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Protein

Extracellular sulfatase Sulf-2

Gene

Sulf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521CalciumBy similarity
Metal bindingi53 – 531CalciumBy similarity
Metal bindingi88 – 881Calcium; via 3-oxoalanineBy similarity
Metal bindingi317 – 3171CalciumBy similarity
Metal bindingi318 – 3181CalciumBy similarity

GO - Molecular functioni

  • arylsulfatase activity Source: UniProtKB
  • calcium ion binding Source: InterPro
  • N-acetylglucosamine-6-sulfatase activity Source: UniProtKB

GO - Biological processi

  • bone development Source: BHF-UCL
  • cartilage development Source: UniProtKB
  • chondrocyte development Source: UniProtKB
  • embryonic skeletal system development Source: UniProtKB
  • esophagus smooth muscle contraction Source: UniProtKB
  • glial cell-derived neurotrophic factor receptor signaling pathway Source: UniProtKB
  • glomerular basement membrane development Source: UniProtKB
  • glomerular filtration Source: UniProtKB
  • heparan sulfate proteoglycan metabolic process Source: UniProtKB
  • innervation Source: UniProtKB
  • kidney development Source: BHF-UCL
  • liver regeneration Source: MGI
  • negative regulation of fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • positive regulation of canonical Wnt signaling pathway Source: MGI
  • positive regulation of catenin import into nucleus Source: MGI
  • positive regulation of vascular endothelial growth factor production Source: UniProtKB
  • positive regulation of Wnt signaling pathway Source: MGI
  • regulation of hepatocyte proliferation Source: MGI
  • response to wounding Source: MGI
  • sulfur compound metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular sulfatase Sulf-2 (EC:3.1.6.-)
Short name:
mSulf-2
Gene namesi
Name:Sulf2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1919293. Sulf2.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • endoplasmic reticulum Source: MGI
  • extracellular space Source: MGI
  • Golgi stack Source: UniProtKB-SubCell
  • 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 – 2424Sequence analysisAdd
BLAST
Chaini25 – 875851Extracellular sulfatase Sulf-2PRO_0000033441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence analysis
Modified residuei88 – 8813-oxoalanine (Cys)By similarity
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence analysis
Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence analysis
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence analysis
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis
Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence analysis
Glycosylationi566 – 5661N-linked (GlcNAc...)Sequence analysis
Glycosylationi613 – 6131N-linked (GlcNAc...)Sequence analysis
Glycosylationi722 – 7221N-linked (GlcNAc...)Sequence analysis
Glycosylationi759 – 7591N-linked (GlcNAc...)Sequence analysis
Glycosylationi769 – 7691N-linked (GlcNAc...)Sequence analysis

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

MaxQBiQ8CFG0.
PaxDbiQ8CFG0.
PRIDEiQ8CFG0.

PTM databases

iPTMnetiQ8CFG0.
PhosphoSiteiQ8CFG0.

Expressioni

Gene expression databases

BgeeiQ8CFG0.
CleanExiMM_SULF2.
GenevisibleiQ8CFG0. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000085405.

Structurei

3D structure databases

ProteinModelPortaliQ8CFG0.
SMRiQ8CFG0. Positions 35-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3731. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00400000022041.
HOVERGENiHBG056431.
InParanoidiQ8CFG0.
KOiK14607.
OMAiCDCHRIS.
OrthoDBiEOG7FR7H6.
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.
IPR024607. Sulfatase_CS.
IPR000917. Sulfatase_N.
[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.

Q8CFG0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPPGLPLWL LSTALLSLLA GSSAFLSHPR LKGRFQRDRR NIRPNIILVL
60 70 80 90 100
TDDQDVELGS MQVMNKTRRI MEQGGAHFIN AFVTTPMCCP SRSSILTGKY
110 120 130 140 150
VHNHNTYTNN ENCSSPSWQA QHESRTFAVY LNSTGYRTAF FGKYLNEYNG
160 170 180 190 200
SYVPPGWKEW VGLLKNSRFY NYTLCRNGVK EKHGSDYSTD YLTDLITNDS
210 220 230 240 250
VSFFRTSKKM YPHRPVLMVI SHAAPHGPED SAPQYSRLFP NASQHITPSY
260 270 280 290 300
NYAPNPDKHW IMRYTGPMKP IHMEFTNMLQ RKRLQTLMSV DDSMETIYDM
310 320 330 340 350
LVETGELDNT YILYTADHGY HIGQFGLVKG KSMPYEFDIR VPFYVRGPNV
360 370 380 390 400
EAGSLNPHIV LNIDLAPTIL DIAGLDIPAD MDGKSILKLL DSERPVNRFH
410 420 430 440 450
LKKKLRVWRD SFLVERGKLL HKREGDKVNA QEENFLPKYQ RVKDLCQRAE
460 470 480 490 500
YQTACEQLGQ KWQCVEDASG TLKLHKCKGP MRFGGGGGSR ALSNLVPKYD
510 520 530 540 550
GQSSEACSCD SGGGGDYKLG LAGRRKLFKK KYKTSYARNR SIRSVAIEVD
560 570 580 590 600
GEIYHVGLDT VPQPRNLSKP HWPGAPEDQD DKDGGSFSGT GGLPDYSAPN
610 620 630 640 650
PIKVTHRCYI LENDTVQCDL DLYKSLQAWK DHKLHIDHEI ETLQNKIKNL
660 670 680 690 700
REVRGHLKKK RPEECDCHRI SYHSQHKGRL KHKGSSLHPF RKGLQEKDKV
710 720 730 740 750
WLLREQKRKK KLRKLLKRLQ NNDTCSMPGL TCFTHDNHHW QTAPLWTLGP
760 770 780 790 800
FCACTSANNN TYWCLRTINE THNFLFCEFA TGFIEYFDLS TDPYQLMNAV
810 820 830 840 850
NTLDRDVLNQ LHVQLMELRS CKGYKQCNPR TRNMDLGLRD GGSYEQYRQF
860 870
QRRKWPEMKR PSSKSLGQLW EGWEG
Length:875
Mass (Da):100,497
Last modified:July 27, 2011 - v2
Checksum:iA04AE401029FCCDC
GO

Sequence cautioni

The sequence BAB25464.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311L → F in BAC38279 (PubMed:16141072).Curated
Sequence conflicti285 – 2851Q → H in BAC26165 (PubMed:16141072).Curated
Sequence conflicti534 – 5341T → A in BAC26165 (PubMed:16141072).Curated
Sequence conflicti614 – 6141D → G in BAC26165 (PubMed:16141072).Curated
Sequence conflicti669 – 6691R → K in AAM76862 (PubMed:12368295).Curated
Sequence conflicti669 – 6691R → K in AAH27238 (PubMed:15489334).Curated
Sequence conflicti669 – 6691R → K in AAI41087 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY101177 mRNA. Translation: AAM76862.1.
AK008108 mRNA. Translation: BAB25464.1. Different initiation.
AK028874 mRNA. Translation: BAC26165.1.
AK034712 mRNA. Translation: BAC28804.2.
AK036685 mRNA. Translation: BAC29534.1.
AK049170 mRNA. Translation: BAC33584.1.
AK081643 mRNA. Translation: BAC38279.1.
AK133336 mRNA. Translation: BAE21607.1.
AK165183 mRNA. Translation: BAE38065.1.
AL589873 Genomic DNA. Translation: CAM13978.1.
BC027238 mRNA. Translation: AAH27238.2.
BC141086 mRNA. Translation: AAI41087.1.
CCDSiCCDS17086.1.
RefSeqiNP_001239507.1. NM_001252578.1.
NP_001239508.1. NM_001252579.1.
NP_082348.2. NM_028072.5.
XP_006500272.1. XM_006500209.2.
XP_006500273.1. XM_006500210.2.
XP_006500274.1. XM_006500211.2.
UniGeneiMm.1011.

Genome annotation databases

EnsembliENSMUST00000088086; ENSMUSP00000085405; ENSMUSG00000006800.
ENSMUST00000109249; ENSMUSP00000104872; ENSMUSG00000006800.
GeneIDi72043.
KEGGimmu:72043.
UCSCiuc008nyk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY101177 mRNA. Translation: AAM76862.1.
AK008108 mRNA. Translation: BAB25464.1. Different initiation.
AK028874 mRNA. Translation: BAC26165.1.
AK034712 mRNA. Translation: BAC28804.2.
AK036685 mRNA. Translation: BAC29534.1.
AK049170 mRNA. Translation: BAC33584.1.
AK081643 mRNA. Translation: BAC38279.1.
AK133336 mRNA. Translation: BAE21607.1.
AK165183 mRNA. Translation: BAE38065.1.
AL589873 Genomic DNA. Translation: CAM13978.1.
BC027238 mRNA. Translation: AAH27238.2.
BC141086 mRNA. Translation: AAI41087.1.
CCDSiCCDS17086.1.
RefSeqiNP_001239507.1. NM_001252578.1.
NP_001239508.1. NM_001252579.1.
NP_082348.2. NM_028072.5.
XP_006500272.1. XM_006500209.2.
XP_006500273.1. XM_006500210.2.
XP_006500274.1. XM_006500211.2.
UniGeneiMm.1011.

3D structure databases

ProteinModelPortaliQ8CFG0.
SMRiQ8CFG0. Positions 35-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000085405.

PTM databases

iPTMnetiQ8CFG0.
PhosphoSiteiQ8CFG0.

Proteomic databases

MaxQBiQ8CFG0.
PaxDbiQ8CFG0.
PRIDEiQ8CFG0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000088086; ENSMUSP00000085405; ENSMUSG00000006800.
ENSMUST00000109249; ENSMUSP00000104872; ENSMUSG00000006800.
GeneIDi72043.
KEGGimmu:72043.
UCSCiuc008nyk.2. mouse.

Organism-specific databases

CTDi55959.
MGIiMGI:1919293. Sulf2.

Phylogenomic databases

eggNOGiKOG3731. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00400000022041.
HOVERGENiHBG056431.
InParanoidiQ8CFG0.
KOiK14607.
OMAiCDCHRIS.
OrthoDBiEOG7FR7H6.
TreeFamiTF313545.

Miscellaneous databases

ChiTaRSiSulf2. mouse.
NextBioi335292.
PROiQ8CFG0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CFG0.
CleanExiMM_SULF2.
GenevisibleiQ8CFG0. MM.

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.
IPR024607. Sulfatase_CS.
IPR000917. Sulfatase_N.
[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]
ProtoNetiSearch...

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].
    Tissue: Mammary tumor.
  2. "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: Bone, Cervix squamous cell, Embryo, Embryonic stem cell, Head, Skin and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: Czech II.
    Tissue: Brain and Mammary gland.

Entry informationi

Entry nameiSULF2_MOUSE
AccessioniPrimary (citable) accession number: Q8CFG0
Secondary accession number(s): B2RUD5
, Q3TNM3, Q8BM68, Q8BUZ4, Q8BX28, Q8BZ51, Q8C169, Q9D8E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: July 27, 2011
Last modified: February 17, 2016
This is version 109 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.