SUMF2_BOVIN
ID SUMF2_BOVIN Reviewed; 301 AA.
AC Q58CP2; A6QPD0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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; BT021905; AAX46752.1; -; mRNA.
DR EMBL; BC149259; AAI49260.1; -; mRNA.
DR RefSeq; NP_001014881.1; NM_001014881.1.
DR AlphaFoldDB; Q58CP2; -.
DR SMR; Q58CP2; -.
DR STRING; 9913.ENSBTAP00000010773; -.
DR PaxDb; Q58CP2; -.
DR Ensembl; ENSBTAT00000010773; ENSBTAP00000010773; ENSBTAG00000008190.
DR GeneID; 509497; -.
DR KEGG; bta:509497; -.
DR CTD; 25870; -.
DR VEuPathDB; HostDB:ENSBTAG00000008190; -.
DR VGNC; VGNC:35472; SUMF2.
DR eggNOG; ENOG502QRY6; Eukaryota.
DR GeneTree; ENSGT00940000162897; -.
DR HOGENOM; CLU_012431_4_2_1; -.
DR InParanoid; Q58CP2; -.
DR OrthoDB; 835112at2759; -.
DR TreeFam; TF324027; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000008190; Expressed in prostate gland and 106 other tissues.
DR ExpressionAtlas; Q58CP2; baseline.
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_0000033458"
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; 33829 MW; 3C338435297C6FD5 CRC64;
MGISLSPLLT VLSLLSGRWL ELGNGQTVNM VQLPGGRFQM GTDSPDGRDG EGPVREVTVK
PFAIDIFPVT NKDFREFVRE KKYRTEAEVF GWSFVFEDLV SDELRNKATQ RMQSLLWWLP
VERAFWRQPA GPGSGIREKL EFPVVHVSWN DARAYCAWRG KRLPTEEEWE FAARGGLKGQ
VYPWGNKFQP NRTNLWQGKF PKGDKAEDGF HGVSPVNAFP PQNDYGLYDL VGNVWEWTAS
QYQAADQDMR VLRGASWIDT ADGSANHRAR VTTRMGNTPD SASDNLGFRC ASGAGRPPGE
L
