UFSP2_DROME
ID UFSP2_DROME Reviewed; 607 AA.
AC Q9VUR0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Probable Ufm1-specific protease 2 {ECO:0000250|UniProtKB:Q9NUQ7};
DE Short=UfSP2 {ECO:0000250|UniProtKB:Q9NUQ7};
DE EC=3.4.22.- {ECO:0000250|UniProtKB:Q99K23, ECO:0000250|UniProtKB:Q9NUQ7};
GN ORFNames=CG16979;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Thiol protease which recognizes and hydrolyzes the peptide
CC bond at the C-terminal Gly of UFM1, a ubiquitin-like modifier protein
CC bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15
CC ubiquitin-like proteins. {ECO:0000250|UniProtKB:Q99K23,
CC ECO:0000250|UniProtKB:Q9NUQ7}.
CC -!- SIMILARITY: Belongs to the peptidase C78 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014296; AAF49615.1; -; Genomic_DNA.
DR EMBL; BT001409; AAN71164.1; -; mRNA.
DR RefSeq; NP_648779.1; NM_140522.3.
DR AlphaFoldDB; Q9VUR0; -.
DR SMR; Q9VUR0; -.
DR BioGRID; 65006; 2.
DR STRING; 7227.FBpp0075316; -.
DR MEROPS; C78.A01; -.
DR PaxDb; Q9VUR0; -.
DR PRIDE; Q9VUR0; -.
DR DNASU; 39687; -.
DR EnsemblMetazoa; FBtr0075563; FBpp0075316; FBgn0036512.
DR GeneID; 39687; -.
DR KEGG; dme:Dmel_CG16979; -.
DR UCSC; CG16979-RA; d. melanogaster.
DR FlyBase; FBgn0036512; CG16979.
DR VEuPathDB; VectorBase:FBgn0036512; -.
DR eggNOG; KOG2433; Eukaryota.
DR GeneTree; ENSGT00940000157115; -.
DR HOGENOM; CLU_021066_1_0_1; -.
DR InParanoid; Q9VUR0; -.
DR OMA; CGLVKFG; -.
DR OrthoDB; 444004at2759; -.
DR PhylomeDB; Q9VUR0; -.
DR BioGRID-ORCS; 39687; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39687; -.
DR PRO; PR:Q9VUR0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036512; Expressed in testis and 27 other tissues.
DR Genevisible; Q9VUR0; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
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; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR Pfam; PF07910; Peptidase_C78; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..607
FT /note="Probable Ufm1-specific protease 2"
FT /id="PRO_0000280372"
FT ACT_SITE 440
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
FT ACT_SITE 564
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
FT ACT_SITE 566
FT /evidence="ECO:0000250|UniProtKB:Q99K23"
SQ SEQUENCE 607 AA; 68251 MW; A2F9059B0CF5E7CA CRC64;
MLPKLKISAF LLKRLERTKQ QCSGCLFGVF YGEGTLLLLS FNIESSLGQL NYEQIQHRFP
AELDLCGLVK FGGCTDGEAH LNEVIKSVDI TDNPILLQCE LGTLVGLRAS FFVHGKLEEV
PYEVMEAHQL YNDFCFTRLQ CGFFLQTAAT PESVAREMHV LRKRVADGNL VFNVPQTKIF
INNYGPLDKQ FSGDSQIQDL IDVIPTPGHE KETASVDKKK LKGQNTPVKR LAPTGCDYEV
IPIDVMRSRS RDPVSGEPPH PALSIAVTNE EQIRVQVPLE IEAMAILCRK TKLQRLYDVL
IESICRGLRL FELSLIEHLT ESGSGKLLVP ASYHFYPQEF GHFVSCAYLE GLSDDTPSML
MRRKRLHRQF ALPISRPYFR RANQMLFLGE TEDAPWTPLL NTHIGLRPSG VVDGKEYLVN
GNYHYYHYLQ QQVQDKGWGC AYRSLQTICS WFVLQGYTNA PIPTHLEVQE YLHKINDKPA
AFVGSSQWIG STEISMCLQG FLNVDSKILH VASGAELATI ASELAMHFQT QGTPVMIGGG
VLAHTIIGVD YCVQTGQVKF LILDPHYTGA DDLATIQIKG WCGWKGMDFW AKGSYYNLCM
PQRPILY
