ID   UFSP2_CHICK             Reviewed;         460 AA.
AC   Q5ZIF3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
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};
GN   ORFNames=RCJMB04_27c22 {ECO:0000303|PubMed:15642098};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720831; CAG32490.1; -; mRNA.
DR   RefSeq; NP_001026307.1; NM_001031136.1.
DR   AlphaFoldDB; Q5ZIF3; -.
DR   SMR; Q5ZIF3; -.
DR   STRING; 9031.ENSGALP00000017231; -.
DR   MEROPS; C78.002; -.
DR   PaxDb; Q5ZIF3; -.
DR   GeneID; 422542; -.
DR   KEGG; gga:422542; -.
DR   CTD; 55325; -.
DR   VEuPathDB; HostDB:geneid_422542; -.
DR   eggNOG; KOG2433; Eukaryota.
DR   InParanoid; Q5ZIF3; -.
DR   PhylomeDB; Q5ZIF3; -.
DR   PRO; PR:Q5ZIF3; -.
DR   Proteomes; UP000000539; 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..460
FT                   /note="Ufm1-specific protease 2"
FT                   /id="PRO_0000280366"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        417
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000250|UniProtKB:Q99K23"
SQ   SEQUENCE   460 AA;  52099 MW;  6296663CBA2F2ECF CRC64;
     MDILFRIRGG LDLAFQLATT DEASAKSVLK YVFSDLANKL SSDVLVLRIC NSSVYVWPNN
     GINTVPELTD DSACKEIKRF VHFDQDDETR RKLGKKKDKK LQDMVINIDL MLEMTSSSDA
     LAPVIERENK EHHYINMTLP VDVVVSVSPD ETWGKVQNLL VKAIHKQLTD MERCIMKYMK
     GTSIVVPEQF HFMLPGKNHL VTISYPTGIS DDQLESYRKE LHGLFNLPCD RPYFKRANAY
     HFPDEPYKDG YLKNPHLHLN SPGPESGVVY LVHGTYSYHH YMQDRTDDSG WGCAYRSLQT
     ICSWFKQQGY VDAPIPTHKE IQQALVDAGD KPAAFVGSRQ WIGSVEVQLV LNQLFGITSK
     ILFVSQGSEL ALQGRELANH FKTEGTPVMI GGGVLAHTIL GVAWNEMTGQ IKYLILDPHY
     TGGEDLHVIL DKGWCAWKGP DFWSKDAYYN LCLPQRPKTI