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Q8IWU6 (SULF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Extracellular sulfatase Sulf-1

Short name=hSulf-1
EC=3.1.6.-
Gene names
Name:SULF1
Synonyms:KIAA1077
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length871 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

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.

Tissue specificity

Expressed at highest levels in testis, stomach, skeletal muscle, lung, kidney, pancreas, small intestine and colon. It is also detected in normal ovarian surface epithelial cells. Down-regulation seen in ovarian carcinoma cell lines, ovarian cancers, breast, pancreatic, renal and hepatocellular carcinoma cell lines.

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.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0-8.0.

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 sequence or structural similarity. Source: BHF-UCL

cartilage development

Inferred from sequence or structural similarity. Source: UniProtKB

chondrocyte development

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic skeletal system development

Inferred from sequence or structural similarity. Source: UniProtKB

esophagus smooth muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

glial cell-derived neurotrophic factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular basement membrane development

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular filtration

Inferred from sequence or structural similarity. Source: UniProtKB

heparan sulfate proteoglycan metabolic process

Inferred from direct assay PubMed 18687675PubMed 19666466PubMed 19822709. Source: UniProtKB

innervation

Inferred from sequence or structural similarity. Source: UniProtKB

kidney development

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of angiogenesis

Inferred from direct assay PubMed 16778174. Source: UniProtKB

negative regulation of cell migration

Inferred from mutant phenotype PubMed 21266348. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from direct assay PubMed 16778174. Source: UniProtKB

negative regulation of fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 20479257. Source: UniProtKB

negative regulation of prostatic bud formation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of BMP signaling pathway

Inferred from mutant phenotype PubMed 20479257. Source: UniProtKB

positive regulation of Wnt signaling pathway

Inferred from direct assay PubMed 19520866. Source: UniProtKB

positive regulation vascular endothelial growth factor production

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 21266348. Source: UniProtKB

vascular endothelial growth factor receptor signaling pathway

Inferred from direct assay PubMed 16778174. 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 direct assay Ref.1PubMed 18687675PubMed 19520866PubMed 19666466. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 18687675. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 19666466. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 19520866. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionN-acetylglucosamine-6-sulfatase activity

Inferred from direct assay PubMed 18687675PubMed 19666466. Source: UniProtKB

arylsulfatase activity

Inferred from direct assay Ref.1. 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 – 871849Extracellular sulfatase Sulf-1
PRO_0000033434

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...) Ref.5
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Potential
Glycosylation7731N-linked (GlcNAc...) Potential
Glycosylation7831N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis87 – 882CC → AA: Loss of arylsulfatase activity and loss of ability to modulate apoptosis. Ref.1 Ref.2
Sequence conflict491L → P in AAO33315. Ref.2
Sequence conflict7281K → R in BAC11258. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q8IWU6 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 9A90ADB280304364

FASTA871101,027
        10         20         30         40         50         60 
MKYSCCALVL AVLGTELLGS LCSTVRSPRF RGRIQQERKN IRPNIILVLT DDQDVELGSL 

        70         80         90        100        110        120 
QVMNKTRKIM EHGGATFINA 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 PHRPVMMVIS HAAPHGPEDS APQFSKLYPN 

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

       310        320        330        340        350        360 
VETGELENTY IIYTADHGYH IGQFGLVKGK SMPYDFDIRV PFFIRGPSVE PGSIVPQIVL 

       370        380        390        400        410        420 
NIDLAPTILD IAGLDTPPDV DGKSVLKLLD PEKPGNRFRT NKKAKIWRDT FLVERGKFLR 

       430        440        450        460        470        480 
KKEESSKNIQ QSNHLPKYER VKELCQQARY QTACEQPGQK WQCIEDTSGK LRIHKCKGPS 

       490        500        510        520        530        540 
DLLTVRQSTR NLYARGFHDK DKECSCRESG YRASRSQRKS QRQFLRNQGT PKYKPRFVHT 

       550        560        570        580        590        600 
RQTRSLSVEF EGEIYDINLE EEEELQVLQP RNIAKRHDEG HKGPRDLQAS SGGNRGRMLA 

       610        620        630        640        650        660 
DSSNAVGPPT TVRVTHKCFI LPNDSIHCER ELYQSARAWK DHKAYIDKEI EALQDKIKNL 

       670        680        690        700        710        720 
REVRGHLKRR KPEECSCSKQ SYYNKEKGVK KQEKLKSHLH PFKEAAQEVD SKLQLFKENN 

       730        740        750        760        770        780 
RRRKKERKEK RRQRKGEECS LPGLTCFTHD NNHWQTAPFW NLGSFCACTS SNNNTYWCLR 

       790        800        810        820        830        840 
TVNETHNFLF CEFATGFLEY FDMNTDPYQL TNTVHTVERG ILNQLHVQLM ELRSCQGYKQ 

       850        860        870 
CNPRPKNLDV GNKDGGSYDL HRGQLWDGWE G 

« 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], CHARACTERIZATION, MUTAGENESIS OF 87-CYS-CYS-88.
Tissue: Prostate.
[2]"Loss of HSulf-1 up-regulates heparin-binding growth factor signaling in cancer."
Lai J., Chien J., Staub J., Avula R., Greene E.L., Matthews T.A., Smith D.I., Kaufmann S.H., Roberts L.R., Shridhar V.
J. Biol. Chem. 278:23107-23117(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF 87-CYS-CYS-88.
[3]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-871.
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-871.
Tissue: Teratocarcinoma.
[5]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-197.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY101175 mRNA. Translation: AAM76860.1.
AF545571 mRNA. Translation: AAO33315.1.
AB029000 mRNA. Translation: BAA83029.1.
AK074873 mRNA. Translation: BAC11258.1.
RefSeqNP_001121676.1. NM_001128204.1.
NP_001121677.1. NM_001128205.1.
NP_001121678.1. NM_001128206.1.
NP_055985.2. NM_015170.2.
UniGeneHs.409602.

3D structure databases

ProteinModelPortalQ8IWU6.
SMRQ8IWU6. Positions 42-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116820. 2 interactions.
STRING9606.ENSP00000260128.

PTM databases

PhosphoSiteQ8IWU6.

Polymorphism databases

DMDM33112447.

Proteomic databases

PaxDbQ8IWU6.
PRIDEQ8IWU6.

Protocols and materials databases

DNASU23213.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260128; ENSP00000260128; ENSG00000137573.
ENST00000402687; ENSP00000385704; ENSG00000137573.
ENST00000419716; ENSP00000390315; ENSG00000137573.
ENST00000458141; ENSP00000403040; ENSG00000137573.
GeneID23213.
KEGGhsa:23213.
UCSCuc003xyd.2. human.

Organism-specific databases

CTD23213.
GeneCardsGC08P070428.
HGNCHGNC:20391. SULF1.
HPAHPA054728.
MIM610012. gene.
neXtProtNX_Q8IWU6.
Orphanet2496. Mesomelia-synostoses syndrome.
PharmGKBPA134861022.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3119.
HOGENOMHOG000290161.
HOVERGENHBG056431.
InParanoidQ8IWU6.
KOK14607.
OMASVRVTHK.
OrthoDBEOG7FR7H6.
PhylomeDBQ8IWU6.
TreeFamTF313545.

Gene expression databases

ArrayExpressQ8IWU6.
BgeeQ8IWU6.
CleanExHS_SULF1.
GenevestigatorQ8IWU6.

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. human.
GeneWikiSULF1.
GenomeRNAi23213.
NextBio44771.
PROQ8IWU6.
SOURCESearch...

Entry information

Entry nameSULF1_HUMAN
AccessionPrimary (citable) accession number: Q8IWU6
Secondary accession number(s): Q86YV8, Q8NCA2, Q9UPS5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM