ID   SUMF2_PONAB             Reviewed;         301 AA.
AC   Q5RCR5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
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:0000250|UniProtKB:Q8NBJ7};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CR858204; CAH90442.1; -; mRNA.
DR   RefSeq; NP_001125223.1; NM_001131751.1.
DR   AlphaFoldDB; Q5RCR5; -.
DR   SMR; Q5RCR5; -.
DR   STRING; 9601.ENSPPYP00000019664; -.
DR   GeneID; 100172116; -.
DR   CTD; 25870; -.
DR   eggNOG; ENOG502QRY6; Eukaryota.
DR   InParanoid; Q5RCR5; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Metal-binding; 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_0000033461"
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:0000250|UniProtKB:Q8NBJ7"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT   BINDING         208
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT   BINDING         229
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT   BINDING         232
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
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   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        156..290
FT                   /evidence="ECO:0000250|UniProtKB:Q8NBJ7"
SQ   SEQUENCE   301 AA;  33857 MW;  1E834CAF569227E5 CRC64;
     MARHGLPLLP LLSLLVGAWL KLGNGQATSM VQLQGGRFLM GTNSPDSRDG EGPVREATVK
     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