ID B0WCR0_CULQU Unreviewed; 594 AA.
AC B0WCR0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=6036443 {ECO:0000313|EnsemblMetazoa:CPIJ004845-PA};
GN ORFNames=CpipJ_CPIJ004845 {ECO:0000313|EMBL:EDS43786.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS43786.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS43786.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ004845-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ004845-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR EMBL; DS231890; EDS43786.1; -; Genomic_DNA.
DR RefSeq; XP_001846494.1; XM_001846442.1.
DR AlphaFoldDB; B0WCR0; -.
DR STRING; 7176.B0WCR0; -.
DR MEROPS; C67.A01; -.
DR EnsemblMetazoa; CPIJ004845-RA; CPIJ004845-PA; CPIJ004845.
DR KEGG; cqu:CpipJ_CPIJ004845; -.
DR VEuPathDB; VectorBase:CPIJ004845; -.
DR VEuPathDB; VectorBase:CQUJHB001066; -.
DR eggNOG; KOG3556; Eukaryota.
DR HOGENOM; CLU_003910_2_0_1; -.
DR InParanoid; B0WCR0; -.
DR OMA; PIFVLEH; -.
DR OrthoDB; 5397179at2759; -.
DR Proteomes; UP000002320; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR PANTHER; PTHR11830:SF3; CYLINDROMATOSIS, ISOFORM D; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000313|EMBL:EDS43786.1};
KW Ribosomal protein {ECO:0000313|EMBL:EDS43786.1}.
FT DOMAIN 229..588
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 29..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..68
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 66719 MW; A9A0F979FCF01F38 CRC64;
MIPDFVDLMN SDVSDIPLTV LDFYDPADSS EHYEDPTDTS SLITFDNGNG SVLPPPPPHG
PSPSDPEAVI QPSPLKELPD NALLEVGSMV EVDVEHAELY GVIRWIGPLH IPGTISSSNT
RVMVGIELEE EPMEGSVEIT DGVYDNVRLY KCPAHRGIFV FPAQCNQDRR FQDVLPSANQ
IPPKVVASSS KSEAGQMFGA KDCPIVVGSV APLKILKPDG LDAICGKFKG IQGHHNSCYL
DATLFSMFTF TSVFDSLLFR PREPEDNSQY EEVQRVLREE IVNPLRANHF VRADRVMKLR
QLLDRLSSVT GLTSEEKDPE EFLNSLLAQI LRADPFLKLS SGLDTFYYQL FVEKDDQLKL
PSVQQLFEQS FLTSNIKLKE VPSCLIIQMP RFGKNFKMYP RILPSQVLDV TDIIEDSPRQ
CTVCGCLAEH ECRDCFGMMQ GSIDSLESTA FCQTCLEKAH THVKRQNHTP SPLTVPKDYK
MMADHCPVPR LFMELFAVVC IETSHYVAFV KAASGQDAPW VFFDSMADRK GEQNGYNIPE
MIPVPDLPQW LSEDGARQLN EKAINDKMLP EHAKRLLCDA YMCMYQSTDV MMYR
//
