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Database: UniProt
Entry: A0A3P8XFW6_ESOLU
LinkDB: A0A3P8XFW6_ESOLU
Original site: A0A3P8XFW6_ESOLU 
ID   A0A3P8XFW6_ESOLU        Unreviewed;       882 AA.
AC   A0A3P8XFW6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000003480.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000003480.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000003480.2}
RP   IDENTIFICATION.
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};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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DR   AlphaFoldDB; A0A3P8XFW6; -.
DR   Ensembl; ENSELUT00000013964.2; ENSELUP00000003480.2; ENSELUG00000004755.2.
DR   GeneTree; ENSGT00940000157401; -.
DR   InParanoid; A0A3P8XFW6; -.
DR   OMA; MTNHFVE; -.
DR   Proteomes; UP000265140; LG08.
DR   Bgee; ENSELUG00000004755; Expressed in bone element and 11 other cell types or tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProt.
DR   CDD; cd02658; Peptidase_C19B; 1.
DR   CDD; cd14384; UBA1_UBP13; 1.
DR   CDD; cd14387; UBA2_UBP13; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR016308-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR016308-3};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00502}.
FT   DOMAIN          181..289
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   DOMAIN          336..879
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          652..693
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          728..768
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          767..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        345
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT   ACT_SITE        841
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-1"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
FT   BINDING         208
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"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016308-3"
SQ   SEQUENCE   882 AA;  99374 MW;  D18D454ADB895E84 CRC64;
     SQKRTGHPSE NAKMAADLGE LLVPYMPTIR VPRTGDRVFK SECAFSYDSP ESEGGLYVCM
     NTFLGFGREH VERHYRKTGQ SVYMHLKRHV KEKSPGAAGG AIPRRRNGKV FLDLELNRDF
     NGDEYECEDE AKLVIFPDHY EIPLPNIEEL PALVTIACDA VLNAVSAYKK QEHDSWEEEI
     QTSKHSRGLR QLDNGVRIPP SGWKCQKCEM RENLWLNLTD GSVLCGKWFF DGAGGNGHAL
     EHYKETKFPL AVKLDNITPD GADIYSFDEE EAVLDPQISE HLQHFGIDML QMQRNGTENG
     HHNTDNSNDA RPRVSEWEVI QEAGMKLKAV YGSGFTGIKN LGNSCYLGTT MQVLFSIPEF
     QRAYVGNLQR IFDYSPLDPT TDFNTQMAKL GHGLLSGLFS KPPIKSELIE QVMKEEHKPK
     GISPKMFKAL ISRGHPEFSS NRQQDAHEFF LHLINLVERN SAGSENPSDV FRHLVEERVQ
     CCQTKRVRYT HKVDYVMQLP APMEAASNRE ELIAYEAKRK EAEENMRAPP EPVRARIPFT
     ACLQAFTEPE NVPDFWSSAL QAKSAGVKTS RFASFPEYLV MQIKKFTFGV DWVPKKLDLS
     IEVPDFLDLS RFRGTGLQAG EEELPDLAPP IVLPEDTRGE GQFQLVSPLS PEIDESAAMQ
     LAEMGFPLEA CRKAVYYTGN MGPEMAFNWI IAHMEEPDFA EPLALPSFME PATSMASPGL
     AGTPLDNQPP EESIAILTSM GFPRRHTVQA LRASNNNLER ALDWIFTHPE REEDEETSDA
     LSDMADTTEP NDNVFSNANT NSDSTLSPDQ DPSGPRVKDG PGRYELFAFI SHMGASTMSG
     HYICHVKKEG RWVIFNDHKV CLSERPPKDL GYIYFYRRLS SR
//
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