ID   UFSP2_RAT               Reviewed;         461 AA.
AC   Q5XIB4;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
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:0000312|RGD:1311161};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; BC083771; AAH83771.1; -; mRNA.
DR   RefSeq; NP_001014164.1; NM_001014142.1.
DR   RefSeq; XP_008769487.1; XM_008771265.2.
DR   AlphaFoldDB; Q5XIB4; -.
DR   SMR; Q5XIB4; -.
DR   STRING; 10116.ENSRNOP00000016723; -.
DR   MEROPS; C78.002; -.
DR   PhosphoSitePlus; Q5XIB4; -.
DR   jPOST; Q5XIB4; -.
DR   PaxDb; Q5XIB4; -.
DR   PRIDE; Q5XIB4; -.
DR   Ensembl; ENSRNOT00000016723; ENSRNOP00000016723; ENSRNOG00000012087.
DR   GeneID; 361151; -.
DR   KEGG; rno:361151; -.
DR   CTD; 55325; -.
DR   RGD; 1311161; Ufsp2.
DR   eggNOG; KOG2433; Eukaryota.
DR   GeneTree; ENSGT00940000157115; -.
DR   HOGENOM; CLU_021066_1_1_1; -.
DR   InParanoid; Q5XIB4; -.
DR   OMA; GHIKYLI; -.
DR   OrthoDB; 444004at2759; -.
DR   PhylomeDB; Q5XIB4; -.
DR   TreeFam; TF325896; -.
DR   PRO; PR:Q5XIB4; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000012087; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q5XIB4; RN.
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   Cytoplasm; Endoplasmic reticulum; Hydrolase; Nucleus; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..461
FT                   /note="Ufm1-specific protease 2"
FT                   /id="PRO_0000280365"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        418
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
SQ   SEQUENCE   461 AA;  52307 MW;  055B3B67019C54C8 CRC64;
     MDILFRIRGG FDLAFQLAPP KEMFIKNALR QVLNDLTTKL SSDALVFRIC NSSVYLWPNS
     DANTGELTDS SACKSVVDLI QFDQEEDTKR KFMKKKDKKL TDMQQIVNID LMLEISTPLG
     AVTPIIEREN EEHHYINMSL PIDAVVSVAP EETWGKVRKL LVDAILNQLV DVEKCILRYM
     KGTSIVVPEP LHFLLPGGKN LVTVLYPSGI PDDQLQAYRK ELHDLFKLPH DRPYLKRINA
     YHFPDELYKD GYIRNPHAYL SPPNIEGSMI CMVQGTYAYH HYMQNRVDDN GWGCAYRSLQ
     TVCSWFRHQG YTERAIPTHR EIQQALVDAG DKPATFVGSR QWIGSIEVQL VLNQLIGVTS
     KILFVNQGSE MASQGRELAN HFQNVGTPVM IGGGVLAHTI LGVAWNETTG QIKFLILDPH
     YTGAEDLQVI LEKGWCGWKG PDFWNKDAYY NLCLPQRPNA L