GenomeNet

Database: UniProt
Entry: F7FMN7_MACMU
LinkDB: F7FMN7_MACMU
Original site: F7FMN7_MACMU 
ID   F7FMN7_MACMU            Unreviewed;       384 AA.
AC   F7FMN7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN   Name=UCHL5 {ECO:0000313|Ensembl:ENSMMUP00000029812.4,
GN   ECO:0000313|VGNC:VGNC:79197};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000029812.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000029812.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029812.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000256|ARBA:ARBA00000707,
CC         ECO:0000256|RuleBase:RU361215};
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
CC       {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|RuleBase:RU361215}.
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DR   AlphaFoldDB; F7FMN7; -.
DR   SMR; F7FMN7; -.
DR   Ensembl; ENSMMUT00000031862.4; ENSMMUP00000029812.4; ENSMMUG00000022641.4.
DR   VEuPathDB; HostDB:ENSMMUG00000022641; -.
DR   VGNC; VGNC:79197; UCHL5.
DR   GeneTree; ENSGT00940000155195; -.
DR   Proteomes; UP000006718; Chromosome 1.
DR   Bgee; ENSMMUG00000022641; Expressed in ileum and 23 other cell types or tissues.
DR   ExpressionAtlas; F7FMN7; baseline.
DR   GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070628; F:proteasome binding; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02255; Peptidase_C12; 1.
DR   Gene3D; 1.20.58.860; -; 1.
DR   Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001578; Peptidase_C12_UCH.
DR   InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR   InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR   InterPro; IPR033837; UCH37.
DR   InterPro; IPR041507; UCH_C.
DR   PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR10589:SF16; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L5; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   Pfam; PF18031; UCH_C; 1.
DR   PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361215};
KW   Protease {ECO:0000256|RuleBase:RU361215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Thiol protease {ECO:0000256|RuleBase:RU361215};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU361215}.
FT   DOMAIN          75..276
FT                   /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT                   cysteine active-site"
FT                   /evidence="ECO:0000259|Pfam:PF01088"
FT   DOMAIN          332..376
FT                   /note="Peptidase C12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18031"
FT   ACT_SITE        155
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   ACT_SITE        231
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-1"
FT   SITE            246
FT                   /note="Important for enzyme activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038120-2"
SQ   SEQUENCE   384 AA;  43279 MW;  98265DA9F19B8290 CRC64;
     MSLGWLERPR ALRRAAGDGA RRLSGSRRGD VWWTSSAAGL LRSVAGCSWC GGRPRARGGS
     GRCVAGAMTG NAGEWCLMES DPGVFTELIK GFGCRGAQVE EIWSLEPENF EKLKPVHGLI
     FLFKWQPGEE PAGSVVQDSR LDTIFFAKQV INNACATQAI VSVLLNCTHQ DVHLGETLSE
     FKEFSQSFDA AMKGLALSNS DVIRQVHNSF ARQQMFEFDT KTSAKEEDAF HFVSYVPVNG
     RLYELDGLRE GPIDLGACNQ DDWISAVRPV IEKRIQKYSE GEIRFNLMAI VSDRKMIYEQ
     KIAELQRQLA EEEPMDTDQG NSMLSAIQSE VAKNQMLIEE EVQKLKRYKI ENIRRKHNYL
     PFIMELLKTL AEHQQLIPLV EKIF
//
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