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
//