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Protein

Sulfatase-modifying factor 1

Gene

Sumf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Using molecular oxygen and an unidentified reducing agent, oxidizes a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also called C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS and ARSE (By similarity).By similarity

Catalytic activityi

[sulfatase]-cysteine + acceptor = [sulfatase]-3-oxoalanine + reduced acceptor.

Pathwayi: sulfatase oxidation

This protein is involved in the pathway sulfatase oxidation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway sulfatase oxidation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi128 – 1281Calcium 2By similarity
Metal bindingi257 – 2571Calcium 1By similarity
Metal bindingi258 – 2581Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi271 – 2711Calcium 1By similarity
Metal bindingi273 – 2731Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi291 – 2911Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi294 – 2941Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi298 – 2981Calcium 2By similarity
Active sitei331 – 3311Proton acceptorBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: UniProtKB-KW
  • protein homodimerization activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-1660662. Glycosphingolipid metabolism.
R-MMU-1663150. The activation of arylsulfatases.
UniPathwayiUPA00910.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfatase-modifying factor 1 (EC:1.8.99.-)
Alternative name(s):
C-alpha-formylglycine-generating enzyme 1
Gene namesi
Name:Sumf1
Synonyms:Fge
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1889844. Sumf1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131By similarityAdd
BLAST
Chaini32 – 372341Sulfatase-modifying factor 1PRO_0000033457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 ↔ 50
Glycosylationi139 – 1391N-linked (GlcNAc...)By similarity
Disulfide bondi216 ↔ 363By similarity
Disulfide bondi233 ↔ 344By similarity
Disulfide bondi334 ↔ 339Redox-activeBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8R0F3.
MaxQBiQ8R0F3.
PaxDbiQ8R0F3.
PRIDEiQ8R0F3.

PTM databases

PhosphoSiteiQ8R0F3.

Expressioni

Gene expression databases

BgeeiQ8R0F3.
CleanExiMM_SUMF1.
ExpressionAtlasiQ8R0F3. baseline and differential.
GenevisibleiQ8R0F3. MM.

Interactioni

Subunit structurei

Monomer, homodimer and heterodimer with SUMF2.By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi208463. 2 interactions.
IntActiQ8R0F3. 2 interactions.
MINTiMINT-4136123.
STRINGi10090.ENSMUSP00000032191.

Structurei

3D structure databases

ProteinModelPortaliQ8R0F3.
SMRiQ8R0F3. Positions 84-369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase-modifying factor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IEYZ. Eukaryota.
COG1262. LUCA.
GeneTreeiENSGT00390000008983.
HOGENOMiHOG000135466.
HOVERGENiHBG054193.
InParanoidiQ8R0F3.
KOiK13444.
OMAiWTADLWD.
OrthoDBiEOG7VX8WN.
PhylomeDBiQ8R0F3.
TreeFamiTF324027.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR005532. SUMF_dom.
[Graphical view]
PfamiPF03781. FGE-sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q8R0F3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPAREPAL RCCIRLARVF LLLVLACEVA GSDEAEAREG AASLAGSCGC
60 70 80 90 100
GTPQRAGAHG SSAAAQRYSR EANAPGLTSG PRPLALTKMV PIPAGVFTMG
110 120 130 140 150
TDDPQIRQDG EAPARRVTVD GFYMDAYEVS NADFEKFVNS TGYLTEAEKF
160 170 180 190 200
GDSFVFEGML SEQVKTHIHQ AVAAAPWWLP VKGANWRHPE GPDSSILHRS
210 220 230 240 250
NHPVLHVSWN DAVAYCTWAG KRLPTEAEWE YSCRGGLQNR LFPWGNKLQP
260 270 280 290 300
KGQHYANIWQ GKFPVSNTGE DGFQGTAPVD AFPPNGYGLY NIVGNVWEWT
310 320 330 340 350
SDWWTVHHSV EETFNPKGPT SGKDRVKKGG SYMCHKSYCY RYRCAARSQN
360 370
TPDSSASNLG FRCAADHLPT AD
Length:372
Mass (Da):40,659
Last modified:July 25, 2003 - v2
Checksum:i3C96D488B4291068
GO

Sequence cautioni

The sequence AAH26981.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE30762.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391E → V in BAE34887 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK151874 mRNA. Translation: BAE30762.1. Different initiation.
AK159192 mRNA. Translation: BAE34887.1.
AK160917 mRNA. Translation: BAE36091.1.
AK161203 mRNA. Translation: BAE36238.1.
BC026981 mRNA. Translation: AAH26981.1. Different initiation.
CCDSiCCDS51868.1.
RefSeqiNP_666049.2. NM_145937.3.
UniGeneiMm.439876.

Genome annotation databases

EnsembliENSMUST00000032191; ENSMUSP00000032191; ENSMUSG00000030101.
GeneIDi58911.
KEGGimmu:58911.
UCSCiuc009ddf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK151874 mRNA. Translation: BAE30762.1. Different initiation.
AK159192 mRNA. Translation: BAE34887.1.
AK160917 mRNA. Translation: BAE36091.1.
AK161203 mRNA. Translation: BAE36238.1.
BC026981 mRNA. Translation: AAH26981.1. Different initiation.
CCDSiCCDS51868.1.
RefSeqiNP_666049.2. NM_145937.3.
UniGeneiMm.439876.

3D structure databases

ProteinModelPortaliQ8R0F3.
SMRiQ8R0F3. Positions 84-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208463. 2 interactions.
IntActiQ8R0F3. 2 interactions.
MINTiMINT-4136123.
STRINGi10090.ENSMUSP00000032191.

PTM databases

PhosphoSiteiQ8R0F3.

Proteomic databases

EPDiQ8R0F3.
MaxQBiQ8R0F3.
PaxDbiQ8R0F3.
PRIDEiQ8R0F3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032191; ENSMUSP00000032191; ENSMUSG00000030101.
GeneIDi58911.
KEGGimmu:58911.
UCSCiuc009ddf.2. mouse.

Organism-specific databases

CTDi285362.
MGIiMGI:1889844. Sumf1.

Phylogenomic databases

eggNOGiENOG410IEYZ. Eukaryota.
COG1262. LUCA.
GeneTreeiENSGT00390000008983.
HOGENOMiHOG000135466.
HOVERGENiHBG054193.
InParanoidiQ8R0F3.
KOiK13444.
OMAiWTADLWD.
OrthoDBiEOG7VX8WN.
PhylomeDBiQ8R0F3.
TreeFamiTF324027.

Enzyme and pathway databases

UniPathwayiUPA00910.
ReactomeiR-MMU-1660662. Glycosphingolipid metabolism.
R-MMU-1663150. The activation of arylsulfatases.

Miscellaneous databases

PROiQ8R0F3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R0F3.
CleanExiMM_SUMF1.
ExpressionAtlasiQ8R0F3. baseline and differential.
GenevisibleiQ8R0F3. MM.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR005532. SUMF_dom.
[Graphical view]
PfamiPF03781. FGE-sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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 marrow macrophage and Head.
  2. "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: C57BL/6J.
    Tissue: Retina.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Testis.

Entry informationi

Entry nameiSUMF1_MOUSE
AccessioniPrimary (citable) accession number: Q8R0F3
Secondary accession number(s): Q3TTT6, Q3TXM8, Q3U9A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: July 25, 2003
Last modified: June 8, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The resulting 3-oxoalanine in the substrate protein is called C(alpha)-formylglycine by many authors. It should not be confused with N-formylglycine.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.