ID T1ELN7_HELRO Unreviewed; 830 AA.
AC T1ELN7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=20197487 {ECO:0000313|EnsemblMetazoa:HelroP155886};
GN ORFNames=HELRODRAFT_155886 {ECO:0000313|EMBL:ESN98734.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP155886, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESN98734.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP155886}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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, 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. USP20/USP33 subfamily.
CC {ECO:0000256|ARBA:ARBA00008269}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMQM01001049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB097143; ESN98734.1; -; Genomic_DNA.
DR RefSeq; XP_009022715.1; XM_009024467.1.
DR AlphaFoldDB; T1ELN7; -.
DR STRING; 6412.T1ELN7; -.
DR EnsemblMetazoa; HelroT155886; HelroP155886; HelroG155886.
DR GeneID; 20197487; -.
DR KEGG; hro:HELRODRAFT_155886; -.
DR CTD; 20197487; -.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_004896_0_0_1; -.
DR InParanoid; T1ELN7; -.
DR OMA; IDQDDEC; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.2230.10; DUSP-like; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF86; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51283; DUSP; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000015101};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 2..109
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 126..608
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 606..703
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 715..817
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 280..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 95095 MW; F21CDB2F21FD513A CRC64;
METCSHLDLL KNFSLDELNQ FKNPHCSSCL APNPNLWLCL QPMCNYIGCG ESVKDHSLQH
SQLSKHPLII NLSTKRLWCN VCEMEVHLKM FSQYSQHSYQ ELNMFFCDDS DDSYIEDKMA
QPRGLVGLIN LGNTCYMNAA IQSLSNCPPL TQFFLDCPGY VNLAKRPNIS KIFMRLMAEI
WHKNRPRQLS PTGLFSCIKQ LHPMFRGFSQ HDSQEFLRYL MDNLHEELKE IIITPVEYDS
QSENSSTSKY SVSKSLTSDL GYDTCESVLA NDQASVAVSC NSSSSGFTQK EFTSRDNVDE
ESHDSDNTQI NSDENFEHVD ENVFAGEMEN YSKDIPPRTR SQTSLRADMF DNIRESNEMN
KLHQTPEYSS IISDIFDGHI LSSVQCMTCE NISTTKEVFQ DLSLPIPSSD QIPVIRSSNG
IVLSSHGSSD DLLAKRPGWM SWFYNLFRGM IWGPSIHLQD CLAAFFSADD LKGDNMYSCE
KCKKLRNGLK YSKVMKLPEI LCIHLKRFRH DYTFSSSSAS KISSAVVFPV ERLDMQPYLH
KDCKDSVTSY CLIAVICHHG TANGGHYTAY GLNTINNTWY EYDDQTVTEV DIQQVERSQA
YVLFYQKLDD EINILREKVQ SVMKINNNGL MKFYISRKWL SKFKTFSEPG PINNYDFLCR
HGAVKPQYSS DIMDLVIELP PRMWEFFHST FGGGPSVNHL LTCDTCKVEI ESLKKRREYE
LNMFLQLNRA FKENEPGNSA VVAISMTWFR EWENFVRGIS DIPPKKIENS HICTMRSNSS
SPVLLQNSDY GQMGEDTYNF LSDLYGGGPL VYVQQRIYQM RLSSSNSDNY
//
