ID G1KAT4_ANOCA Unreviewed; 969 AA.
AC G1KAT4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 74.
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:ENSACAP00000002401.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000002401.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000002401.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000002401.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000002401.3}
RP IDENTIFICATION.
RG Ensembl;
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR RefSeq; XP_008108416.1; XM_008110209.2.
DR AlphaFoldDB; G1KAT4; -.
DR STRING; 28377.ENSACAP00000002401; -.
DR MEROPS; C19.053; -.
DR Ensembl; ENSACAT00000002462.3; ENSACAP00000002401.3; ENSACAG00000002348.4.
DR GeneID; 100552832; -.
DR KEGG; acs:100552832; -.
DR CTD; 57695; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000158091; -.
DR HOGENOM; CLU_012557_0_0_1; -.
DR OrthoDB; 227085at2759; -.
DR TreeFam; TF323032; -.
DR Proteomes; UP000001646; Chromosome 1.
DR Bgee; ENSACAG00000002348; Expressed in forelimb bud and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
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 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; 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 Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 330..944
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 135..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 109142 MW; B19C2DFFAD104401 CRC64;
MTLLKLCGSI RMHSMQTGTT KWKEGTFEIV DKDSKVTLVI HYNAGGIPKM FQLNRNIKKV
VVQPNKGKLC RLMITLKDSS FLMVDKIPLK DAEEMKLFLE GVQNGTHAAV KIPLGSGSFV
GVLGNRGTQK DSYRQFPYTE NQKRGNVESK VLSSPGRTSV KITPVPGMSG NRFNGSTSPA
TSTPHRTGLL ENRERRKRAP TTPEMNEDYP KENDSSTNNK AMTDPTRKFL HSCREKQLNL
KQAEENRASG LLPLQSSSFY GSRSSKDYSA GNSNLDRSNV LNQTPSAKRT LGFLSQPAPL
SVKKMRSNQD YMGWNKSRVP LSTHPQQQLQ GFANLGNTCY MNAILQSLFS IQSLANDLLK
QNIPWKKVPC NALIRRFSVL LAKKDVCSFE AKKELLKKVK NAISATAERF SGYMQNDAHE
FLSQCLDQLK EDMEKLNKTW KSEPSSGEDS SVGRISDDLS ATRVYTCPII TNLEFEVQHS
IICKMCGETV TKREQFNDLS IDLPRRKKLL PSRSIQDSLD LFFRAEEIEY SCEKCNGKSA
LVTHKFSRLP RVLILHLKRY SYNVALSLNH KVGQQVVIPR FLTLQSHCTE STRPPLNLGW
SAQSTISRPL KVSQMVNSCS VSPSTPSRKY TFKFKGPVVS TMDSDSEEEP LKRPVTNSPK
QCDKEQQRDD LEKSSKRVRT ESEKASESTN AGFDGMNEDE LLAAVLEMSK KETSLSLSHD
EDKPTNSPDT GFGDEELQDL PDNTEPMDVE KPRVSAESGF ATFTEITKDF DENKENKTPE
GAQGDIDWLQ QYDLEREREE QELQQALAQS LQEQQEAREQ KEDDDLKRAT ELSLQEFNNS
LLDSLASDED SGNEDFLDME YSEAEAEELK RNAETGELPN SYRLTSVVSH IGDTSSSGHY
ISDVYDIRKQ AWFTCNDLAV SRIQEASVQS DRDRSGYIFF YMHKDIFDEL LEVEKNTPCV
TAPAKSVVS
//
