ID   UFSP2_XENLA             Reviewed;         464 AA.
AC   Q3B8N0; Q4FZM8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 52.
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};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH99346.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC099346; AAH99346.1; ALT_INIT; mRNA.
DR   EMBL; BC106198; AAI06199.1; -; mRNA.
DR   RefSeq; XP_018085877.1; XM_018230388.1.
DR   AlphaFoldDB; Q3B8N0; -.
DR   SMR; Q3B8N0; -.
DR   MEROPS; C78.002; -.
DR   DNASU; 735166; -.
DR   GeneID; 735166; -.
DR   KEGG; xla:735166; -.
DR   CTD; 735166; -.
DR   Xenbase; XB-GENE-5850325; ufsp2.L.
DR   OrthoDB; 444004at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 735166; Expressed in pancreas and 19 other tissues.
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..464
FT                   /note="Ufm1-specific protease 2"
FT                   /id="PRO_0000280368"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        421
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        423
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
SQ   SEQUENCE   464 AA;  52113 MW;  AC6B9212C9AF0DEA CRC64;
     MVVITSACII FRIRGGLNLS FPLTATDETS AKKALFRAVC DLSSKLLSES LVLNICNSVL
     YIWPNTGTCT HPTELSDDTP CKDILRFIQV DDERKVSKKK EKKSQDLQQM VNIKLLFERS
     TSSEAVSPVI HQDISSQQLV NMVLPIDTVV SVSPDEAWGK VRQLLVNGLT HQLSEMEKCL
     LKYMKGTSFY VAEPNHFLLP DQGLATVIYP AGVADVQLED CRQALHEQFN LPLDRPYFRR
     ANAFHFPDEP YKDGYIRNPH LQLGTPPLEG ATVSLVQGLY SYHHYMQDRM DDNGWGCAYR
     SLQTICSWFK YQGYTDKPIP THKEIQQALV DVGDKPASFV GSRQWIGSIE VQLVLDHLLG
     ITSKIMFVSQ GTELASRGRE LVHHFTSEGT PVMIGGGVLA HTILGVAWSE LTGDIRFLIL
     DPHYKGGEDL HVILEKGWCG WKGPEFWDAT AYYNLCLPQR PTAI