SUMF1_BOVIN
ID SUMF1_BOVIN Reviewed; 374 AA.
AC Q0P5L5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Formylglycine-generating enzyme {ECO:0000250|UniProtKB:Q8NBK3};
DE Short=FGE {ECO:0000250|UniProtKB:Q8NBK3};
DE EC=1.8.3.7 {ECO:0000250|UniProtKB:Q8NBK3};
DE AltName: Full=C-alpha-formylglycine-generating enzyme 1 {ECO:0000250|UniProtKB:Q8NBK3};
DE AltName: Full=Sulfatase-modifying factor 1 {ECO:0000250|UniProtKB:Q8NBK3};
DE Flags: Precursor;
GN Name=SUMF1 {ECO:0000250|UniProtKB:Q8NBK3};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidase that catalyzes the conversion of cysteine to 3-
CC oxoalanine on target proteins, using molecular oxygen and an
CC unidentified reducing agent. 3-oxoalanine modification, which is also
CC named formylglycine (fGly), occurs in the maturation of arylsulfatases
CC and some alkaline phosphatases that use the hydrated form of 3-
CC oxoalanine as a catalytic nucleophile. Known substrates include GALNS,
CC ARSA, STS and ARSE. {ECO:0000250|UniProtKB:Q8NBK3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a thiol + L-cysteinyl-[sulfatase] + O2 = 3-oxo-L-alanyl-
CC [sulfatase] + an organic disulfide + H(+) + H2O + hydrogen sulfide;
CC Xref=Rhea:RHEA:51152, Rhea:RHEA-COMP:12900, Rhea:RHEA-COMP:12901,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:29256, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:35489, ChEBI:CHEBI:85621; EC=1.8.3.7;
CC Evidence={ECO:0000250|UniProtKB:Q8NBK3};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q8NBK3};
CC Note=The catalytic copper is required to activate oxygen and catalyze
CC oxidative C-H activation. {ECO:0000250|UniProtKB:Q8NBK3};
CC -!- PATHWAY: Protein modification; sulfatase oxidation.
CC {ECO:0000250|UniProtKB:Q8NBK3}.
CC -!- SUBUNIT: Monomer, homodimer and heterodimer with SUMF2.
CC {ECO:0000250|UniProtKB:Q8NBK3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q8NBK3}.
CC -!- PTM: N-glycosylated. Contains high-mannose-type oligosaccharides.
CC {ECO:0000250|UniProtKB:Q8NBK3}.
CC -!- SIMILARITY: Belongs to the sulfatase-modifying factor family.
CC {ECO:0000305}.
CC -!- CAUTION: The enzyme reaction was initially thought to act via a redox-
CC active disulfide bond mechanism; however the disulfide bond only takes
CC place with inactive enzyme that lacks the copper cofactor. The
CC catalytic copper is required to activate oxygen and catalyze oxidative
CC C-H activation. {ECO:0000250|UniProtKB:Q8NBK3}.
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DR EMBL; BC119885; AAI19886.1; -; mRNA.
DR RefSeq; NP_001069544.1; NM_001076076.1.
DR AlphaFoldDB; Q0P5L5; -.
DR SMR; Q0P5L5; -.
DR STRING; 9913.ENSBTAP00000052631; -.
DR PaxDb; Q0P5L5; -.
DR PRIDE; Q0P5L5; -.
DR Ensembl; ENSBTAT00000055237; ENSBTAP00000052631; ENSBTAG00000039855.
DR GeneID; 536435; -.
DR KEGG; bta:536435; -.
DR CTD; 285362; -.
DR VEuPathDB; HostDB:ENSBTAG00000039855; -.
DR VGNC; VGNC:35471; SUMF1.
DR eggNOG; ENOG502QVDG; Eukaryota.
DR GeneTree; ENSGT00390000008983; -.
DR HOGENOM; CLU_012431_4_1_1; -.
DR InParanoid; Q0P5L5; -.
DR OMA; WTADLWD; -.
DR OrthoDB; 835112at2759; -.
DR TreeFam; TF324027; -.
DR Reactome; R-BTA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-BTA-1663150; The activation of arylsulfatases.
DR UniPathway; UPA00910; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000039855; Expressed in saliva-secreting gland and 104 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:1903135; F:cupric ion binding; ISS:UniProtKB.
DR GO; GO:0120147; F:Formylglycine-generating oxidase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0018158; P:protein oxidation; ISS:UniProtKB.
DR Gene3D; 3.90.1580.10; -; 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
PE 2: Evidence at transcript level;
KW Calcium; Copper; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT CHAIN 34..374
FT /note="Formylglycine-generating enzyme"
FT /id="PRO_0000333034"
FT REGION 57..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..360
FT /note="Interaction with sulfatases"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 336
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 341
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 50..52
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT DISULFID 218..365
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT DISULFID 235..346
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
SQ SEQUENCE 374 AA; 40342 MW; 964E6D59A80DB2C9 CRC64;
MAAPALGPAR GCGAELTLVL LLSLFLLLGW AAGGEEAGPE AGAPSLVGSC GCGNPQRPGA
QGSSAAAHRY SREANAPGSV PGGRPSPPTK MVPIPAGVFT MGTDDPQIKQ DGEAPARRVA
IDAFYMDAYE VSNAEFEKFV NSTGYLTEAE KFGDSFVFEG MLSEQVKSDI QQAVAAAPWW
LPVKGANWRH PEGPDSTVLH RPDHPVLHVS WNDAVAYCTW AGKRLPTEAE WEYSCRGGLQ
NRLFPWGNKL QPKGQHYANI WQGEFPVTNT GEDGFRGTAP VDAFPPNGYG LYNIVGNAWE
WTSDWWTVHH SAEETINPKG PPSGKDRVKK GGSYMCHKSY CYRYRCAARS QNTPDSSASN
LGFRCAADHL PTTG
