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Q8K007

- SULF1_MOUSE

UniProt

Q8K007 - SULF1_MOUSE

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Protein
Extracellular sulfatase Sulf-1
Gene
Sulf1, Kiaa1077
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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.

Cofactori

Binds 1 calcium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi51 – 511Calcium By similarity
Metal bindingi52 – 521Calcium By similarity
Metal bindingi87 – 871Calcium; via 3-oxoalanine By similarity
Metal bindingi316 – 3161Calcium By similarity
Metal bindingi317 – 3171Calcium By similarity

GO - Molecular functioni

  1. N-acetylglucosamine-6-sulfatase activity Source: UniProtKB
  2. arylsulfatase activity Source: UniProtKB
  3. calcium ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. bone development Source: BHF-UCL
  3. cartilage condensation Source: UniProtKB
  4. cartilage development Source: UniProtKB
  5. cell adhesion Source: UniProtKB
  6. chondrocyte development Source: UniProtKB
  7. embryonic skeletal system development Source: UniProtKB
  8. esophagus smooth muscle contraction Source: UniProtKB
  9. glial cell-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
  10. glomerular basement membrane development Source: UniProtKB
  11. glomerular filtration Source: UniProtKB
  12. heparan sulfate proteoglycan metabolic process Source: UniProtKB
  13. innervation Source: UniProtKB
  14. kidney development Source: BHF-UCL
  15. limb joint morphogenesis Source: UniProtKB
  16. negative regulation of angiogenesis Source: UniProtKB
  17. negative regulation of cell migration Source: UniProtKB
  18. negative regulation of endothelial cell proliferation Source: UniProtKB
  19. negative regulation of fibroblast growth factor receptor signaling pathway Source: UniProtKB
  20. negative regulation of prostatic bud formation Source: UniProtKB
  21. positive regulation of BMP signaling pathway Source: UniProtKB
  22. positive regulation of Wnt signaling pathway Source: UniProtKB
  23. positive regulation of smooth muscle cell proliferation Source: UniProtKB
  24. positive regulation vascular endothelial growth factor production Source: UniProtKB
  25. sulfur compound metabolic process Source: MGI
  26. vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular sulfatase Sulf-1 (EC:3.1.6.-)
Short name:
mSulf-1
Gene namesi
Name:Sulf1
Synonyms:Kiaa1077
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2138563. Sulf1.

Subcellular locationi

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

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. Golgi stack Source: UniProtKB-SubCell
  3. cell surface Source: UniProtKB
  4. endoplasmic reticulum Source: UniProtKB
  5. extracellular space Source: UniProtKB
  6. membrane raft Source: UniProtKB
  7. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 870848Extracellular sulfatase Sulf-1
PRO_0000033435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...) Reviewed prediction
Modified residuei87 – 8713-oxoalanine (Cys) By similarity
Glycosylationi111 – 1111N-linked (GlcNAc...) Reviewed prediction
Glycosylationi131 – 1311N-linked (GlcNAc...) Reviewed prediction
Glycosylationi148 – 1481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi170 – 1701N-linked (GlcNAc...) Reviewed prediction
Glycosylationi197 – 1971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi240 – 2401N-linked (GlcNAc...) Reviewed prediction
Glycosylationi622 – 6221N-linked (GlcNAc...) Reviewed prediction
Glycosylationi772 – 7721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi782 – 7821N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

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.

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8K007.
PRIDEiQ8K007.

PTM databases

PhosphoSiteiQ8K007.

Expressioni

Gene expression databases

BgeeiQ8K007.
CleanExiMM_SULF1.
GenevestigatoriQ8K007.

Structurei

3D structure databases

ProteinModelPortaliQ8K007.
SMRiQ8K007. Positions 34-411.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00400000022041.
HOGENOMiHOG000290161.
HOVERGENiHBG056431.
KOiK14607.
OMAiKPDECDC.
OrthoDBiEOG7FR7H6.
PhylomeDBiQ8K007.
TreeFamiTF313545.

Family and domain databases

Gene3Di3.40.720.10. 3 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR014615. Extracellular_sulfatase.
IPR024609. Extracellular_sulfatase_C.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF12548. DUF3740. 1 hit.
PF00884. Sulfatase. 1 hit.
[Graphical view]
PIRSFiPIRSF036665. Sulf1. 1 hit.
SUPFAMiSSF53649. SSF53649. 3 hits.
PROSITEiPS00523. SULFATASE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8K007-1 [UniParc]FASTAAdd to Basket

« Hide

MKYSLWALLL AVLGTQLLGS LCSTVRSQRF RGRIQQERKN IRPNIILVLT    50
DDQDVELGSL QVMNKTRKIM EQGGATFTNA FVTTPMCCPS RSSMLTGKYV 100
HNHNVYTNNE NCSSPSWQAM HEPRTFAVYL NNTGYRTAFF GKYLNEYNGS 150
YIPPGWREWL GLIKNSRFYN YTVCRNGIKE KHGFDYAKDY FTDLITNESI 200
NYFKMSKRMY PHRPIMMVIS HAAPHGPEDS APQFSKLYPN ASQHITPSYN 250
YAPNMDKHWI MQYTGPMLPI HMEFTNVLQR KRLQTLMSVD DSVERLYNML 300
VESGELDNTY IIYTADHGYH IGQFGLVKGK SMPYDFDIRV PFFIRGPSIE 350
PGSIVPQIVL NIDLAPTILD IAGLDSPSDV DGKSVLKLLD LEKPGNRFRT 400
NKKAKIWRDT FLVERGKFLR KKEESGKNIQ QSNHLPKYER VKELCQQARY 450
QTACEQPGQN WQCIEDTSGK LRIHKCKGPS DLLTVRQNAR NLYSRGLHDK 500
DKECHCRDSG YRSSRSQRKN QRQFLRNKGT PKYKPRFVHT RQTRSLSVEF 550
EGEIYDINLE EEELQVLPPR SIAKRHDEGH QGFIGHQAAA GDIRNEMLAD 600
SNNAVGLPAT VRVTHKCFIL PNDTIHCERE LYQSARAWKD HKAYIDKEIE 650
VLQDKIKNLR EVRGHLKKRK PEECGCGDQS YYNKEKGVKR QEKLKSHLHP 700
FKEAAAQEVD SKLQLFKEHR RRKKERKEKK RQRKGEECSL PGLTCFTHDN 750
NHWQTAPFWN LGSFCACTSS NNNTYWCLRT VNETHNFLFC EFATGFLEYF 800
DMNTDPYQLT NTVHTVERSI LNQLHIQLME LRSCQGYKQC NPRPKSLDIG 850
AKEGGNYDPH RGQLWDGWEG 870
Length:870
Mass (Da):100,923
Last modified:October 1, 2002 - v1
Checksum:i4A9BE710D7CF4F9D
GO

Sequence cautioni

The sequence BAC32179.1 differs from that shown. Reason: Intron retention.
The sequence BAC98088.1 differs from that shown. Reason: Intron retention. The sequence is a pre-RNA and intronic sequences remain.
The sequence BAC98088.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti486 – 4861R → H in BAC25858. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14820.1.
RefSeqiNP_001185494.1. NM_001198565.1.
NP_001185495.1. NM_001198566.1.
NP_758498.1. NM_172294.1.
UniGeneiMm.45563.

Genome annotation databases

EnsembliENSMUST00000088585; ENSMUSP00000085949; ENSMUSG00000016918.
ENSMUST00000177608; ENSMUSP00000137523; ENSMUSG00000016918.
ENSMUST00000180062; ENSMUSP00000136014; ENSMUSG00000016918.
GeneIDi240725.
KEGGimmu:240725.
UCSCiuc007aia.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14820.1.
RefSeqi NP_001185494.1. NM_001198565.1.
NP_001185495.1. NM_001198566.1.
NP_758498.1. NM_172294.1.
UniGenei Mm.45563.

3D structure databases

ProteinModelPortali Q8K007.
SMRi Q8K007. Positions 34-411.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8K007.

Proteomic databases

PaxDbi Q8K007.
PRIDEi Q8K007.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000088585 ; ENSMUSP00000085949 ; ENSMUSG00000016918 .
ENSMUST00000177608 ; ENSMUSP00000137523 ; ENSMUSG00000016918 .
ENSMUST00000180062 ; ENSMUSP00000136014 ; ENSMUSG00000016918 .
GeneIDi 240725.
KEGGi mmu:240725.
UCSCi uc007aia.2. mouse.

Organism-specific databases

CTDi 23213.
MGIi MGI:2138563. Sulf1.
Rougei Search...

Phylogenomic databases

eggNOGi COG3119.
GeneTreei ENSGT00400000022041.
HOGENOMi HOG000290161.
HOVERGENi HBG056431.
KOi K14607.
OMAi KPDECDC.
OrthoDBi EOG7FR7H6.
PhylomeDBi Q8K007.
TreeFami TF313545.

Miscellaneous databases

ChiTaRSi SULF1. mouse.
NextBioi 384701.
PROi Q8K007.
SOURCEi Search...

Gene expression databases

Bgeei Q8K007.
CleanExi MM_SULF1.
Genevestigatori Q8K007.

Family and domain databases

Gene3Di 3.40.720.10. 3 hits.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR014615. Extracellular_sulfatase.
IPR024609. Extracellular_sulfatase_C.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view ]
Pfami PF12548. DUF3740. 1 hit.
PF00884. Sulfatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036665. Sulf1. 1 hit.
SUPFAMi SSF53649. SSF53649. 3 hits.
PROSITEi PS00523. SULFATASE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiSULF1_MOUSE
AccessioniPrimary (citable) accession number: Q8K007
Secondary accession number(s): Q6ZPZ0, Q8BLJ0, Q8C1D3
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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