UFSP1_MOUSE
ID UFSP1_MOUSE Reviewed; 217 AA.
AC Q9CZP0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ufm1-specific protease 1;
DE Short=UfSP1;
DE EC=3.4.22.-;
GN Name=Ufsp1; Synonyms=D5Ertd655e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Mammary tumor;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF CYS-53.
RX PubMed=17182609; DOI=10.1074/jbc.m610590200;
RA Kang S.H., Kim G.R., Seong M., Baek S.H., Seol J.H., Bang O.S., Ovaa H.,
RA Tatsumi K., Komatsu M., Tanaka K., Chung C.H.;
RT "Two novel ubiquitin-fold modifier 1 (Ufm1)-specific Proteases, UfSP1 and
RT UfSP2.";
RL J. Biol. Chem. 282:5256-5262(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 6-215, AND MUTAGENESIS OF TYR-41;
RP CYS-53; TRP-98; GLN-154; ASP-175 AND HIS-177.
RX PubMed=18321862; DOI=10.1074/jbc.m708756200;
RA Ha B.H., Ahn H.C., Kang S.H., Tanaka K., Chung C.H., Kim E.E.;
RT "Structural basis for Ufm1 processing by UfSP1.";
RL J. Biol. Chem. 283:14893-14900(2008).
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:0000269|PubMed:17182609}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC brain, heart, kidney and skeletal muscle.
CC {ECO:0000269|PubMed:17182609}.
CC -!- SIMILARITY: Belongs to the peptidase C78 family. {ECO:0000305}.
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DR EMBL; AF312033; AAK28831.1; -; Genomic_DNA.
DR EMBL; AK012343; BAB28174.1; -; mRNA.
DR EMBL; BC016577; AAH16577.1; -; mRNA.
DR EMBL; BC087958; AAH87958.1; -; mRNA.
DR CCDS; CCDS19764.1; -.
DR RefSeq; NP_081632.1; NM_027356.2.
DR PDB; 2Z84; X-ray; 1.70 A; A=6-215.
DR PDBsum; 2Z84; -.
DR AlphaFoldDB; Q9CZP0; -.
DR SMR; Q9CZP0; -.
DR BioGRID; 213935; 1.
DR STRING; 10090.ENSMUSP00000056156; -.
DR MEROPS; C78.001; -.
DR PhosphoSitePlus; Q9CZP0; -.
DR EPD; Q9CZP0; -.
DR MaxQB; Q9CZP0; -.
DR PaxDb; Q9CZP0; -.
DR PeptideAtlas; Q9CZP0; -.
DR PRIDE; Q9CZP0; -.
DR ProteomicsDB; 299639; -.
DR Antibodypedia; 16700; 26 antibodies from 14 providers.
DR Ensembl; ENSMUST00000052825; ENSMUSP00000056156; ENSMUSG00000051502.
DR GeneID; 70240; -.
DR KEGG; mmu:70240; -.
DR UCSC; uc009abz.1; mouse.
DR CTD; 402682; -.
DR MGI; MGI:1917490; Ufsp1.
DR VEuPathDB; HostDB:ENSMUSG00000051502; -.
DR eggNOG; KOG2433; Eukaryota.
DR GeneTree; ENSGT00940000162936; -.
DR HOGENOM; CLU_114366_0_0_1; -.
DR InParanoid; Q9CZP0; -.
DR OMA; QTLCSWP; -.
DR OrthoDB; 444004at2759; -.
DR PhylomeDB; Q9CZP0; -.
DR TreeFam; TF325896; -.
DR BioGRID-ORCS; 70240; 3 hits in 74 CRISPR screens.
DR EvolutionaryTrace; Q9CZP0; -.
DR PRO; PR:Q9CZP0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CZP0; protein.
DR Bgee; ENSMUSG00000051502; Expressed in bone marrow and 101 other tissues.
DR ExpressionAtlas; Q9CZP0; baseline and differential.
DR Genevisible; Q9CZP0; MM.
DR GO; GO:0071567; F:deUFMylase activity; IDA:UniProtKB.
DR GO; GO:0016790; F:thiolester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR012462; Peptidase_C78_UfSP1/2.
DR Pfam; PF07910; Peptidase_C78; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..217
FT /note="Ufm1-specific protease 1"
FT /id="PRO_0000280361"
FT ACT_SITE 53
FT ACT_SITE 175
FT ACT_SITE 177
FT MUTAGEN 41
FT /note="Y->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:18321862"
FT MUTAGEN 53
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:17182609,
FT ECO:0000269|PubMed:18321862"
FT MUTAGEN 98
FT /note="W->A: Does not affect proteolysis activity."
FT /evidence="ECO:0000269|PubMed:18321862"
FT MUTAGEN 154
FT /note="Q->A: Does not affect proteolysis activity."
FT /evidence="ECO:0000269|PubMed:18321862"
FT MUTAGEN 175
FT /note="D->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:18321862"
FT MUTAGEN 177
FT /note="H->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:18321862"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:2Z84"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:2Z84"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2Z84"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:2Z84"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2Z84"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:2Z84"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2Z84"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:2Z84"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:2Z84"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:2Z84"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:2Z84"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:2Z84"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2Z84"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2Z84"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:2Z84"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:2Z84"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:2Z84"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:2Z84"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:2Z84"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:2Z84"
SQ SEQUENCE 217 AA; 23421 MW; 2790F140B2FA0A35 CRC64;
MTAALPSTLE LLKDVHLGLP VPCHDPARLA LLSGHYLYYH YGCDGLDDRG WGCGYRTLQT
LCSWPGGQSS GVPGLPALQG ALEAMGDKPP GFRGSRNWIG CVEASLCLEH FGGPQGRLCH
LPRGVGLRGE EERLYSHFTT GGGPVMVGGD ADAQSKALLG ICEGPGSEVY VLILDPHYWG
TPKNRCELQA AGWVGWQKVK SVFDSNSFYN LCFTRNL
