SUMF1_MOUSE
ID SUMF1_MOUSE Reviewed; 372 AA.
AC Q8R0F3; Q3TTT6; Q3TXM8; Q3U9A5;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
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:0000312|MGI:MGI:1889844};
GN Synonyms=Fge {ECO:0000250|UniProtKB:Q8NBK3};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=17360554; DOI=10.1073/pnas.0700382104;
RA Settembre C., Annunziata I., Spampanato C., Zarcone D., Cobellis G.,
RA Nusco E., Zito E., Tacchetti C., Cosma M.P., Ballabio A.;
RT "Systemic inflammation and neurodegeneration in a mouse model of multiple
RT sulfatase deficiency.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4506-4511(2007).
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 -!- DISRUPTION PHENOTYPE: Mice display frequent early mortality, congenital
CC growth retardation, skeletal abnormalities and neurological defects.
CC Defects are caused by absence of all sulfatases activities. Massive
CC glycosaminoglycans accumulation and cell vacuolization are observed in
CC all tissues and are associated with systemic inflammation, apoptosis
CC and neurodegeneration. {ECO:0000269|PubMed:17360554}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE30762.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK151874; BAE30762.1; ALT_INIT; mRNA.
DR EMBL; AK159192; BAE34887.1; -; mRNA.
DR EMBL; AK160917; BAE36091.1; -; mRNA.
DR EMBL; AK161203; BAE36238.1; -; mRNA.
DR EMBL; BC026981; AAH26981.1; ALT_INIT; mRNA.
DR CCDS; CCDS51868.1; -.
DR RefSeq; NP_666049.2; NM_145937.3.
DR AlphaFoldDB; Q8R0F3; -.
DR SMR; Q8R0F3; -.
DR BioGRID; 208463; 19.
DR STRING; 10090.ENSMUSP00000032191; -.
DR GlyConnect; 2742; 2 N-Linked glycans (1 site).
DR GlyGen; Q8R0F3; 1 site, 2 N-linked glycans (1 site).
DR PhosphoSitePlus; Q8R0F3; -.
DR EPD; Q8R0F3; -.
DR MaxQB; Q8R0F3; -.
DR PaxDb; Q8R0F3; -.
DR PeptideAtlas; Q8R0F3; -.
DR PRIDE; Q8R0F3; -.
DR ProteomicsDB; 257505; -.
DR Antibodypedia; 44604; 200 antibodies from 30 providers.
DR DNASU; 58911; -.
DR Ensembl; ENSMUST00000032191; ENSMUSP00000032191; ENSMUSG00000030101.
DR GeneID; 58911; -.
DR KEGG; mmu:58911; -.
DR UCSC; uc009ddf.2; mouse.
DR CTD; 285362; -.
DR MGI; MGI:1889844; Sumf1.
DR VEuPathDB; HostDB:ENSMUSG00000030101; -.
DR eggNOG; ENOG502QVDG; Eukaryota.
DR GeneTree; ENSGT00390000008983; -.
DR HOGENOM; CLU_012431_4_1_1; -.
DR InParanoid; Q8R0F3; -.
DR OMA; WTADLWD; -.
DR OrthoDB; 835112at2759; -.
DR PhylomeDB; Q8R0F3; -.
DR TreeFam; TF324027; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-1663150; The activation of arylsulfatases.
DR UniPathway; UPA00910; -.
DR BioGRID-ORCS; 58911; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Sumf1; mouse.
DR PRO; PR:Q8R0F3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8R0F3; protein.
DR Bgee; ENSMUSG00000030101; Expressed in ascending aorta and 251 other tissues.
DR ExpressionAtlas; Q8R0F3; baseline and differential.
DR Genevisible; Q8R0F3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
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; IPI:MGI.
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 1: Evidence at protein level;
KW Calcium; Copper; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT CHAIN 32..372
FT /note="Formylglycine-generating enzyme"
FT /id="PRO_0000033457"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..358
FT /note="Interaction with sulfatases"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 271
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 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 294
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 334
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT BINDING 339
FT /ligand="Cu(2+)"
FT /ligand_id="ChEBI:CHEBI:29036"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 48..50
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT DISULFID 216..363
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT DISULFID 233..344
FT /evidence="ECO:0000250|UniProtKB:Q8NBK3"
FT CONFLICT 39
FT /note="E -> V (in Ref. 1; BAE34887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40659 MW; 3C96D488B4291068 CRC64;
MAAPAREPAL RCCIRLARVF LLLVLACEVA GSDEAEAREG AASLAGSCGC GTPQRAGAHG
SSAAAQRYSR EANAPGLTSG PRPLALTKMV PIPAGVFTMG TDDPQIRQDG EAPARRVTVD
GFYMDAYEVS NADFEKFVNS TGYLTEAEKF GDSFVFEGML SEQVKTHIHQ AVAAAPWWLP
VKGANWRHPE GPDSSILHRS NHPVLHVSWN DAVAYCTWAG KRLPTEAEWE YSCRGGLQNR
LFPWGNKLQP KGQHYANIWQ GKFPVSNTGE DGFQGTAPVD AFPPNGYGLY NIVGNVWEWT
SDWWTVHHSV EETFNPKGPT SGKDRVKKGG SYMCHKSYCY RYRCAARSQN TPDSSASNLG
FRCAADHLPT AD
