ID A0A2U4BMR5_TURTR Unreviewed; 981 AA.
AC A0A2U4BMR5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP37 {ECO:0000313|RefSeq:XP_019794502.1,
GN ECO:0000313|RefSeq:XP_019794503.1, ECO:0000313|RefSeq:XP_033715644.1,
GN ECO:0000313|RefSeq:XP_033715645.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019794503.1};
RN [1] {ECO:0000313|RefSeq:XP_019794502.1, ECO:0000313|RefSeq:XP_019794503.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019794502.1,
RC ECO:0000313|RefSeq:XP_019794503.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR RefSeq; XP_019794502.1; XM_019938943.2.
DR RefSeq; XP_019794503.1; XM_019938944.2.
DR RefSeq; XP_033715644.1; XM_033859753.1.
DR RefSeq; XP_033715645.1; XM_033859754.1.
DR STRING; 9739.ENSTTRP00000010236; -.
DR GeneID; 101321482; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000245320; Chromosome 7.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02257; Peptidase_C19; 2.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 2.30.29.180; Ubiquitin carboxyl-terminal hydrolase 26/29/37, pleckstrin homology-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR032069; USP37-like_PH.
DR InterPro; IPR038093; USP37-like_PH_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 1.
DR Pfam; PF02809; UIM; 3.
DR SMART; SM00726; UIM; 4.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50330; UIM; 3.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU366025,
KW ECO:0000313|RefSeq:XP_019794502.1};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 343..953
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 111..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 799..830
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 111..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 110255 MW; 17E7B388E6D12D97 CRC64;
MSPLKIHGPI RIRSMQTGIT KWKEGSFEVV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV
VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLNAA MKPSQGSGSF
GAILGSRTSQ KETNRQLSYS DNQVSSKRGS LETKDDIPFR KVLGNPGRGS IKAAAGSGVT
ATRTVPSLTS TSTPLRSGLL ENRTEKRKRM LSSGSELNED YPKENDSSSN NKAMTDPSRK
YLTSSREKQL SLKQSEENRT SGLLPLQSSS FYGSRAASKD YSPGSTNLDR TNITSQTPSA
KRSLGFLPQP APLSVKKLRC NQDYTGWNKP RVPLSSHQQQ QLQGFSNLGN TCYMNAILQS
LFSLQSFAND LLKQGIPWKK IPLNALIRRF AHLLVKKDIC NSETKKDLLK KVKNAISATA
ERFSGYMQND AHEFLSQCLD QLKEDMEKLN KTWKTEPVPG EENSPDISAT RVYTCPVISN
LEFEVQHSII CKACGEIIPK REQFNDLSID LPRRKKPLPP RSIQDSLDLF FRAEELEYSC
EKCGGKCALV RHKFNRLPRI LILHLKRYSF NVALSLNNKI GQQVIIPRYL TLSSHCTENT
KPPFNLGWSA QMAISRPLKA SQMVNSCITS PSTPSKNFTF KSKNSLALCL DSDSEDELKR
SVALSQRLCE MSGSEQQQED LEKDSKSCRL EPGKSELENS GFDGMSEEEL LAAVLEISKR
EASPPLSHED DDKPTSSPDT GFAEDDIQEM SENPDPVETE KPKTVTEPDP ASFTEITKDC
DENKENKTPE GTQGEVDWLQ QYDMEREREE QELQQALAQS LQEQEAWEQK EDDDLKRATE
LSLQEFNNSF LDSVGSDEDS GNEDVLDMEY TEAETEELKR NAETGNLPHS YRLISVVSHI
GSTSSSGHYI SDVYDIKKQA WFTYNDLEVS KIQEASVQSD RDRSGYIFFY MHKEIFDELL
ETEKTSQALS MEVGKTTRQA S
//
