ID A0A1S3PH97_SALSA Unreviewed; 496 AA.
AC A0A1S3PH97;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=LOC106585262 {ECO:0000313|RefSeq:XP_014026769.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014026769.1};
RN [1] {ECO:0000313|RefSeq:XP_014026769.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014026769.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_014026769.1; XM_014171294.1.
DR AlphaFoldDB; A0A1S3PH97; -.
DR STRING; 8030.ENSSSAP00000095585; -.
DR PaxDb; 8030-ENSSSAP00000095585; -.
DR GeneID; 106585262; -.
DR KEGG; sasa:106585262; -.
DR OrthoDB; 719409at2759; -.
DR Proteomes; UP000087266; Chromosome ssa24.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR CDD; cd02669; Peptidase_C19M; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033809; USP39.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646:SF16; U4_U6.U5 TRI-SNRNP-ASSOCIATED PROTEIN 2; 1.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 33..130
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 155..484
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 496 AA; 57462 MW; 2E03A06A514C8BEE CRC64;
MVSVKREREL DLEDDEATVP VKVGRSSEDR RSRHCPYLDT INRSVLDFDF EKLCSISLSH
INVYACLICG KYFQGRGLKS HAYTHSVQFT HHVFLNLHTL KFYCLPDNYE IIDSSLEDIT
YVLKPTFTRQ HISGLDKQGK LYRAYDGTTY LPGIVGLNNI KANDYANVVL QALSNVPPLR
NYFLEEENYC GIRRPPGDIM FLLVQRFGEL MRKLWNPRNF KAHVSPHEML QAVVLCSKKN
FQITKQGDAV DFLSWFMNAL HGALGGTKKK PSSLTKVFQG SMRIFSKKLP HPDLPPEEKV
ALLLKEEYQE EMSESTFLFL TLDLPTAPLY KDEKEQLIIP QVPLFNILAK FNGNTEKEYK
TYKENFLKRF QLLKLPPYLI FCIKRFTKNN FFVEKNPTIV NFPITNVDLR EYLTEEAQVT
EKNTTYDLVA NVVHDGKPTE GAYRIHVLHH GTGKWYELQD LQVTDILPQM ITLSEAYIQI
WKRRENEDDT TNHTGA
//
