ID A0A3Q2C9H0_CYPVA Unreviewed; 1586 AA.
AC A0A3Q2C9H0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=USP6 {ECO:0000313|Ensembl:ENSCVAP00000001436.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000001436.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000001436.1}
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|ARBA:ARBA00000707};
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DR STRING; 28743.ENSCVAP00000001436; -.
DR Ensembl; ENSCVAT00000013423.1; ENSCVAP00000001436.1; ENSCVAG00000002419.1.
DR GeneTree; ENSGT00940000155797; -.
DR OMA; FKADNRR; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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:SF76; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 32; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF14836; Ubiquitin_3; 1.
DR Pfam; PF00443; UCH; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00695; DUSP; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT DOMAIN 236..263
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 264..299
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 369..594
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 743..1549
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 448..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1586 AA; 177606 MW; C4BB97F4162C16C2 CRC64;
MGAKESRIGF LSYDEAVRRV TDVELKRLKD AFKRTSGLSF YMTQQCFYRE VLGDGVPPKV
AEVIYSSFGG SSKGLHFNNL MVGLVLLTRG RDEEKAKYLF SLFASDLGGY AAREDIEAVL
QVLDGEVPSS LKKCFIESDK VNYERFRIWL LQNKEAFTLS RWLLSGGVCV TLTDDSDTPT
FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF VPLVSPPIHA SLGEGLFHAF
DENRDNHIDF KEISCGLSAC CRGPVAERQK FCFKVFDVDR DGVLSRDELH EMVVALLEVW
KDNRTDTIPE LLTNVSDIVE EILKMHDTTK LGHLTLEDYQ IWSVKSALAN EFLNLLFQVC
HIVLGLRPAT PEEEGQIIRG WLERESRHGL QQGQNWFLIS MLWWQQWKDY VKYDSPRCCL
PVQEHNGIVV EQPSILSFLR APMATATVEP AHPDRPGGLG SFGPSSPSEE KSPDAVSSAS
EATENALSPQ LAPSAAESCF ARQHNLSENN NQCFSAANGH LPSQLTAQRP GAIDNQSLVT
TEPIKAPTLT MEGGRLRRSL QLVPGRDFEM VPEPVWRALY HWYGANLSLP RPVILESKTG
QAELELFPRY LLFLRQQPAT RSPQSNIWVN MGNVPSPNAP LKRMLAYTGC FSRMGTIKDI
HLYLSQRLRI KEEDMRLWLY NSENYLTLLD DEDHTLESLK IHDEQQLVIE VRNKDMSWPE
EMSFIANSSK MDRHKVPTEK GATGLSNLGN TCFMNSSIQC VSNTKPLSDY FLSGRHLYEL
NRTNPIGMRG HMAKCYGDLV MELWSGTQKS VAPLKLRWTI AKYAPRFNGF QQQDSQELLA
FLLDGLHEDL NRVHEKPYVE LKDSDGRPDW EVASEAWENH LRRNRSIVVD LFHGQLKSQV
KCKTCGHISA RFDPFNFLSL PLPMDSSMHL EITVIKLDGS TPVRYGLRLN MDEKYTGLKK
LLSELCVLKP EQILLAEVHA SNIKNFPQDN QKVRLSVNGF LCAFEVPVPG SPTSLSSPTL
TDVTPTVNDS AANGHLIPNG GPGTAVASSP ETPLVNGVGN GHITPVQESP FIGYIIAMHR
KMMRTELYFL SSQKNRPSLF GMPLIVPCTV HTSKKDLYDA VWIQVSRLAS PLPPQEASNH
AQDCDDSMGY QYPFTLRVVG KDGNSCAWCP WYRFCRGCTV ECTEDRASVG NAYIAVDWDP
TALHLRYQTS QERIVEEHCS VEQSRRAQAE PISLDSCLKA FTSEEELGED ELYYCSKCKT
HRLATKKLDL WRLPPILIVH LKRFQFVNGR WIKSQKIVKF PREKFDPSAF LAPRDLEHRC
LQSRSESEDL LRVGEDNLSS ISAPAGFCNL PKASPASSRR SAPSLSRNSS PSGSPKSGGR
RPGRLRLPQL GSKHRLSSSK ENLDGAASSE ADGAPQTDAE AGVTAAAAGP LSSGDPMASE
SSCGTEASSS HCDVILVNGD SNGMGSDCSI ESNAEPEGSL LQHRDMCLDP LYNLYAISCH
SGIMGGGHYV TYAKNPNDKW YCYNDSSCKE VHSEEIDTDS AYILFYEQQG VDYSQFLPKI
DGKKMADTSS MDEDFESDYK KYCVLQ
//
