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Protein

Sulfatase-modifying factor 1

Gene

SUMF1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 bindingi130 – 1301Calcium 2By similarity
Metal bindingi259 – 2591Calcium 1By similarity
Metal bindingi260 – 2601Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi273 – 2731Calcium 1By similarity
Metal bindingi275 – 2751Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi293 – 2931Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi296 – 2961Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi298 – 2981Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi300 – 3001Calcium 2By similarity
Active sitei333 – 3331Proton acceptorCurated

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-1660662. Glycosphingolipid metabolism.
R-BTA-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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 22

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333By similarityAdd
BLAST
Chaini34 – 374341Sulfatase-modifying factor 1PRO_0000333034Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 52By similarity
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence analysis
Disulfide bondi218 ↔ 365By similarity
Disulfide bondi235 ↔ 346By similarity
Disulfide bondi336 ↔ 341Redox-activeBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ0P5L5.
PRIDEiQ0P5L5.

Interactioni

Subunit structurei

Monomer, homodimer and heterodimer with SUMF2.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000052631.

Structurei

3D structure databases

ProteinModelPortaliQ0P5L5.
SMRiQ0P5L5. Positions 89-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni341 – 36020Interaction with sulfatasesBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the sulfatase-modifying factor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IEYZ. Eukaryota.
COG1262. LUCA.
GeneTreeiENSGT00390000008983.
HOGENOMiHOG000135466.
HOVERGENiHBG054193.
InParanoidiQ0P5L5.
KOiK13444.
OMAiWTADLWD.
OrthoDBiEOG7VX8WN.
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.

Q0P5L5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPALGPAR GCGAELTLVL LLSLFLLLGW AAGGEEAGPE AGAPSLVGSC
60 70 80 90 100
GCGNPQRPGA QGSSAAAHRY SREANAPGSV PGGRPSPPTK MVPIPAGVFT
110 120 130 140 150
MGTDDPQIKQ DGEAPARRVA IDAFYMDAYE VSNAEFEKFV NSTGYLTEAE
160 170 180 190 200
KFGDSFVFEG MLSEQVKSDI QQAVAAAPWW LPVKGANWRH PEGPDSTVLH
210 220 230 240 250
RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLQ NRLFPWGNKL
260 270 280 290 300
QPKGQHYANI WQGEFPVTNT GEDGFRGTAP VDAFPPNGYG LYNIVGNAWE
310 320 330 340 350
WTSDWWTVHH SAEETINPKG PPSGKDRVKK GGSYMCHKSY CYRYRCAARS
360 370
QNTPDSSASN LGFRCAADHL PTTG
Length:374
Mass (Da):40,342
Last modified:September 19, 2006 - v1
Checksum:i964E6D59A80DB2C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC119885 mRNA. Translation: AAI19886.1.
RefSeqiNP_001069544.1. NM_001076076.1.
UniGeneiBt.30055.

Genome annotation databases

EnsembliENSBTAT00000055237; ENSBTAP00000052631; ENSBTAG00000039855.
GeneIDi536435.
KEGGibta:536435.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC119885 mRNA. Translation: AAI19886.1.
RefSeqiNP_001069544.1. NM_001076076.1.
UniGeneiBt.30055.

3D structure databases

ProteinModelPortaliQ0P5L5.
SMRiQ0P5L5. Positions 89-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000052631.

Proteomic databases

PaxDbiQ0P5L5.
PRIDEiQ0P5L5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000055237; ENSBTAP00000052631; ENSBTAG00000039855.
GeneIDi536435.
KEGGibta:536435.

Organism-specific databases

CTDi285362.

Phylogenomic databases

eggNOGiENOG410IEYZ. Eukaryota.
COG1262. LUCA.
GeneTreeiENSGT00390000008983.
HOGENOMiHOG000135466.
HOVERGENiHBG054193.
InParanoidiQ0P5L5.
KOiK13444.
OMAiWTADLWD.
OrthoDBiEOG7VX8WN.
TreeFamiTF324027.

Enzyme and pathway databases

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

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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hippocampus.

Entry informationi

Entry nameiSUMF1_BOVIN
AccessioniPrimary (citable) accession number: Q0P5L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 19, 2006
Last modified: June 8, 2016
This is version 68 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.