ID A0A384AKT3_BALAS Unreviewed; 981 AA.
AC A0A384AKT3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_007187977.1,
GN ECO:0000313|RefSeq:XP_028023715.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028023715.1};
RN [1] {ECO:0000313|RefSeq:XP_007187977.1, ECO:0000313|RefSeq:XP_028023715.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007187977.1,
RC ECO:0000313|RefSeq:XP_028023715.1};
RG RefSeq;
RL Submitted (JAN-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_007187975.1; XM_007187913.1.
DR RefSeq; XP_007187976.1; XM_007187914.1.
DR RefSeq; XP_007187977.1; XM_007187915.2.
DR RefSeq; XP_028023715.1; XM_028167914.1.
DR AlphaFoldDB; A0A384AKT3; -.
DR STRING; 310752.A0A384AKT3; -.
DR GeneID; 103018239; -.
DR KEGG; bacu:103018239; -.
DR CTD; 57695; -.
DR InParanoid; A0A384AKT3; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000261681; Unplaced.
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; 2.
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_007187977.1};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
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 670..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..797
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..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..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; 110303 MW; B83ADB1C06EB6EBF CRC64;
MSPLKIHGPI RIRSMQTGIT KWKEGSFEVV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV
VLRPSGTKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLNAA MKPSQGSGSF
GAILGSRTSQ KETNRQLSYS DNQVSSKRGS LETKDDIPFR KVLGNPGRGS IKAAAGSGVT
ATRTVPSLTS TSTPLRSGLL ENRTEKRKRM LSSGSELNED YPKENDSSSN NKAMTDPSRK
YLTSSREKQL SLKQSEENRT SGLLPLQSSS FYGSRAASKD YSPGSTNLDR TNISSQTPSA
KRSLGFLPQP APLSVKKLRC NQDYTGWNKP RVPLSSHQQQ QLQGFSNLGN TCYMNAILQS
LFSLQSFAND LLKQGIPWKK IPLNALIRRF AHLLVKKDIC NSETKKDLLK KVKNAISATA
ERFSGYMQND AHEFLSQCLD QLKEDMEKLN KTWKTEPVPG EENSPDISAT RVYTCPVITN
LEFEVQHSII CKACGEIIPK REQFNDLSID LPRRKKPLPP RSVQDSLDLF FRAEELEYSC
EKCGGKCALV RHKFNRLPRI LILHLKRYSF NVALSLNNKI GQQVIIPRYL TLSSHCTENT
KPPFNLGWSA QMAISRPLKA SQMVNSCITS PSTPSKNFTF KSKNSLALCL DSDSEDELKR
SVALSQRLCE MSGSEQQQED LEKDSKSCRL ERDKSELENS GFDGMSEEEL LAAVLEISKT
EASPSLSHED DDKPTSSPDT GFAEDDIQEM PENPDPVETE KPKTVTEPDP ASFTEITKDC
DENKENKTPE GSQGEVDWLQ QYDMEREREE QELQQALAQS LQEQEAWEQK EDDDLKRATE
LSLQEFNNSF LDSLGSDEDS GNEDVLDMEY TEAEAEELKR NAETGNLPHS YRLISVVSHI
GSTSSSGHYI SDVYDIKKQA WFTYNDLEVS KIQEASVQSD RDRSGYIFFY MHKEIFDELL
ETEKTSQALS MEVGKTTRQA S
//
