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Database: UniProt
Entry: S4R5C4_PETMA
LinkDB: S4R5C4_PETMA
Original site: S4R5C4_PETMA 
ID   S4R5C4_PETMA            Unreviewed;       600 AA.
AC   S4R5C4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase BAP1 {ECO:0000256|ARBA:ARBA00039967};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
DE   AltName: Full=BRCA1-associated protein 1 {ECO:0000256|ARBA:ARBA00042257};
GN   Name=BAP1 {ECO:0000313|Ensembl:ENSPMAP00000000404.1};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000000404.1};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000000404.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007182}.
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DR   AlphaFoldDB; S4R5C4; -.
DR   STRING; 7757.ENSPMAP00000000404; -.
DR   Ensembl; ENSPMAT00000000405.1; ENSPMAP00000000404.1; ENSPMAG00000000365.1.
DR   GeneTree; ENSGT00940000156388; -.
DR   HOGENOM; CLU_018316_5_0_1; -.
DR   OMA; RMKDFTT; -.
DR   Proteomes; UP000245300; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; IPR041507; UCH_C.
DR   PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR10589:SF28; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE BAP1; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   Pfam; PF18031; UCH_C; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          20..69
FT                   /note="Ubiquitin carboxyl-terminal hydrolase family 1
FT                   cysteine active-site"
FT                   /evidence="ECO:0000259|Pfam:PF01088"
FT   DOMAIN          515..560
FT                   /note="Peptidase C12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18031"
FT   REGION          139..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..600
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   600 AA;  64906 MW;  338FA83AFD1E5643 CRC64;
     RPEPRHLPEK QNGLSAVRTM EAFHFVSYVP INGRLFELDG LKAYPIDHGP WGEEEEWTDK
     ARRVIMERIG LATGGEPYHD IRFNLMAVVP DRRQIYEQKL TMLKANRNTV LEALQQLVLV
     TQPELIRAQN PLDATVKATL HSEGSSHDSK AGLPPEGSVQ EARAAPAAPA VPGGGVNGEP
     SRPGPCKAEA GVSPADGGGG GATPPAQAAG PSPSASIPAP RLPAFLDNHN YAKSPLQVLL
     GMGAGKTRLG IWDAPAWPFH VRAGAWRRTD SRTGRTSAVD GDLGTLAQYL HVLHTSHYDT
     QCLHVHTPSS TYTTHTAQRE TQHQLSVAIN SQTQNNAHSG AAEAPGSPAP SDESTDTASE
     IGSAFNSPLR SPVRSRSATR PGSPVSLAPA LPRALLSEEV FARLDAAKHD RALHDMGHRV
     GHELLALEPD GRLRVTSARR LPSPTDGPGA PPAAPALDRT EPPEAAVAAP SGGRAAARSP
     GQDRGPGLPA RRPVQPGKYS PQELLTLLKG VEADISNYEV CLKEEVEKRK KYKIDDQRRT
     HNYDEFICTF ISMLAQQGKL SSLVEQNISV RRRQGVSIGR LHKQRKPDRR RRSRPNRTRK
//
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