ID G1KHK7_ANOCA Unreviewed; 899 AA.
AC G1KHK7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
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:ENSACAP00000008111.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000008111.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000008111.3,
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:ENSACAP00000008111.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP4 subfamily.
CC {ECO:0000256|ARBA:ARBA00037971}.
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DR AlphaFoldDB; G1KHK7; -.
DR STRING; 28377.ENSACAP00000008111; -.
DR MEROPS; C19.010; -.
DR Ensembl; ENSACAT00000008283.4; ENSACAP00000008111.3; ENSACAG00000008007.4.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000156645; -.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; G1KHK7; -.
DR TreeFam; TF106276; -.
DR Proteomes; UP000001646; Chromosome 2.
DR Bgee; ENSACAG00000008007; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028135; Ub_USP-typ.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 4; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
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 259..872
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 100817 MW; 576823DACF96EB51 CRC64;
MAAAEAGFEG GGGGGSSGGA TASPRPDAGT QRTELTPLLG APLCPGESCR WPPNGLALDS
ETQTLKEHLI DELDYVLVPT EAWNKLVNWY GCIEGQKPIL RKVSHLLKIH GVRCFFFFSA
TIEKEMRKQF NIPDGKEIRL WSRYMSNTYE QLSKLDSTIQ DAGLYQGQVV LIEVKNEDGS
WPRQSSQTKS STATSRNLAT SSKSSAGSCS SVVASSAITN GDSNNSYGLN SSHGKGGSSF
SCNFYNNRES SPQSQPGLCG LSNLGNTCFM NSALQCLSNT PPLTEYFLED EYEAEINQEN
PLGMRGEIAE AYAELIKQMW SGRYTHVAPR IFKVTFGHPV VLDFNSQKSQ LASSCWELWE
LKSKIPGGPK NFHLNSELML YRAYGCEQYV NHRLRNDSII VDIFHGLFKS TLVCPKCSKV
SVTFDPFCYL TLPLPMKKDR TMEVLFVFAD PQRKPSQCRV VVPMMGGVTD LCDALSQLSG
IPAENMVVTD VYNHRFHKIF QMDEGLSNIM PKDNIFVYEI SKPAEDGAEC VTLSIYFREK
KARQSSATPA TVLYGQPLLI AVPKHKLTLD YLYSVILERI GRYVKIPSKE DCPDVCSDNE
TCNGSNSVSE GEVEEMEHQN GEEENKEKIL ETDASQSEDG TQVESGKEGL HHRKRLFTFS
LVNSYGTSEI NSLPTEGKIL KLSSHATVAI DWDSDTRKLL FDEHEAQAFE KHCSMFQPQK
RKTAVALRDC IELFTTMETL GEHDPWYCPN CKKHQQATKK FDLWSLPRIL VVHLKRFSYN
RYWRDKLDTV VEFPIRDLNM SEFVCDPAAS PYVYDLIAVS NHYGGMGVGH YTAYAKNKIN
GKWYYFDDSS VSPASEEQIV TKAAYVLFYQ RRDDKLQRNP SPCTNTKMKS EECDGMDTN
//