ID   UBP11_YEAST             Reviewed;         717 AA.
AC   P36026; D6VXF9;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 11;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 11;
DE   AltName: Full=Ubiquitin thioesterase 11;
DE   AltName: Full=Ubiquitin-specific-processing protease 11;
GN   Name=UBP11; OrderedLocusNames=YKR098C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
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;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; Z28323; CAA82178.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09249.1; -; Genomic_DNA.
DR   PIR; S38177; S38177.
DR   RefSeq; NP_013024.1; NM_001179888.1.
DR   AlphaFoldDB; P36026; -.
DR   SMR; P36026; -.
DR   BioGRID; 34229; 79.
DR   IntAct; P36026; 1.
DR   MINT; P36026; -.
DR   STRING; 4932.YKR098C; -.
DR   MEROPS; C19.102; -.
DR   iPTMnet; P36026; -.
DR   MaxQB; P36026; -.
DR   PaxDb; 4932-YKR098C; -.
DR   PeptideAtlas; P36026; -.
DR   EnsemblFungi; YKR098C_mRNA; YKR098C; YKR098C.
DR   GeneID; 853973; -.
DR   KEGG; sce:YKR098C; -.
DR   AGR; SGD:S000001806; -.
DR   SGD; S000001806; UBP11.
DR   VEuPathDB; FungiDB:YKR098C; -.
DR   eggNOG; KOG1868; Eukaryota.
DR   GeneTree; ENSGT00940000168459; -.
DR   HOGENOM; CLU_004122_1_0_1; -.
DR   InParanoid; P36026; -.
DR   OMA; GICRTIK; -.
DR   OrthoDB; 227085at2759; -.
DR   BioCyc; YEAST:G3O-32060-MONOMER; -.
DR   BioGRID-ORCS; 853973; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P36026; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36026; Protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:SGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF24; USP DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..717
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 11"
FT                   /id="PRO_0000080596"
FT   DOMAIN          298..707
FT                   /note="USP"
FT   REGION          231..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        545..565
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        307
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        649
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   717 AA;  82703 MW;  9BAA1EEEB5DD9A65 CRC64;
     MLLNPDQILN LVRKVYEVDI KQFYSQLRLK NLRGLLDHAA HLFNVYLRDL EINQEMEALT
     AFIIGCYYLY LIIPQSLQFQ TRNNLYSSYA KLKNDYQDEH VMGYVLKVVR DESTVIVDRY
     LAESNGICRT IKRKRAYSLP LRPLPVHMAS LSIHNKFDGS LHEIPNELTK PTNDNSKEDI
     VRESNQIASS NKLEAGSEVA YYTSKEALSK PSYLKLSTGK DALFKTLSSP ATAPPVHSLE
     VSSQIRDSSQ DSSSSLSKVE KPKEEEGKIE AIESSAPKAY NLPVIEDSND LLSELSITGL
     QNPCNTCYIN SIIQCLFGTT LFRDLFLTKK YRLFLNTNKY PKEVQLSRSI YVLFKKMYLN
     GGRAIIPNRF LKMCKKLRPD LNIPDDQQDT QEFLLIVLAR IHEELSNENV VKYYPDLVSY
     DANALQVNPS KYEKWYERNV ITDGLSPIDH IYRGQLENIL KCQRCGNSSY SYSTFYVLSL
     AIPKLSLYSF TSKSRKIKLE DCINLFTGDE ELSGDNAWDC PNCRITDSKS KKEEITSQKK
     KSTIFGFHSR SRSKSPHHHH HHHHSSDDST KNAKKRNSKK LTTIKSLDFI VLPPILVIHL
     SRFYYDLTKK NSTVITYPLI LNIILKNGKV IRYKLYGTVN HSGNLINGHY TSVVNKEKSH
     EIGLNRQVWV TFDDDYIQQH RKDRNNFEAG KTEMSSDEVY VLFYERMDEE NYEEEFC
//