ID A0A3Q0CKB2_MESAU Unreviewed; 957 AA.
AC A0A3Q0CKB2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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_021083045.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021083045.1};
RN [1] {ECO:0000313|RefSeq:XP_021083045.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [2] {ECO:0000313|RefSeq:XP_021083045.1}
RP IDENTIFICATION.
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_021083045.1; XM_021227386.1.
DR AlphaFoldDB; A0A3Q0CKB2; -.
DR Proteomes; UP000189706; 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; 3.
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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 341..929
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 131..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 775..806
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 131..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 107822 MW; DD1BA9439A01BBFD CRC64;
MSPLKIYGPI RIRSMQTGIT KWKEGSFEIV EKDNKVSLVV HYNTGGIPRT FQLNHNIKNV
VLRPSGTKQS RLMLTLQDNS FLSIDKVPSK EAEEMRLFLD AVHQNRLHAA MKPSQGSGSF
GAILGSRASQ KETNRQLSYS DNQASSKRGG LETKDDIPFR KVLGNPSRGS IKTVAGSGMA
VSRTIPSLTL TSTPLRSGLL ENRTEKRKRM LSGPELTEDY PKENDSSSNN KAMTDPSRKY
LTSSREKQLS LKQAEENRTS GLLPLQSSSF YGSRAGSKDY SSGGSNLDRS NVSSQTPSAK
RSLGFLPQPA PLSVKNLRCN QDYTGWNKPR VPLSSHQQQL QGFSNLGNTC YMNAILQSLF
SLQSFANDLL KQSIPWKKIP LNALIRRFAN LLIKKDISNS ETKKELLKKV KNAISTTAER
FSGYVQNDAH EFLSQCLDQL KEDMEKLNKT WKTEPVLGEE NSPDASATKV FTCPVITNLE
FEVQHSIICK ACGETIPKRE QFNDLSIDLP RRKKPLPPRS IQDSLDLFFR AEELEYSCEK
CGGKCALVRH KFNRLPRVLI LHLKRYSFNV ALSLNNKIGQ QVIIPRYLTL SSHCTENTKP
PFTLGWSAHM AMKFTFKSKS SFTSCLDSDS EDELKRSVAL GQRLCDMSGH EQQQEDVEKD
SKLCRLEPGK SELETSGFDK MSEEEVLAAV LEISRREASP VLSHEDDDKP TSSPDTGFAE
DDVQEMPENP DAMETEKPKT ITEPDPASFT EITKDCDENK ENKTPEGSQG EVDWLQQYDM
EREREEQELQ QALAQSLQEQ EAWEQKEDDD LKRATELSLQ EFNNSFLDSL GSDEDSGNED
VLDMEYTEAE AEELKRNAET GTLPHSYRLI SVVSHIGSTS SSGHYISDVY DIKKQAWFTY
NDLEVSKIQE ATVQSDRDRS GYIFFYMHKE IFDELLETEK NSQALNMEVG KATRQAS
//
