.ENSMUSP00000137523; -.
DR GlyGen; Q8K007; 10 sites.
DR iPTMnet; Q8K007; -.
DR PhosphoSitePlus; Q8K007; -.
DR MaxQB; Q8K007; -.
DR PaxDb; Q8K007; -.
DR PRIDE; Q8K007; -.
DR ProteomicsDB; 254693; -.
DR Antibodypedia; 25041; 125 antibodies from 24 providers.
DR DNASU; 240725; -.
DR Ensembl; ENSMUST00000088585; ENSMUSP00000085949; ENSMUSG00000016918.
DR Ensembl; ENSMUST00000177608; ENSMUSP00000137523; ENSMUSG00000016918.
DR Ensembl; ENSMUST00000180062; ENSMUSP00000136014; ENSMUSG00000016918.
DR GeneID; 240725; -.
DR KEGG; mmu:240725; -.
DR UCSC; uc007aia.2; mouse.
DR CTD; 23213; -.
DR MGI; MGI:2138563; Sulf1.
DR VEuPathDB; HostDB:ENSMUSG00000016918; -.
DR eggNOG; KOG3731; Eukaryota.
DR GeneTree; ENSGT00940000157544; -.
DR HOGENOM; CLU_006332_2_0_1; -.
DR InParanoid; Q8K007; -.
DR OMA; QCIEDTA; -.
DR OrthoDB; 1273622at2759; -.
DR PhylomeDB; Q8K007; -.
DR TreeFam; TF313545; -.
DR BioGRID-ORCS; 240725; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Sulf1; mouse.
DR PRO; PR:Q8K007; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8K007; protein.
DR Bgee; ENSMUSG00000016918; Expressed in vestibular membrane of cochlear duct and 250 other tissues.
DR ExpressionAtlas; Q8K007; baseline and differential.
DR Genevisible; Q8K007; MM.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS: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:0005886; C:plasma membrane; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IGI:BHF-UCL.
DR GO; GO:0001502; P:cartilage condensation; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0002063; P:chondrocyte development; IMP:UniProtKB.
DR GO; GO:0048706; P:embryonic skeletal system development; IGI:UniProtKB.
DR GO; GO:0014846; P:esophagus smooth muscle contraction; IGI:UniProtKB.
DR GO; GO:0035860; P:glial cell-derived neurotrophic factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0032836; P:glomerular basement membrane development; IGI:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; IGI:UniProtKB.
DR GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; IMP:UniProtKB.
DR GO; GO:0060384; P:innervation; IGI:UniProtKB.
DR GO; GO:0001822; P:kidney development; IGI:BHF-UCL.
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; IDA:UniProtKB.
DR GO; GO:0060686; P:negative regulation of prostatic bud formation; IDA: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; IGI:UniProtKB.
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:MGI.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:MGI.
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 2: Evidence at transcript level;
KW Apoptosis; Calcium; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Hydrolase; 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_0000033435"
FT REGION 507..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..870
FT /note="Disordered"
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"
FT CONFLICT 486
FT /note="R -> H (in Ref. 2; BAC25858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 100923 MW; 4A9BE710D7CF4F9D CRC64;
MKYSLWALLL AVLGTQLLGS LCSTVRSQRF RGRIQQERKN IRPNIILVLT DDQDVELGSL
QVMNKTRKIM EQGGATFTNA FVTTPMCCPS RSSMLTGKYV HNHNVYTNNE NCSSPSWQAM
HEPRTFAVYL NNTGYRTAFF GKYLNEYNGS YIPPGWREWL GLIKNSRFYN YTVCRNGIKE
KHGFDYAKDY FTDLITNESI NYFKMSKRMY PHRPIMMVIS HAAPHGPEDS APQFSKLYPN
ASQHITPSYN YAPNMDKHWI MQYTGPMLPI HMEFTNVLQR KRLQTLMSVD DSVERLYNML
VESGELDNTY IIYTADHGYH IGQFGLVKGK SMPYDFDIRV PFFIRGPSIE PGSIVPQIVL
NIDLAPTILD IAGLDSPSDV DGKSVLKLLD LEKPGNRFRT NKKAKIWRDT FLVERGKFLR
KKEESGKNIQ QSNHLPKYER VKELCQQARY QTACEQPGQN WQCIEDTSGK LRIHKCKGPS
DLLTVRQNAR NLYSRGLHDK DKECHCRDSG YRSSRSQRKN QRQFLRNKGT PKYKPRFVHT
RQTRSLSVEF EGEIYDINLE EEELQVLPPR SIAKRHDEGH QGFIGHQAAA GDIRNEMLAD
SNNAVGLPAT VRVTHKCFIL PNDTIHCERE LYQSARAWKD HKAYIDKEIE VLQDKIKNLR
EVRGHLKKRK PEECGCGDQS YYNKEKGVKR QEKLKSHLHP FKEAAAQEVD SKLQLFKEHR
RRKKERKEKK RQRKGEECSL PGLTCFTHDN NHWQTAPFWN LGSFCACTSS NNNTYWCLRT
VNETHNFLFC EFATGFLEYF DMNTDPYQLT NTVHTVERSI LNQLHIQLME LRSCQGYKQC
NPRPKSLDIG AKEGGNYDPH RGQLWDGWEG
