ID F7DC76_XENTR Unreviewed; 976 AA.
AC F7DC76;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 69.
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|Ensembl:ENSXETP00000032749,
GN ECO:0000313|RefSeq:XP_002933983.2, ECO:0000313|RefSeq:XP_004917684.1,
GN ECO:0000313|Xenbase:XB-GENE-984278};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000032749};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000032749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000032749};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000032749}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_002933983.2, ECO:0000313|RefSeq:XP_004917684.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_002933983.2,
RC ECO:0000313|RefSeq:XP_004917684.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_002933983.2,
RC ECO:0000313|RefSeq:XP_004917684.1};
RG RefSeq;
RL Submitted (NOV-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 ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR RefSeq; XP_002933983.2; XM_002933937.4.
DR RefSeq; XP_004917684.1; XM_004917627.4.
DR Ensembl; ENSXETT00000032749; ENSXETP00000032749; ENSXETG00000014977.
DR GeneID; 100124313; -.
DR KEGG; xtr:100124313; -.
DR AGR; Xenbase:XB-GENE-984278; -.
DR CTD; 57695; -.
DR Xenbase; XB-GENE-984278; usp37.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_012557_0_0_1; -.
DR OMA; CGEVVNK; -.
DR OrthoDB; 227085at2759; -.
DR TreeFam; TF323032; -.
DR Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR Proteomes; UP000008143; Chromosome 9.
DR Bgee; ENSXETG00000014977; Expressed in ovary and 13 other cell types or tissues.
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; 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 Hydrolase {ECO:0000256|RuleBase:RU366025,
KW ECO:0000313|RefSeq:XP_002933983.2};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 337..948
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 128..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 976 AA; 110102 MW; A72664BB3B1A3FE2 CRC64;
MALHSLHGPI RIHCLKVGTS KWKEGCCEVI EKDNKYCLVV NYNAGGMPTR FQLNQNIKTI
VVKPNGGTQS RFMLTLKDAS SLTIDKVPLK DAENLKHFLE SLDKATIVKS NQGSGSFSGV
LGNRSTQIEA NRPLLNKTQT PSKRVSFDGK DETPVKKLLS NTGRAPVKSS PGNTVSSGRS
GINVTPSPPQ RTSMMESRSE KRKRIQTPSP EIVEDYPKEN DSSTTNKALS DTGRRFLNSS
REKQLSLKQT EENRQGLMPL QSSSFYSSRL TPKEFTTSNT YPDRSSASSQ PPPAKRSLVL
PSQPSPLSVK KLKPNQDYPG WNKQRVLSTH PQPQQLQGFS NLGNTCYMNA ILQSLFSLQP
FAHDLLKQGI PYRKIPTNAL IRRFAHLLAK KDICSPEVKK DLLKKVKSAI SATAERFSGY
MQNDAHEFLS QCLDQLKEDM GKLNKTWKTE LSSGDDVPGV KANDDLSTRI YTCPVTCNFE
FEVQHSIICK ICGETVNKRE QFNDLSIDLP RRKKPSPSRS IQDSLDLFFR LEDLEYACEK
CSGKSATVMH KFSRLPRILI LHLKRYSFNV ILSLNNKVGQ QVVIPRYLTL SSHCTESTRT
PLSLGWNAQT ALNARPLKLS QMVNSCTMST STPLRKQMFK AANSLPVCLD SESDDEQIKR
CVSHSQRICD MELKEQQCED KDKKEASKCL ETGDACFDEM NDDELVAAVL EMSKKETSLS
ESHDDEDKLS SSPDTGFGGD DDVQEIAENH EPMEEERVKT AKEMGVLQYS DMAKDFDENK
ENKTPEASQN DVDWLQYDLE REREEQELQQ ALAQSLQEQE AREMKEDDDL KRATELSLQE
FNNTLMDGMV SDEDSGNEEV LDMEYSEAET EELKKNAETG DLPHSYRLIS VVSHIGSSSS
SGHYISDVYD VRKQAWFTYN DLEVSRTQET TVQSDRDRSG YIFFYMHKDV FDELVEEAKK
SQPASTELNR PIRPPL
//
