SUMF2_MOUSE
ID SUMF2_MOUSE Reviewed; 308 AA.
AC Q8BPG6; Q3TZL1; Q3UUL0; Q9CZ47;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Inactive C-alpha-formylglycine-generating enzyme 2 {ECO:0000305};
DE AltName: Full=Sulfatase-modifying factor 2 {ECO:0000250|UniProtKB:Q8NBJ7};
DE Flags: Precursor;
GN Name=Sumf2 {ECO:0000312|MGI:MGI:1915152};
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=Embryo, and Hypothalamus;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Lung;
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).
CC -!- FUNCTION: Lacks formylglycine generating activity and is unable to
CC convert newly synthesized inactive sulfatases to their active form.
CC Inhibits the activation of sulfatases by SUMF1.
CC {ECO:0000250|UniProtKB:Q8NBJ7}.
CC -!- SUBUNIT: Homodimer and heterodimer with SUMF1.
CC {ECO:0000250|UniProtKB:Q8NBJ7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q8NBJ7}.
CC -!- DOMAIN: The non-canonical ER retention motif mediates retention of the
CC protein in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8NBJ7}.
CC -!- SIMILARITY: Belongs to the sulfatase-modifying factor family.
CC {ECO:0000305}.
CC -!- CAUTION: Although strongly similar to formylglycine-generating enzyme,
CC lacks the catalytic Cys residues that bind the catalytic copper. The
CC catalytic copper is required to activate oxygen and catalyze oxidative
CC C-H activation. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE23615.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK076022; BAC36127.1; -; mRNA.
DR EMBL; AK138300; BAE23615.1; ALT_INIT; mRNA.
DR EMBL; AK157784; BAE34197.1; -; mRNA.
DR EMBL; CH466529; EDL19497.1; -; Genomic_DNA.
DR CCDS; CCDS19700.1; -.
DR RefSeq; NP_080721.1; NM_026445.2.
DR AlphaFoldDB; Q8BPG6; -.
DR SMR; Q8BPG6; -.
DR BioGRID; 212525; 6.
DR STRING; 10090.ENSMUSP00000126036; -.
DR GlyGen; Q8BPG6; 1 site.
DR PhosphoSitePlus; Q8BPG6; -.
DR SwissPalm; Q8BPG6; -.
DR REPRODUCTION-2DPAGE; IPI00223483; -.
DR EPD; Q8BPG6; -.
DR MaxQB; Q8BPG6; -.
DR PaxDb; Q8BPG6; -.
DR PRIDE; Q8BPG6; -.
DR ProteomicsDB; 257506; -.
DR Ensembl; ENSMUST00000171300; ENSMUSP00000126036; ENSMUSG00000025538.
DR GeneID; 67902; -.
DR KEGG; mmu:67902; -.
DR UCSC; uc008ztk.1; mouse.
DR CTD; 25870; -.
DR MGI; MGI:1915152; Sumf2.
DR VEuPathDB; HostDB:ENSMUSG00000025538; -.
DR eggNOG; ENOG502QRY6; Eukaryota.
DR GeneTree; ENSGT00940000162897; -.
DR HOGENOM; CLU_012431_4_2_1; -.
DR InParanoid; Q8BPG6; -.
DR OMA; YEWTADC; -.
DR OrthoDB; 835112at2759; -.
DR PhylomeDB; Q8BPG6; -.
DR TreeFam; TF324027; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-1663150; The activation of arylsulfatases.
DR BioGRID-ORCS; 67902; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q8BPG6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BPG6; protein.
DR Bgee; ENSMUSG00000025538; Expressed in manus and 216 other tissues.
DR ExpressionAtlas; Q8BPG6; baseline and differential.
DR Genevisible; Q8BPG6; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..308
FT /note="Inactive C-alpha-formylglycine-generating enzyme 2"
FT /id="PRO_0000033460"
FT REGION 281..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 305..308
FT /note="Non-canonical ER retention motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT COMPBIAS 281..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 163..297
FT /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT CONFLICT 2
FT /note="R -> G (in Ref. 1; BAE23615)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="W -> R (in Ref. 1; BAC36127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 34737 MW; 65B34055653044D8 CRC64;
MRSEFWFPSM GSLLPPVLLL WLLSCPRLQL GHAQDPAMVH LPGGRFLMGT DAPDGRDGEG
PAREVTVKPF AIDIFPVTNK DFREFVREKK YQTEAEAFGW SFVFEDFVSP ELRKQENLMP
AVHWWQPVPK AFWRQPAGPG SGIREKLELP VVHVSWNDAG AYCAWRGRRL PTEEEWEFAA
RGGLKGQVYP WGNRFQPNRT NLWQGKFPKG DKAEDGFHGL SPVNAFPPQN NYGLYDLMGN
VWEWTASTYQ PAGQDMRVLR GASWIDTADG SANHRARVTT RMGNTPDSAS DNLGFRCASS
AGRPKEDL
