ID   B4DPD5_HUMAN            Unreviewed;       308 AA.
AC   B4DPD5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Ubiquitin thioesterase {ECO:0000256|PIRNR:PIRNR013503};
DE            EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR013503};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG60547.1};
RN   [1] {ECO:0000313|EMBL:BAG60547.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Kidney {ECO:0000313|EMBL:BAG60547.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR013503};
CC   -!- SIMILARITY: Belongs to the peptidase C65 family.
CC       {ECO:0000256|ARBA:ARBA00006579, ECO:0000256|PIRNR:PIRNR013503}.
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DR   EMBL; AK298287; BAG60547.1; -; mRNA.
DR   AlphaFoldDB; B4DPD5; -.
DR   IntAct; B4DPD5; 3.
DR   MEROPS; C65.001; -.
DR   MaxQB; B4DPD5; -.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd22763; OTUB1; 1.
DR   Gene3D; 3.30.200.60; Peptidase C65 Otubain, subdomain 1; 1.
DR   Gene3D; 1.20.1300.20; Peptidase C65 Otubain, subdomain 2; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR016615; Otubain.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR019400; Peptidase_C65_otubain.
DR   InterPro; IPR042468; Peptidase_C65_otubain_sub1.
DR   InterPro; IPR042467; Peptidase_C65_otubain_sub2.
DR   PANTHER; PTHR12931:SF19; UBIQUITIN THIOESTERASE OTUB1; 1.
DR   PANTHER; PTHR12931; UBIQUITIN THIOLESTERASE PROTEIN OTUB; 1.
DR   Pfam; PF10275; Peptidase_C65; 1.
DR   PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR013503};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR013503};
KW   Thiol protease {ECO:0000256|PIRNR:PIRNR013503};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PIRNR:PIRNR013503}.
FT   DOMAIN          117..308
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR013503-1"
FT   ACT_SITE        128
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR013503-1"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000256|PIRSR:PIRSR013503-1"
FT   SITE            258
FT                   /note="Interacts with free ubiquitin"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR013503-2"
FT   SITE            272
FT                   /note="Interacts with free ubiquitin"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR013503-2"
FT   SITE            274
FT                   /note="Interacts with free ubiquitin"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR013503-2"
FT   SITE            298
FT                   /note="Interacts with free ubiquitin"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR013503-2"
FT   SITE            303
FT                   /note="Interacts with free ubiquitin"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR013503-2"
SQ   SEQUENCE   308 AA;  35181 MW;  BFF9F3468240EC8A CRC64;
     MCGVEGCCQG GATRRGSLPG GRQLATRKRS VVRRCLKMAA EEPQQQKQEP LGSDSEGVNC
     LAYDEAIMAQ QDRIQQEIAV QNPLVSERLE LSVLYKEYAE DDNIYQQKIK DLHKKYSYIR
     KTRPDGNCFY RAFGFSHLEA LLDDSKELQR FKAVSAKSKE DLVSQGFTEL TIEDFHNTFM
     DLIEQVEKQT SVADLLASFN DQSTSDYLVV YLRLLTSGYL QRESKFFEHF IEGGRTVKEF
     CQQEVEPMCK ESDHIHIIAL AQALSVSIQV EYMDRGEGGT TNPHIFPEGS EPKVYLLYRP
     GHYDILYK
//