UFSP2_MOUSE
ID UFSP2_MOUSE Reviewed; 461 AA.
AC Q99K23; Q8C5I0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ufm1-specific protease 2 {ECO:0000303|PubMed:17182609};
DE Short=UfSP2 {ECO:0000303|PubMed:17182609};
DE EC=3.4.22.- {ECO:0000269|PubMed:21228277};
GN Name=Ufsp2 {ECO:0000303|PubMed:17182609, ECO:0000312|MGI:MGI:1913679};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Pancreas;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-294.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Pancreas, Spleen, 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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT ARG-94/ALA-128/SER-294,
RP FUNCTION, INTERACTION WITH DDRGK1, SUBCELLULAR LOCATION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF TYR-282; CYS-294; HIS-398; ASP-418 AND HIS-420,
RP AND ACTIVE SITE.
RX PubMed=21228277; DOI=10.1074/jbc.m110.172171;
RA Ha B.H., Jeon Y.J., Shin S.C., Tatsumi K., Komatsu M., Tanaka K.,
RA Watson C.M., Wallis G., Chung C.H., Kim E.E.;
RT "Structure of Ubiquitin-fold modifier 1 specific protease, UfSP2.";
RL J. Biol. Chem. 286:10248-10257(2011).
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 (PubMed:17182609,
CC PubMed:21228277). Through TRIP4 deufmylation may regulate intracellular
CC nuclear receptors transactivation and thereby regulate cell
CC proliferation and differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q9NUQ7, ECO:0000269|PubMed:17182609,
CC ECO:0000269|PubMed:21228277}.
CC -!- SUBUNIT: Interacts with DDRGK1 (PubMed:21228277). Interacts with TRIP4;
CC deufmylates TRIP4 (By similarity). {ECO:0000250|UniProtKB:Q9NUQ7,
CC ECO:0000269|PubMed:21228277}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21228277}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:21228277}. Nucleus
CC {ECO:0000269|PubMed:21228277}.
CC -!- TISSUE SPECIFICITY: Expressed at high level in brain, kidney, stomach,
CC skeletal muscle and testis. {ECO:0000269|PubMed:17182609}.
CC -!- SIMILARITY: Belongs to the peptidase C78 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37214.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK075795; BAC35964.1; -; mRNA.
DR EMBL; AK078309; BAC37214.1; ALT_SEQ; mRNA.
DR EMBL; BC005503; AAH05503.1; -; mRNA.
DR CCDS; CCDS22284.1; -.
DR RefSeq; NP_619609.1; NM_138668.2.
DR RefSeq; XP_017168107.1; XM_017312618.1.
DR PDB; 3OQC; X-ray; 2.60 A; A/B=1-461.
DR PDBsum; 3OQC; -.
DR AlphaFoldDB; Q99K23; -.
DR SMR; Q99K23; -.
DR BioGRID; 228658; 1.
DR STRING; 10090.ENSMUSP00000034051; -.
DR MEROPS; C78.002; -.
DR iPTMnet; Q99K23; -.
DR PhosphoSitePlus; Q99K23; -.
DR SwissPalm; Q99K23; -.
DR EPD; Q99K23; -.
DR MaxQB; Q99K23; -.
DR PaxDb; Q99K23; -.
DR PeptideAtlas; Q99K23; -.
DR PRIDE; Q99K23; -.
DR ProteomicsDB; 298470; -.
DR Antibodypedia; 45789; 105 antibodies from 20 providers.
DR DNASU; 192169; -.
DR Ensembl; ENSMUST00000034051; ENSMUSP00000034051; ENSMUSG00000031634.
DR GeneID; 192169; -.
DR KEGG; mmu:192169; -.
DR UCSC; uc009lpp.2; mouse.
DR CTD; 55325; -.
DR MGI; MGI:1913679; Ufsp2.
DR VEuPathDB; HostDB:ENSMUSG00000031634; -.
DR eggNOG; KOG2433; Eukaryota.
DR GeneTree; ENSGT00940000157115; -.
DR HOGENOM; CLU_021066_1_1_1; -.
DR InParanoid; Q99K23; -.
DR OMA; GHIKYLI; -.
DR OrthoDB; 444004at2759; -.
DR PhylomeDB; Q99K23; -.
DR TreeFam; TF325896; -.
DR BioGRID-ORCS; 192169; 13 hits in 73 CRISPR screens.
DR ChiTaRS; Ufsp2; mouse.
DR EvolutionaryTrace; Q99K23; -.
DR PRO; PR:Q99K23; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q99K23; protein.
DR Bgee; ENSMUSG00000031634; Expressed in seminal vesicle and 254 other tissues.
DR ExpressionAtlas; Q99K23; baseline and differential.
DR Genevisible; Q99K23; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Hydrolase; Nucleus;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..461
FT /note="Ufm1-specific protease 2"
FT /id="PRO_0000280363"
FT ACT_SITE 294
FT /evidence="ECO:0000269|PubMed:21228277"
FT ACT_SITE 418
FT /evidence="ECO:0000269|PubMed:21228277"
FT ACT_SITE 420
FT /evidence="ECO:0000269|PubMed:21228277"
FT MUTAGEN 282
FT /note="Y->H: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21228277"
FT MUTAGEN 294
FT /note="C->S: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:17182609,
FT ECO:0000269|PubMed:21228277"
FT MUTAGEN 398
FT /note="H->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:21228277"
FT MUTAGEN 418
FT /note="D->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21228277"
FT MUTAGEN 420
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21228277"
FT STRAND 3..16
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 21..41
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 135..148
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 157..179
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3OQC"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 368..374
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:3OQC"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 396..405
FT /evidence="ECO:0007829|PDB:3OQC"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:3OQC"
FT HELIX 427..432
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:3OQC"
FT STRAND 450..455
FT /evidence="ECO:0007829|PDB:3OQC"
SQ SEQUENCE 461 AA; 52515 MW; A04A842782C2A0CE CRC64;
MDILFRIRGG FDLAFQLAPP KEMFIKNALR QVLSDLTTKL SSDALVLRVC NSSVYLWPNS
DANTGELTDS SACKNVVRFI QFDQEEDTKR KFIKKKDKKL TDTQQIVNID LMLEISTPLG
AVTPILEREN EEHHYINMSL PIDAVVSVAP EESWGKVRKL LVDAILRQLV DVEKCILRYM
KGTSIVVPEP LHFQLPGKKN LVTVLYPSGI PDDQLQAYRK ELHDLFNLPH DRPYFKRINA
YHFPDELYKD GYIRNPHTYL SPPNIEGSMI CVVQGTYAYH HYMQDRIDDN GWGCAYRSLQ
TICSWFRHQG YTERSIPTHR EIQQALVDAG DKPATFVGSR QWIGSIEVQM VLNQLIGVTS
KILFVNQGSE MASQGRELAN HFQNVGTPVM VGGGVLAHTI LGVAWNETTG QIKFLILDPH
YTGAEDLQVM LEKGWCGWKS PDFWNKDAYY NLCLPQRPNA L
