ID A0A2D0S000_ICTPU Unreviewed; 858 AA.
AC A0A2D0S000;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|PIRNR:PIRNR016308};
DE EC=3.4.19.12 {ECO:0000256|PIRNR:PIRNR016308};
GN Name=usp13 {ECO:0000313|RefSeq:XP_017336074.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017336074.1};
RN [1] {ECO:0000313|RefSeq:XP_017336074.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017336074.1};
RG RefSeq;
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,
CC ECO:0000256|PIRNR:PIRNR016308};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|PIRNR:PIRNR016308}.
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 RefSeq; XP_017336074.1; XM_017480585.3.
DR AlphaFoldDB; A0A2D0S000; -.
DR GeneID; 108272271; -.
DR CTD; 8975; -.
DR OrthoDB; 166948at2759; -.
DR Proteomes; UP000221080; Chromosome 11.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02658; Peptidase_C19B; 1.
DR CDD; cd14384; UBA1_UBP13; 1.
DR CDD; cd14386; UBA2_UBP5; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR InterPro; IPR041432; UBP13_Znf-UBP_var.
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:SF10; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 14; 1.
DR Pfam; PF00627; UBA; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR Pfam; PF17807; zf-UBP_var; 1.
DR PIRSF; PIRSF016308; UBP; 1.
DR SMART; SM00165; UBA; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR016308};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR016308}; Protease {ECO:0000256|PIRNR:PIRNR016308};
KW Thiol protease {ECO:0000256|PIRNR:PIRNR016308};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR016308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR016308};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 168..276
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 318..855
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 633..674
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 708..748
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 753..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT ACT_SITE 817
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ SEQUENCE 858 AA; 97425 MW; EADD277E7D502586 CRC64;
MATDLGELLV PYMPTIRVPR SGDRVYKSEC AFSYDSPESE GGLYVCMNTF LGFGREHVER
HYRKTGQSVY MHLKRHVKEK ATGAAGGAVP RRRNGKVFLD LELNRDFNGD DFEYEDEAKL
VIFPDHYEIP LPNIEELPAL VTIACDAILN AASAYKKQEQ DSWEEELQVS KHARSLRQQE
NGVRIPPSGW KCAKCEMREN LWLNLTDGSV LCGKWFFDGS GGNGHALEHY KETKFPLAVK
LDTITPDGAD VYSFDEEEAV LDPHIAEHLT HFGIDMLKMQ RTENGHHTDN HVQPRATEWE
VIQESGLKLK AVYGSGYTGL RNLGNSCYLS TTMQVLFSIP EFQRAYVGNL QRIFDYSPLD
PTQDFSTQMA KLGHGLLSGQ YSKPPIKSEL IEQVMKEEYK QHRGISPRMF KALVSKGHPE
FSSNRQQDAQ EFFLHFINLV ERNSSGSENP SDVFRFIVEE RVQCCQSQKV RYTQRVDYLM
QLPVPIEAAT NREELIAYET KRKDAEKNLR APPDPVRARI PFTACLQAFN EPENVLDFWS
SALQAKSAGV KTSRFTTFPE YMVVQLKKFT FGVDWVPKKL DVSVDMPDFM DLNRFRATGL
QAGEEELPDL TPPIVIPEDI RDSSVNNSLE SPEIDEASVM QLAEMGFPLE ACRKAVYYTG
NMGAEMAFNW IIAHMEEPDF AEPLAIPSYM EADLPSASFP TVSPLDNQPP EESISILTSM
GFPRHHTIRA LKATNNNLER ALDWIFTHPE SEEESEAMSD MVDTEPNDTS FSNANTHSDS
TLSPEQEMSS PRVRDGPGRY ELFAFISHMG TSTMSGHYVC HIKKEGRWVI YNDHRVCLSE
SPPKDLGYIY FYRRLPSC
//
