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Q8K007 (SULF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Extracellular sulfatase Sulf-1

Short name=mSulf-1
EC=3.1.6.-
Gene names
Name:Sulf1
Synonyms:Kiaa1077
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length870 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin. Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits signaling by heparin-dependent growth factors, diminishes proliferation, and facilitates apoptosis in response to exogenous stimulation By similarity.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Endoplasmic reticulum By similarity. Golgi apparatusGolgi stack By similarity. Cell surface By similarity. Note: Also localized on the cell surface By similarity.

Post-translational modification

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 By similarity.

Sequence similarities

Belongs to the sulfatase family.

Sequence caution

The sequence BAC32179.1 differs from that shown. Reason: Intron retention.

The sequence BAC98088.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC98088.1 differs from that shown. Reason: Intron retention. The sequence is a pre-RNA and intronic sequences remain.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentEndoplasmic reticulum
Golgi apparatus
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

bone development

Inferred from genetic interaction PubMed 17593974. Source: BHF-UCL

cartilage condensation

Inferred from sequence or structural similarity. Source: UniProtKB

cartilage development

Inferred from mutant phenotype PubMed 20479257. Source: UniProtKB

cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

chondrocyte development

Inferred from mutant phenotype PubMed 20479257. Source: UniProtKB

embryonic skeletal system development

Inferred from genetic interaction PubMed 18213582. Source: UniProtKB

esophagus smooth muscle contraction

Inferred from genetic interaction PubMed 17720696. Source: UniProtKB

glial cell-derived neurotrophic factor receptor signaling pathway

Inferred from direct assay PubMed 17720696. Source: UniProtKB

glomerular basement membrane development

Inferred from genetic interaction PubMed 21719793. Source: UniProtKB

glomerular filtration

Inferred from genetic interaction PubMed 21719793. Source: UniProtKB

heparan sulfate proteoglycan metabolic process

Inferred from mutant phenotype PubMed 18687675. Source: UniProtKB

innervation

Inferred from genetic interaction PubMed 17720696. Source: UniProtKB

kidney development

Inferred from genetic interaction PubMed 17593974. Source: BHF-UCL

limb joint morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fibroblast growth factor receptor signaling pathway

Inferred from direct assay PubMed 20410206. Source: UniProtKB

negative regulation of prostatic bud formation

Inferred from direct assay PubMed 20410206. Source: UniProtKB

positive regulation of BMP signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation vascular endothelial growth factor production

Inferred from genetic interaction PubMed 21719793. Source: UniProtKB

sulfur compound metabolic process

Inferred from sequence orthology Ref.1. Source: MGI

vascular endothelial growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi stack

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 21719793. Source: UniProtKB

   Molecular_functionN-acetylglucosamine-6-sulfatase activity

Inferred from mutant phenotype PubMed 18687675. Source: UniProtKB

arylsulfatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 870848Extracellular sulfatase Sulf-1
PRO_0000033435

Sites

Metal binding511Calcium By similarity
Metal binding521Calcium By similarity
Metal binding871Calcium; via 3-oxoalanine By similarity
Metal binding3161Calcium By similarity
Metal binding3171Calcium By similarity

Amino acid modifications

Modified residue8713-oxoalanine (Cys) By similarity
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation6221N-linked (GlcNAc...) Potential
Glycosylation7721N-linked (GlcNAc...) Potential
Glycosylation7821N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict4861R → H in BAC25858. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8K007 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 4A9BE710D7CF4F9D

FASTA870100,923
        10         20         30         40         50         60 
MKYSLWALLL AVLGTQLLGS LCSTVRSQRF RGRIQQERKN IRPNIILVLT DDQDVELGSL 

        70         80         90        100        110        120 
QVMNKTRKIM EQGGATFTNA FVTTPMCCPS RSSMLTGKYV HNHNVYTNNE NCSSPSWQAM 

       130        140        150        160        170        180 
HEPRTFAVYL NNTGYRTAFF GKYLNEYNGS YIPPGWREWL GLIKNSRFYN YTVCRNGIKE 

       190        200        210        220        230        240 
KHGFDYAKDY FTDLITNESI NYFKMSKRMY PHRPIMMVIS HAAPHGPEDS APQFSKLYPN 

       250        260        270        280        290        300 
ASQHITPSYN YAPNMDKHWI MQYTGPMLPI HMEFTNVLQR KRLQTLMSVD DSVERLYNML 

       310        320        330        340        350        360 
VESGELDNTY IIYTADHGYH IGQFGLVKGK SMPYDFDIRV PFFIRGPSIE PGSIVPQIVL 

       370        380        390        400        410        420 
NIDLAPTILD IAGLDSPSDV DGKSVLKLLD LEKPGNRFRT NKKAKIWRDT FLVERGKFLR 

       430        440        450        460        470        480 
KKEESGKNIQ QSNHLPKYER VKELCQQARY QTACEQPGQN WQCIEDTSGK LRIHKCKGPS 

       490        500        510        520        530        540 
DLLTVRQNAR NLYSRGLHDK DKECHCRDSG YRSSRSQRKN QRQFLRNKGT PKYKPRFVHT 

       550        560        570        580        590        600 
RQTRSLSVEF EGEIYDINLE EEELQVLPPR SIAKRHDEGH QGFIGHQAAA GDIRNEMLAD 

       610        620        630        640        650        660 
SNNAVGLPAT VRVTHKCFIL PNDTIHCERE LYQSARAWKD HKAYIDKEIE VLQDKIKNLR 

       670        680        690        700        710        720 
EVRGHLKKRK PEECGCGDQS YYNKEKGVKR QEKLKSHLHP FKEAAAQEVD SKLQLFKEHR 

       730        740        750        760        770        780 
RRKKERKEKK RQRKGEECSL PGLTCFTHDN NHWQTAPFWN LGSFCACTSS NNNTYWCLRT 

       790        800        810        820        830        840 
VNETHNFLFC EFATGFLEYF DMNTDPYQLT NTVHTVERSI LNQLHIQLME LRSCQGYKQC 

       850        860        870 
NPRPKSLDIG AKEGGNYDPH RGQLWDGWEG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of two extracellular heparin-degrading endosulfatases in mice and humans."
Morimoto-Tomita M., Uchimura K., Werb Z., Hemmerich S., Rosen S.D.
J. Biol. Chem. 277:49175-49185(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryonic tail.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Head.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo, Eye and Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY101178 mRNA. Translation: AAM76863.1.
AK129278 Transcribed RNA. Translation: BAC98088.1. Sequence problems.
AK028285 mRNA. Translation: BAC25858.1.
AK045002 mRNA. Translation: BAC32179.1. Sequence problems.
BC034547 mRNA. Translation: AAH34547.1.
BC049276 mRNA. Translation: AAH49276.1.
CCDSCCDS14820.1.
RefSeqNP_001185494.1. NM_001198565.1.
NP_001185495.1. NM_001198566.1.
NP_758498.1. NM_172294.1.
UniGeneMm.45563.

3D structure databases

ProteinModelPortalQ8K007.
SMRQ8K007. Positions 34-411.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8K007.

Proteomic databases

PaxDbQ8K007.
PRIDEQ8K007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000088585; ENSMUSP00000085949; ENSMUSG00000016918.
ENSMUST00000177608; ENSMUSP00000137523; ENSMUSG00000016918.
ENSMUST00000180062; ENSMUSP00000136014; ENSMUSG00000016918.
GeneID240725.
KEGGmmu:240725.
UCSCuc007aia.2. mouse.

Organism-specific databases

CTD23213.
MGIMGI:2138563. Sulf1.
RougeSearch...

Phylogenomic databases

eggNOGCOG3119.
GeneTreeENSGT00400000022041.
HOGENOMHOG000290161.
HOVERGENHBG056431.
KOK14607.
OMAKPDECDC.
OrthoDBEOG7FR7H6.
PhylomeDBQ8K007.
TreeFamTF313545.

Gene expression databases

BgeeQ8K007.
CleanExMM_SULF1.
GenevestigatorQ8K007.

Family and domain databases

Gene3D3.40.720.10. 3 hits.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR014615. Extracellular_sulfatase.
IPR024609. Extracellular_sulfatase_C.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamPF12548. DUF3740. 1 hit.
PF00884. Sulfatase. 1 hit.
[Graphical view]
PIRSFPIRSF036665. Sulf1. 1 hit.
SUPFAMSSF53649. SSF53649. 3 hits.
PROSITEPS00523. SULFATASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSULF1. mouse.
NextBio384701.
PROQ8K007.
SOURCESearch...

Entry information

Entry nameSULF1_MOUSE
AccessionPrimary (citable) accession number: Q8K007
Secondary accession number(s): Q6ZPZ0, Q8BLJ0, Q8C1D3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot