ID   A0A1S3RKQ5_SALSA        Unreviewed;      1094 AA.
AC   A0A1S3RKQ5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=LOC106603551 {ECO:0000313|RefSeq:XP_014052866.1};
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_014052866.1};
RN   [1] {ECO:0000313|RefSeq:XP_014052866.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014052866.1};
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};
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DR   RefSeq; XP_014052866.1; XM_014197391.1.
DR   AlphaFoldDB; A0A1S3RKQ5; -.
DR   Ensembl; ENSSSAT00000125396; ENSSSAP00000091232; ENSSSAG00000071195.
DR   GeneID; 106603551; -.
DR   CTD; 29761; -.
DR   OrthoDB; 1423057at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa04.
DR   Bgee; ENSSSAG00000071195; Expressed in semen and 15 other cell types or tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd02665; Peptidase_C19I; 1.
DR   CDD; cd14354; UBA_UBP25; 1.
DR   CDD; cd20486; USP25_C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00726; UIM; 3.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|RefSeq:XP_014052866.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   DOMAIN          187..677
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          485..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..787
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1094 AA;  125109 MW;  62960AC7001A28E5 CRC64;
     MTVEQNVLQQ HSQKHQQTLL NQLREVTGTT DVQLLQQALQ VSHGDLAEAV AFLTEKKTKV
     PQQDEATYYQ TTQVGNDRYI SVGSQADTSE YLPHPALPGA GPSQGDTNVI DLTGDDKDDL
     QRAIALSLEE SSRAFRETGI TDEEQAISRV LEASIAENKA SLKRTHTEVW SDSPNPHDRK
     RMENCPVGLK NVGNTCWFSA VIQSLFNLLE FQRLVLHYSP PVRVQDLPRN QKEHRNLPFM
     QELRNLFSLM VGSKRKYVDP SCAVEILKDA FKSSESQQQD VSEFTHKLLD WLEDAFQMKA
     EEDREGEKPK NPMVELFYGR FLAVGVLEGK KFENTEMFGQ YPLQVNGFKD LHECLEAAMI
     EGEIESLHSS AENSAKSGQE HWFTELPPVL TFELSRFEFN QALGRPEKIH SKLEFPSMLY
     MDRYMDRNRE ITRIKREEIR RLKEHLTLLQ QRLERYLSYG SGPKRFPLAD VLQYAMEFTS
     SKPVCTSPVG DIDTSAPPGG TTGQLLPASS TAEQAPSSTP PEGLAPTPAP STQQRVPIHK
     PFTQSRLPPD LPMHPAPRHI TEEELRVLEG CLHRWRSEVE NDSRDLQGSI SRIHRTIELM
     YSDKSMMQVP YRLHAVLVHE GQANAGHYWA YIYDPHQRCW MKYNDISVTK SSWEELVRDS
     FGGYRNASAY CLMYINDKKP FLIEEEFDKE TGQMLSGLDK LPPDLKAYVK EDNGLFDKEM
     EEWNTLQARK AQQEKLALAV AAAATAAVAE TTATTTSPQP MSTEPSTPDN SAPQQDPEYM
     EQPSPTDYSK HLQEDTERAI SKAAAEQQEE RSPEGLLTAA IKVEYTRLLR FAQEDTAPGS
     DYRLQHVIVY FIQNQAPKKI LERTLLMQFA DRNLGFNERC KSIMKVARAK LDLIKPEEIN
     MEEYEMWHQE YRNFRETTIF LMIGLELFQK KSFVEALMYL IYSYQYNREL LVKGLYRGHD
     DELIGLYRRE CLLKLNENAA GMFESGEEPE VSNGLSIMNE LVVPCIPLLL VHDIEKDLLS
     VEDMRNRWCS YLGQEMEPNL QEKLTDFLPK LLDCSTEIKS FHDPPKLPTY STLELVERYG
     RVMASLSRVP ADGR
//