ID A0A3B5PS06_XIPMA Unreviewed; 1582 AA.
AC A0A3B5PS06;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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=USP32 {ECO:0000313|Ensembl:ENSXMAP00000022513.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000022513.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000022513.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000022513.1};
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 Ensembl; ENSXMAT00000031212.1; ENSXMAP00000022513.1; ENSXMAG00000009437.2.
DR GeneTree; ENSGT00940000155797; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
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; 3.
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; IPR029071; Ubiquitin-like_domsf.
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; 2.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1582
FT /note="ubiquitinyl hydrolase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017359014"
FT DOMAIN 230..265
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 266..301
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 371..584
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 733..1545
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 437..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1582 AA; 176779 MW; 10107A9C0E8E1FF7 CRC64;
VFTKHQILNL IVFPCLLFVN AVTDVELKRL KDAFKRTSGL SCYMTQQCFY REVLGDGVPP
KVAEVIYSSF GGSSKGLHFN NLIVGLVLLT RGRDEEKAKY LFSLFASDLS GYAAREDIEA
VLQALDGEVP SSLKRCFTES DKVNYERFRN WLLQNKEAFT LSRWLLSGGV CVTLTDDSDT
PTFYQTLAGV THLEESDIID LEKRYWLLKA QSRTGRFDLE TFVPLVSPPI HASLSEGLFH
AFDENRDNHI DFKEISCGLS ACCRGPVAER QKFCFKVFDV DRDGILSRDE LHEMVVALLE
VWKDNRTDTI PELHSSISDI VEEIVKMHDT TKLGHLTLED YQIWSVKSAL ANEFLNLLFQ
VCHIVLGLRP ATPEEEGQII RGWLERESRH GLQQSQSWFL ISMLWWQQWK DYVKYVSIVV
EQPSILSSLR PLTATATVEP ANPDRPGGLG TFGPFSPSEE KSPDAVSSAS EATETALSPQ
LAPSAAESCF ARQHNISENN NQCFSGANGH LPSQLTAQRP GAIDNQSLVT TDPIKAPTLT
MEGGRLKRSL QLVPGRDFEM VPEPVWRALY HWYGANLSLP RPVILESKTG QAELELFPCY
LLFLRQQPAT RSPQSNIWVN MGNVPSPNAP LKRMLAYTGC FSRMATIKDI HLYLSQRLRI
KEEDMRLWLY NSENYLTLLD DEDHTLESLK IQDEQQLVIE VRNKDMSWPE EMSFIANSSK
MDRHKVPTEK GATGLSNLGN TCFMNSSIQC VSNTKPLSDY FLSGRHLYEL NRINPIGMRG
HMAKCYGDLV LELWSGTQKS IAPLKLRWTI AKYAPRFNGF QQQDSQELLA FLLDGLHEDL
NRVHEKPYVE LKDSDGRPDW EVASEAWENH LRRNRSIVVD LFHGQLKSQV KCKTCGHISA
RFDPFNFLSL PLPMDSSMHL EITVIKLDGS TPVRYGLRLN MDEKYTGLKK LLSELCSLKP
EQILLAEVHA SNIKNFPQDN QKVRLSVNGF LCAFEVPVPG SPTSLSSPTL TGYSPLAADF
SLTGDITPTV NGSAANGHLI ANGGPGTLLP CTPETPLVNG VANGHMSPMQ DSPFIGYIIA
MHRKMMRTEL YFLSSQKNRP SLFGMPLIVP CTVHTSKKDL YDAVWIQVSR LASPLPPQEA
SNHAQDCDDS MGYQYPFTLR VVGKDGNSCA WCPWYRFCRG CTIECTEDRA SVGNAYIAVD
WDPTALHLRY QTSQERVTYT PAASDWEQHI THTPLWGGIS TLAERKKEIY EICSAVCLST
RSFCLCFLTI VHLKRFQFVN GRWIKSQKIV KFPRGSFDPS AFLAPRDLEH RSLHSRSESE
GLLRVGEDNL SSISAPAGFC NLPKASPASS RRSAPSLSRN SSPSGSPKPA GRRPGRLRLP
QLGSKHRLSS SKENLDGAAS SEADSRDGVS QADTEERVAI AAGAGPVGSS DQAASESSCG
TEASSSHCDV ILMNGDSNGM GSDCSIESNV DPDSSLLQHR DMCLDPLYNL YAISCHSGIM
GGGHYVTYAK NPNDKWYCYN DSSCKEVHSE EIDTDSAYIL FYEQQGVDYS QFLPKIDGKK
MADTSSMDED FESDYKKYCV LQ
//
