SUMF2_HUMAN
ID SUMF2_HUMAN Reviewed; 301 AA.
AC Q8NBJ7; B4DU41; B4DWQ0; Q14DW5; Q53ZE3; Q96BH2; Q9BRN3; Q9BWI1; Q9Y405;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Inactive C-alpha-formylglycine-generating enzyme 2 {ECO:0000305};
DE AltName: Full=Paralog of formylglycine-generating enzyme {ECO:0000303|PubMed:15687489, ECO:0000303|PubMed:15708861, ECO:0000303|PubMed:18266766};
DE Short=pFGE {ECO:0000303|PubMed:15687489, ECO:0000303|PubMed:15708861, ECO:0000303|PubMed:18266766};
DE AltName: Full=Sulfatase-modifying factor 2 {ECO:0000303|PubMed:15962010};
DE Flags: Precursor;
GN Name=SUMF2 {ECO:0000303|PubMed:15962010, ECO:0000312|HGNC:HGNC:20415};
GN ORFNames=PSEC0171 {ECO:0000303|PubMed:16303743},
GN UNQ1968/PRO4500 {ECO:0000303|PubMed:12975309};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT GLU-51.
RX PubMed=12757706; DOI=10.1016/s0092-8674(03)00348-9;
RA Cosma M.P., Pepe S., Annunziata I., Newbold R.F., Grompe M., Parenti G.,
RA Ballabio A.;
RT "The multiple sulfatase deficiency gene encodes an essential and limiting
RT factor for the activity of sulfatases.";
RL Cell 113:445-456(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-51.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLU-51.
RC TISSUE=Colon, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-51.
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT GLU-51.
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT
RP GLU-51.
RC TISSUE=Eye, Ovary, and Placenta;
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 [9]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP SUBCELLULAR LOCATION, DISULFIDE BOND, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15708861; DOI=10.1074/jbc.m413698200;
RA Mariappan M., Preusser-Kunze A., Balleininger M., Eiselt N., Schmidt B.,
RA Gande S.L., Wenzel D., Dierks T., von Figura K.;
RT "Expression, localization, structural, and functional characterization of
RT pFGE, the paralog of the Calpha-formylglycine-generating enzyme.";
RL J. Biol. Chem. 280:15173-15179(2005).
RN [10]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-156 AND CYS-290.
RX PubMed=15962010; DOI=10.1038/sj.embor.7400454;
RA Zito E., Fraldi A., Pepe S., Annunziata I., Kobinger G., Di Natale P.,
RA Ballabio A., Cosma M.P.;
RT "Sulphatase activities are regulated by the interaction of sulphatase-
RT modifying factor 1 with SUMF2.";
RL EMBO Rep. 6:655-660(2005).
RN [11]
RP SUBCELLULAR LOCATION, NON-CANONICAL ER RETENTION MOTIF, AND MUTAGENESIS OF
RP PRO-298; 298-PRO-GLY-299 AND 298-PRO--LEU-301.
RX PubMed=18266766; DOI=10.1111/j.1742-4658.2008.06271.x;
RA Gande S.L., Mariappan M., Schmidt B., Pringle T.H., von Figura K.,
RA Dierks T.;
RT "Paralog of the formylglycine-generating enzyme--retention in the
RT endoplasmic reticulum by canonical and noncanonical signals.";
RL FEBS J. 275:1118-1130(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 27-301 IN COMPLEX WITH CALCIUM
RP IONS, GLYCOSYLATION AT ASN-191, AND DISULFIDE BONDS.
RX PubMed=15687489; DOI=10.1074/jbc.m414317200;
RA Dickmanns A., Schmidt B., Rudolph M.G., Mariappan M., Dierks T.,
RA von Figura K., Ficner R.;
RT "Crystal structure of human pFGE, the paralog of the Calpha-formylglycine-
RT generating enzyme.";
RL J. Biol. Chem. 280:15180-15187(2005).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP VARIANT CYS-228.
RX PubMed=28397838; DOI=10.1038/mp.2017.60;
RA Harripaul R., Vasli N., Mikhailov A., Rafiq M.A., Mittal K.,
RA Windpassinger C., Sheikh T.I., Noor A., Mahmood H., Downey S., Johnson M.,
RA Vleuten K., Bell L., Ilyas M., Khan F.S., Khan V., Moradi M., Ayaz M.,
RA Naeem F., Heidari A., Ahmed I., Ghadami S., Agha Z., Zeinali S., Qamar R.,
RA Mozhdehipanah H., John P., Mir A., Ansar M., French L., Ayub M.,
RA Vincent J.B.;
RT "Mapping autosomal recessive intellectual disability: combined microarray
RT and exome sequencing identifies 26 novel candidate genes in 192
RT consanguineous families.";
RL Mol. Psychiatry 23:973-984(2018).
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:0000269|PubMed:12757706, ECO:0000269|PubMed:15708861,
CC ECO:0000269|PubMed:15962010}.
CC -!- SUBUNIT: Homodimer and heterodimer with SUMF1.
CC {ECO:0000269|PubMed:15687489, ECO:0000269|PubMed:15962010}.
CC -!- INTERACTION:
CC Q8NBJ7; Q92870-2: APBB2; NbExp=3; IntAct=EBI-723091, EBI-21535880;
CC Q8NBJ7; P07339: CTSD; NbExp=3; IntAct=EBI-723091, EBI-2115097;
CC Q8NBJ7; P28799: GRN; NbExp=3; IntAct=EBI-723091, EBI-747754;
CC Q8NBJ7; P04792: HSPB1; NbExp=3; IntAct=EBI-723091, EBI-352682;
CC Q8NBJ7; P42858: HTT; NbExp=6; IntAct=EBI-723091, EBI-466029;
CC Q8NBJ7; P22304: IDS; NbExp=2; IntAct=EBI-723091, EBI-2687288;
CC Q8NBJ7; O60333-2: KIF1B; NbExp=3; IntAct=EBI-723091, EBI-10975473;
CC Q8NBJ7; D3DTS7: PMP22; NbExp=3; IntAct=EBI-723091, EBI-25882629;
CC Q8NBJ7; Q8NBK3: SUMF1; NbExp=9; IntAct=EBI-723091, EBI-2853497;
CC Q8NBJ7; Q8NBJ7: SUMF2; NbExp=2; IntAct=EBI-723091, EBI-723091;
CC Q8NBJ7; P02766: TTR; NbExp=3; IntAct=EBI-723091, EBI-711909;
CC Q8NBJ7; O76024: WFS1; NbExp=3; IntAct=EBI-723091, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:15708861, ECO:0000269|PubMed:15962010,
CC ECO:0000269|PubMed:18266766}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8NBJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBJ7-2; Sequence=VSP_007878;
CC Name=3;
CC IsoId=Q8NBJ7-3; Sequence=VSP_007879;
CC Name=5;
CC IsoId=Q8NBJ7-5; Sequence=VSP_040878;
CC Name=4;
CC IsoId=Q8NBJ7-4; Sequence=VSP_007880;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas. Highest levels in kidney, liver
CC and placenta. {ECO:0000269|PubMed:15708861,
CC ECO:0000269|PubMed:15962010}.
CC -!- DOMAIN: The non-canonical ER retention motif mediates retention of the
CC protein in the endoplasmic reticulum. {ECO:0000269|PubMed:18266766}.
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 at positions 261 and 266 that bind the
CC catalytic copper. The catalytic copper is required to activate oxygen
CC and catalyze oxidative C-H activation. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00224.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB43247.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB43247.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY323911; AAP86218.1; -; mRNA.
DR EMBL; AY359103; AAQ89461.1; -; mRNA.
DR EMBL; AK300488; BAG62203.1; -; mRNA.
DR EMBL; AK301627; BAG63112.1; -; mRNA.
DR EMBL; AK075477; BAC11643.1; -; mRNA.
DR EMBL; AL050037; CAB43247.1; ALT_SEQ; mRNA.
DR EMBL; CH471140; EAX07980.1; -; Genomic_DNA.
DR EMBL; BC000224; AAH00224.1; ALT_INIT; mRNA.
DR EMBL; BC006159; AAH06159.1; -; mRNA.
DR EMBL; BC015600; AAH15600.2; -; mRNA.
DR EMBL; BC084539; AAH84539.1; -; mRNA.
DR EMBL; BC111092; AAI11093.1; -; mRNA.
DR CCDS; CCDS43589.2; -. [Q8NBJ7-5]
DR CCDS; CCDS47589.1; -. [Q8NBJ7-3]
DR CCDS; CCDS55111.1; -. [Q8NBJ7-2]
DR CCDS; CCDS5524.2; -. [Q8NBJ7-1]
DR PIR; T08715; T08715.
DR RefSeq; NP_001035934.2; NM_001042469.1.
DR RefSeq; NP_001035935.2; NM_001042470.1. [Q8NBJ7-5]
DR RefSeq; NP_001123541.1; NM_001130069.2. [Q8NBJ7-3]
DR RefSeq; NP_001139805.1; NM_001146333.1. [Q8NBJ7-2]
DR RefSeq; NP_056226.2; NM_015411.2. [Q8NBJ7-1]
DR PDB; 1Y4J; X-ray; 1.86 A; A/B=27-301.
DR PDBsum; 1Y4J; -.
DR AlphaFoldDB; Q8NBJ7; -.
DR SMR; Q8NBJ7; -.
DR BioGRID; 117386; 55.
DR IntAct; Q8NBJ7; 22.
DR MINT; Q8NBJ7; -.
DR STRING; 9606.ENSP00000341938; -.
DR GlyConnect; 1773; 4 N-Linked glycans (1 site).
DR GlyGen; Q8NBJ7; 5 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q8NBJ7; -.
DR MetOSite; Q8NBJ7; -.
DR PhosphoSitePlus; Q8NBJ7; -.
DR BioMuta; SUMF2; -.
DR DMDM; 296452916; -.
DR REPRODUCTION-2DPAGE; IPI00171412; -.
DR EPD; Q8NBJ7; -.
DR jPOST; Q8NBJ7; -.
DR MassIVE; Q8NBJ7; -.
DR MaxQB; Q8NBJ7; -.
DR PaxDb; Q8NBJ7; -.
DR PeptideAtlas; Q8NBJ7; -.
DR PRIDE; Q8NBJ7; -.
DR ProteomicsDB; 72779; -. [Q8NBJ7-1]
DR ProteomicsDB; 72780; -. [Q8NBJ7-2]
DR ProteomicsDB; 72781; -. [Q8NBJ7-3]
DR ProteomicsDB; 72782; -. [Q8NBJ7-4]
DR ProteomicsDB; 72783; -. [Q8NBJ7-5]
DR Antibodypedia; 13904; 85 antibodies from 21 providers.
DR DNASU; 25870; -.
DR Ensembl; ENST00000275607.13; ENSP00000275607.9; ENSG00000129103.19. [Q8NBJ7-2]
DR Ensembl; ENST00000342190.11; ENSP00000341938.7; ENSG00000129103.19. [Q8NBJ7-3]
DR Ensembl; ENST00000395435.7; ENSP00000378823.3; ENSG00000129103.19. [Q8NBJ7-5]
DR Ensembl; ENST00000434526.8; ENSP00000400922.3; ENSG00000129103.19. [Q8NBJ7-1]
DR GeneID; 25870; -.
DR KEGG; hsa:25870; -.
DR MANE-Select; ENST00000434526.8; ENSP00000400922.3; NM_015411.4; NP_056226.3.
DR UCSC; uc003trt.4; human. [Q8NBJ7-1]
DR CTD; 25870; -.
DR DisGeNET; 25870; -.
DR GeneCards; SUMF2; -.
DR HGNC; HGNC:20415; SUMF2.
DR HPA; ENSG00000129103; Low tissue specificity.
DR MalaCards; SUMF2; -.
DR MIM; 607940; gene.
DR neXtProt; NX_Q8NBJ7; -.
DR OpenTargets; ENSG00000129103; -.
DR PharmGKB; PA134921869; -.
DR VEuPathDB; HostDB:ENSG00000129103; -.
DR eggNOG; ENOG502QRY6; Eukaryota.
DR GeneTree; ENSGT00940000162897; -.
DR HOGENOM; CLU_012431_4_2_1; -.
DR InParanoid; Q8NBJ7; -.
DR OMA; YEWTADC; -.
DR OrthoDB; 835112at2759; -.
DR PhylomeDB; Q8NBJ7; -.
DR PathwayCommons; Q8NBJ7; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR Reactome; R-HSA-1663150; The activation of arylsulfatases.
DR SignaLink; Q8NBJ7; -.
DR BioGRID-ORCS; 25870; 7 hits in 1078 CRISPR screens.
DR ChiTaRS; SUMF2; human.
DR EvolutionaryTrace; Q8NBJ7; -.
DR GeneWiki; SUMF2; -.
DR GenomeRNAi; 25870; -.
DR Pharos; Q8NBJ7; Tbio.
DR PRO; PR:Q8NBJ7; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8NBJ7; protein.
DR Bgee; ENSG00000129103; Expressed in right uterine tube and 175 other tissues.
DR ExpressionAtlas; Q8NBJ7; baseline and differential.
DR Genevisible; Q8NBJ7; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Alternative splicing; Calcium; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Metal-binding;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..301
FT /note="Inactive C-alpha-formylglycine-generating enzyme 2"
FT /id="PRO_0000033459"
FT REGION 274..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 298..301
FT /note="Non-canonical ER retention motif"
FT /evidence="ECO:0000269|PubMed:18266766"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15687489"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15687489"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15687489"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15687489"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15687489"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15687489"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15687489"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15687489"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15687489"
FT DISULFID 156..290
FT /evidence="ECO:0000269|PubMed:15687489,
FT ECO:0000269|PubMed:15708861"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007878"
FT VAR_SEQ 114..301
FT /note="SVLWWLPVEKAFWRQPAGPGSGIRERLEHPVLHVSWNDARAYCAWRGKRLPT
FT EEEWEFAARGGLKGQVYPWGNWFQPNRTNLWQGKFPKGDKAEDGFHGVSPVNAFPAQNN
FT YGLYDLLGNVWEWTASPYQAAEQDMRVLRGASWIDTADGSANHRARVTTRMGNTPDSAS
FT DNLGFRCAADAGRPPGEL -> VKFTHGGTGSSQTAPTCGRESSPRETKLRMASMESPQ
FT MLSPPRTTTGSMTSWGTCGSGQHHRTRLLSRTCASSGGHPGSTQLMALPITGPGSPPGW
FT ATLQIQPQTTSVSAVLQTQAGRQGSCKQPGGDKEKSLLGSLSFPGHVANSAIPSSRASA
FT SGKNFPFPVSHPSVAGASHQGRRGLSLLCFGEGAQCVLTMAGGQVFLLEAKYY (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_007880"
FT VAR_SEQ 114..197
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_040878"
FT VAR_SEQ 227..301
FT /note="LYDLLGNVWEWTASPYQAAEQDMRVLRGASWIDTADGSANHRARVTTRMGNT
FT PDSASDNLGFRCAADAGRPPGEL -> WATLQIQPQTTSVSAVLQTQAGRQGSCKQPGG
FT DKEKSLLGSLSFPGHVANSAIPSSRASASGKNFPFPVSHPSVAGASHQGRRGLSLLCFG
FT EGAQCVLTMAGGQVFLLEAKYY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007879"
FT VARIANT 51
FT /note="D -> E (in dbSNP:rs4245575)"
FT /evidence="ECO:0000269|PubMed:12757706,
FT ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16303743,
FT ECO:0000269|PubMed:17974005, ECO:0007744|PubMed:24275569"
FT /id="VAR_046951"
FT VARIANT 228
FT /note="Y -> C (found in a consanguineous family with
FT intellectual disability; unknown pathological significance;
FT dbSNP:rs778487055)"
FT /evidence="ECO:0000269|PubMed:28397838"
FT /id="VAR_080774"
FT MUTAGEN 156
FT /note="C->A: Abolishes interaction with and inhibition of
FT SUMF1. Can still form homodimers."
FT /evidence="ECO:0000269|PubMed:15962010"
FT MUTAGEN 290
FT /note="C->A: Abolishes interaction with and inhibition of
FT SUMF1. Can still form homodimers."
FT /evidence="ECO:0000269|PubMed:15962010"
FT MUTAGEN 298..301
FT /note="Missing: Abolishes endoplasmic reticulum retention."
FT /evidence="ECO:0000269|PubMed:18266766"
FT MUTAGEN 298..299
FT /note="PG->KD: Does not affect endoplasmic reticulum
FT retention."
FT /evidence="ECO:0000269|PubMed:18266766"
FT MUTAGEN 298
FT /note="P->S: Does not affect endoplasmic reticulum
FT retention."
FT /evidence="ECO:0000269|PubMed:18266766"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1Y4J"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:1Y4J"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:1Y4J"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1Y4J"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1Y4J"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:1Y4J"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1Y4J"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:1Y4J"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:1Y4J"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1Y4J"
SQ SEQUENCE 301 AA; 33843 MW; 1E834CEA56922755 CRC64;
MARHGLPLLP LLSLLVGAWL KLGNGQATSM VQLQGGRFLM GTNSPDSRDG DGPVREATVK
PFAIDIFPVT NKDFRDFVRE KKYRTEAEMF GWSFVFEDFV SDELRNKATQ PMKSVLWWLP
VEKAFWRQPA GPGSGIRERL EHPVLHVSWN DARAYCAWRG KRLPTEEEWE FAARGGLKGQ
VYPWGNWFQP NRTNLWQGKF PKGDKAEDGF HGVSPVNAFP AQNNYGLYDL LGNVWEWTAS
PYQAAEQDMR VLRGASWIDT ADGSANHRAR VTTRMGNTPD SASDNLGFRC AADAGRPPGE
L
