ID   UBP5_PONAB              Reviewed;         858 AA.
AC   Q5R407;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 5;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 5;
DE   AltName: Full=Ubiquitin thioesterase 5;
DE   AltName: Full=Ubiquitin-specific-processing protease 5;
GN   Name=UBP5;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves linear and branched multiubiquitin polymers with a
CC       marked preference for branched polymers. Involved in unanchored 'Lys-
CC       48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked
CC       polyubiquitin with a lower affinity (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Interacts with TRIML1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; CR861453; CAH93509.1; -; mRNA.
DR   RefSeq; NP_001127051.1; NM_001133579.1.
DR   AlphaFoldDB; Q5R407; -.
DR   SMR; Q5R407; -.
DR   STRING; 9601.ENSPPYP00000004792; -.
DR   GeneID; 100174079; -.
DR   KEGG; pon:100174079; -.
DR   CTD; 8078; -.
DR   eggNOG; KOG0944; Eukaryota.
DR   InParanoid; Q5R407; -.
DR   OrthoDB; 556111at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd14383; UBA1_UBP5; 1.
DR   Gene3D; 3.30.40.10; -; 3.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR041432; UBP13_Znf-UBP_var.
DR   InterPro; IPR041812; UBP5_UBA1.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   Pfam; PF17807; zf-UBP_var; 1.
DR   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Disulfide bond; Hydrolase; Metal-binding; Phosphoprotein;
KW   Protease; Reference proteome; Repeat; Thiol protease;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P45974"
FT   CHAIN           2..858
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 5"
FT                   /id="PRO_0000330479"
FT   DOMAIN          326..856
FT                   /note="USP"
FT   DOMAIN          654..695
FT                   /note="UBA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          722..762
FT                   /note="UBA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   ZN_FING         175..283
FT                   /note="UBP-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   REGION          74..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        335
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        818
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10093"
FT   BINDING         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         221..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P45974"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P45974"
FT   MOD_RES         292
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P45974"
FT   MOD_RES         623
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P56399"
FT   MOD_RES         779
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P45974"
FT   MOD_RES         783
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P45974"
FT   MOD_RES         785
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P45974"
FT   DISULFID        195..816
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   858 AA;  95771 MW;  D085E94B31E5D0EA CRC64;
     MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF LGFGKQYVER
     HFNKTGPRVY LHLRRTRRPK EEDPTTGTGD PPRKKPTRLA IGVEGGFDLS EEKFELDEDV
     KIVILPDYLE IARDGLGGLP DIVRDRVTSA VEALLSADSA SRKQEVQAWD GEVRQVSKHA
     FSLKQLDNPA RIPPCGWECS KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET
     GYPLAVKLGT ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM
     NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VLVLFSIPDF QRKYVDKLEK
     IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPVPESGDGE RVPEQKEVQD GIAPRMFKAL
     IGKGHPEFST NRQQDAQEFF LHLINMVERN CRSSENPNEV FRFLVEEKIK CLATEKVKYT
     QRVDYIMQLP VPMDAALNKE ELLEYEEKKR QAEEEKMALP ELVRAQVPFS SCLEAYGAPE
     QVDDFWSTAL QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS
     QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP TSPMLDESVI
     IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD FANPLILPGS SGPGSTSAAA
     DPPPEDCVTT IVSMGFSRDQ ALKALRATNN SLERAVDWIF SHIDDLDAEA AMDISEGRSA
     ADSISESVPV GPKVRDGPGK YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS
     EKPPKDLGYI YFYQRVAS