ID   UFSP2_DANRE             Reviewed;         401 AA.
AC   Q7T347;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Ufm1-specific protease 2 {ECO:0000250|UniProtKB:Q9NUQ7};
DE            Short=UfSP2 {ECO:0000250|UniProtKB:Q9NUQ7};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:Q9NUQ7};
GN   Name=ufsp2 {ECO:0000250|UniProtKB:Q9NUQ7}; ORFNames=zgc:64113;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Thiol-dependent isopeptidase that recognizes and hydrolyzes
CC       the peptide bond at the C-terminal Gly of UFM1, a ubiquitin-like
CC       modifier protein bound to a number of target proteins. Does not
CC       hydrolyze SUMO1 or ISG15 ubiquitin-like proteins.
CC       {ECO:0000250|UniProtKB:Q99K23, ECO:0000250|UniProtKB:Q9NUQ7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99K23}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99K23}. Nucleus
CC       {ECO:0000250|UniProtKB:Q99K23}.
CC   -!- SIMILARITY: Belongs to the peptidase C78 family. {ECO:0000305}.
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DR   EMBL; BC053257; AAH53257.1; -; mRNA.
DR   RefSeq; NP_942105.1; NM_198810.1.
DR   AlphaFoldDB; Q7T347; -.
DR   SMR; Q7T347; -.
DR   STRING; 7955.ENSDARP00000110184; -.
DR   MEROPS; C78.002; -.
DR   PaxDb; Q7T347; -.
DR   GeneID; 336782; -.
DR   KEGG; dre:336782; -.
DR   CTD; 55325; -.
DR   ZFIN; ZDB-GENE-030131-8726; ufsp2.
DR   eggNOG; KOG2433; Eukaryota.
DR   InParanoid; Q7T347; -.
DR   OrthoDB; 444004at2759; -.
DR   PRO; PR:Q7T347; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0071567; F:deUFMylase activity; ISS:UniProtKB.
DR   GO; GO:0016790; F:thiolester hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR   Pfam; PF07910; Peptidase_C78; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; Hydrolase; Nucleus; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..401
FT                   /note="Ufm1-specific protease 2"
FT                   /id="PRO_0000280367"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        360
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
SQ   SEQUENCE   401 AA;  44862 MW;  C6DBC10B285B4CF1 CRC64;
     MGFQSSVEGL TQASACGDIL QYIESDDGGN KKSSKKKDKK KSGPIVVNLK LLFEVTDPAG
     NEAPSLMRMS AQQHSVKMPL PLDCVLSVSA DESMTTVFTG LVEALNKQIA DMEEVVLRYR
     KGSSFLVPQP FHFQLPKPAG LTTVIYPAGV PDSQLQAVRE DLHRKFELSL DRPYLRRANA
     FHFPYEAYKD GYLRNPHIHL NPPNIEDAKL YLVQGVYSYH HYMQDRVDDD GWGCAYRSLQ
     TICSWFQQQG YVETAVPTHT QIQQALVDVG DKEPRFVGSR QWIGSIEVQA VLNQLLGVTS
     KIMFVSQGSE LATKGRELAN HFHTEGTPVM IGGGVLAHTI LGVAWSENTG EIRFLILDPH
     YTGGEDLQII TDKGWCGWKG PEFWDQNAYY NLCLPQRPKT V