ID   UFSP2_PONAB             Reviewed;         469 AA.
AC   Q5RCS9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   03-AUG-2022, entry version 54.
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   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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. Through TRIP4
CC       deufmylation may regulate intracellular nuclear receptors
CC       transactivation and thereby regulate cell proliferation and
CC       differentiation. {ECO:0000250|UniProtKB:Q99K23,
CC       ECO:0000250|UniProtKB:Q9NUQ7}.
CC   -!- SUBUNIT: Interacts with DDRGK1. Interacts with TRIP4; deufmylates
CC       TRIP4. {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; CR858189; CAH90428.1; -; mRNA.
DR   RefSeq; NP_001125214.1; NM_001131742.1.
DR   AlphaFoldDB; Q5RCS9; -.
DR   SMR; Q5RCS9; -.
DR   STRING; 9601.ENSPPYP00000017034; -.
DR   MEROPS; C78.002; -.
DR   GeneID; 100172106; -.
DR   KEGG; pon:100172106; -.
DR   CTD; 55325; -.
DR   eggNOG; KOG2433; Eukaryota.
DR   InParanoid; Q5RCS9; -.
DR   OrthoDB; 444004at2759; -.
DR   Proteomes; UP000001595; 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   GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR   Pfam; PF07910; Peptidase_C78; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Endoplasmic reticulum; Hydrolase; Nucleus;
KW   Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..469
FT                   /note="Ufm1-specific protease 2"
FT                   /id="PRO_0000280364"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUQ7"
SQ   SEQUENCE   469 AA;  53248 MW;  60E392C105482C29 CRC64;
     MVISESMDIL FRIRGGLDLA FQLATPNEIF LKKALKHVLS DLSTKLSSNA LVFRICHSSV
     YIWPSSDINT IPGELTDASA CKNILRFIQF EPEEDIKRKF MRKKDKKLSD MHQIVNIDLM
     LEMSTSLAAV TPIVERESGG HHYVNMTLPV DAVISVAPEE TWGKVRKLLV DAIHNQLTDM
     EKCILKYMKG TSIVVPEPLH FLLPGKKNLV TISYPSGIPD GQLQAYREEL HDLFNLPHDR
     PYFKRSNAYH FPDEPYKDGY IRNPHTYLNP PNMETGMIYV VQGIYGYHHY MQDRIDDNGW
     GCAYRSLQTI CSWFKHQGYT ERSIPTHREI QQALVDAGDK PATFVGSRQW IGSIEVQLVL
     NQLIGITSKI LFVSQGSEIA SQGRELANHF QSEGTPVMIG GGVLAHTILG VAWNEITGQI
     KFLILDPHYT GAEDLQVILE KGWCGWKGPD FWNKDAYYNL CLPQRPNMI