ID M3X194_FELCA Unreviewed; 1619 AA.
AC M3X194;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
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:ENSFCAP00000020387.2,
GN ECO:0000313|VGNC:VGNC:99569};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000020387.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000020387.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000020387.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000020387.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000020387.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000020387.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000020387.2};
RG Ensembl;
RL Submitted (SEP-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 EMBL; AANG04003358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011287376.1; XM_011289074.2.
DR STRING; 9685.ENSFCAP00000020387; -.
DR Ensembl; ENSFCAT00000022260.4; ENSFCAP00000020387.2; ENSFCAG00000027422.4.
DR GeneID; 101088794; -.
DR CTD; 84669; -.
DR VGNC; VGNC:99569; USP32.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000155797; -.
DR HOGENOM; CLU_001060_10_1_1; -.
DR InParanoid; M3X194; -.
DR OMA; FKADNRR; -.
DR OrthoDB; 5474185at2759; -.
DR Proteomes; UP000011712; Chromosome E1.
DR Bgee; ENSFCAG00000027422; Expressed in brain and 10 other cell types or tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 3.
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; 2.
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 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:UP000011712};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT DOMAIN 228..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..586
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 749..1582
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1339..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1619 AA; 183272 MW; C174810F41AF29F9 CRC64;
MGAKESRIGF LSYEEALRRV TDVELKRLKD AFKRTCGLSF YMGQHCFIRE VLGDGVPPKV
AEVIYCSFGG TSKGLHFNNL IVGLVLLTRG RDEEKAKYIF SLFASESGSY VVREEMERML
HVVDGKVPDT LRKCFSEGEK VNYEKFRNWL LLNKDAFTFS RWLLSGGVYV TLTDDSDTPT
FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF GPLVSPPIRP SLSEGLFNAF
DENRDNHIDF KEISCGLSAC CRGPLAERQK FCFKVFDVDR DGVLSRVELR DMVVALLEVW
KDNRTDDIPE LHTDLSDIVE GILNAHDTTK MGHLTLEDYQ IWSVKNVLAN EFLNLLFQVC
HIVLGLRPAT PEEEGQIIRG WLERESRYGL QPGHNWFIIS MQWWQQWKEY VKYDASPVVI
EPSSILNGGK HSFGTAVHSI EQSEDRIGGG SLGYMNTTEE RFSDNISTAS EASETAGGGF
LYSATPGADM CFARQHNTSD NNNQCLLGAN GNILLHLSPQ KPGAIDNQPL VTQEPVKATS
LTLEGGRLKR TPQLIHGRDY EMVPEPVWRA LYHWYGANLA LPRPVIKNSK TEIPELELFP
RYLLFLRQQP ATRTQQSNIW VNMGMMSLRM FPQHLPRGNV PSPNAPLKRV LAYTGCFSRM
QTIKEIHEYL SQRLRIKEED MRLWLYNSEN YLTLLDDEDH RLEYLKIQDE QHLVIEVRNK
DMSWPEEMSF IANSSKIDRH KVPTEKGATG LSNLGNTCFM NSSIQCVSNT QPLTQYFISG
RHLYELNRTN PIGMKGHMAK CYGDLVQELW SGTQKNVAPL KLRWTIAKYA PRFNGFQQQD
SQELLAFLLD GLHEDLNRVH EKPYVELKDS DGRPDWEVAA EAWDNHLRRN RSIVVDLFHG
QLRSQVRCKT CGHISVRFDP FNFLSLPLPM DSYMHLEITV IKLDGTTPVR YGLRLNMDEK
YTGLKKQLSD LCGLKSEQIL LAEVHGSNIK NFPQDNQKVR LSVSGFLCAF EIPIPGSPIS
ASSPTQTDFS SSPSTNGMLT LTTNGDLPRP MFIPNGMPNT VVPCGTEKNF TNGMVNGHMP
SLPDNSFTGY IIAVHRKMMR TELYFLSSQK NRPSLFGMPL IVPCTVHTRK KDLYDAVWIQ
VSRLASPLPP QEASNHAQDC DDSMGYQYPF TLRVVQKDGN SCAWCPWYRF CRGCKIDCGE
DRAFIGNAYI AVDWDPTALH LRYQTSQERV VDEHESVEQS RRAQAEPINL DSCLRAFTSE
EELGENEMYY CSKCKTHCLA TKKLDLWRLP PILIIHLKRF QFVNGRWIKS QKIVKFPRES
FDPSAFLVPR DPALCQCKPL TPQGDDLSEP RVLPGEVKKV DAQNSTGEED VFLSKSPSSL
SANIISSPKG SPSSSRKSGT SCPSSKNSSP NSSPRTLGRS KGRLRLPQIG SKNKLSSSKE
NLDASKENGG GQVCELADSL SRGHMMGGSQ TELVTPQDHE VALANGFLYE HEACGNGYSN
GQLENHSEED STDDQREDVR VKPIYNLYAI SCHSGILGGG HYVTYAKNPN SKWYCYNDSS
CKELHPDEID TDSAYILFYE QQGIDYAQFL PKIDGKKMAD TSSMDEDFES DYKKYCVLQ
//
