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Database: UniProt
Entry: A0A1S3N203_SALSA
LinkDB: A0A1S3N203_SALSA
Original site: A0A1S3N203_SALSA 
ID   A0A1S3N203_SALSA        Unreviewed;      1296 AA.
AC   A0A1S3N203;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Inactive ubiquitin carboxyl-terminal hydrolase 54-like isoform X4 {ECO:0000313|RefSeq:XP_014009504.1};
GN   Name=LOC106576704 {ECO:0000313|RefSeq:XP_014009504.1};
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_014009504.1};
RN   [1] {ECO:0000313|RefSeq:XP_014009504.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014009504.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085}.
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DR   RefSeq; XP_014009504.1; XM_014154029.1.
DR   OrthoDB; 453826at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa18.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   CDD; cd02257; Peptidase_C19; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR22975:SF5; INACTIVE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 54; 1.
DR   PANTHER; PTHR22975; UBIQUITIN SPECIFIC PROTEINASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|RefSeq:XP_014009504.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   DOMAIN          31..352
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          377..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1017..1118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1166..1233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..546
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..780
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..898
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1060..1076
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1093..1108
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1296 AA;  142685 MW;  BF0B08031A7E7F20 CRC64;
     MSWKRNYFAS GSGGLQGIFT PRTMTSIAPS KGLSNEPGQN SCFLNSALQV LWHLDIFRRS
     FRQLTIHKCM EDSCIFCALK SIFAQFQFSS EKVLPSDALR SALAKTFQDE QRFQLGIMDD
     AAECFENILM RIHFHISDET KEDICTAKHC IPHQKFAMTL FEQCVCSSCG ASSDPLPFIQ
     MVHYISTTSL CNQAVRMLEC RDKPTPDMFG ELLRNASTVG DLRNCPSNCG EKLRIRRVLM
     NSPEIITIGL VWDSDHSDLA EDVIHSLGTC LRLGDLFYRV TDDKAKQAEL YLVGMVCYYG
     KHYSTFFFQT KIRKWMYFDD AHVKEIGPKW KDVVSRCIKG HYQPLLLLYA DPRGTPVSVQ
     DLPSRLDLHH FNKAYYDSED SGREPSISSD TRTDSSTDSY SYKYSRSHHE SMASHFSSDS
     QGTVICNQDN DAASHSSLET TGQVADSGPV QCHSLRKGGT VDRKGGASDR KRSSSRPRRL
     EERSRGSKTD EATSAGYHSE GETLKEQQAP RTATKSSSSS RLRDFKETMS NIIHSRPLSA
     SSSGSGALGG LGVEPGAATK SRDWEADSTS SESKSSSSGG RYRPAWRPRR EVLNIDSIFS
     REKRRQAGYS PLGATLPEDS GAPAEGSTGS VTGKEQGPSG NMASSWTLPT PRGHKMEQQP
     PRLIQRMESG YESSERNSNS PVSLDMPLSE GPNAANAHRD TGLKKPSSSG SGPSWRSVPK
     SKSSSALLQD AKASCRGHSH VSLAGEGRSE LDELQEEVAR RAREQELQRR KEKEKEAALG
     FNPRPSKFMD LDELQNQGKG DSFERCVPDA EVLLDQSLRL EQAGDVSAAL SVVSEAMSKL
     RLPMHEGGAN THSRTVAEAR LQKCMRRARG LQQRMQQQQQ EDRPQQQDQE QTEEQDQPCP
     CPQGPPSEQP VPIKILLMDA QEDQPQAVLE ATRSMPSPLH VKPLPSGTNS LPEPSSHPPV
     SMPPSPHTGS TTGGYVAEAR GRWEGLDMSG VLPHVRPLHK HAAVSLPALC VDGWDESHTE
     GGHDQPPALP NCKPAASPHW NSNPAAQTLP IPHPHSRTHS PVSHTSEERG HANMENAYPR
     RPDAVDSPFY TPPTDSHYPP PAPSRPERTP SPASGDYRSC AAMPVDHWAE NMTRFYNSQP
     APVVGSPCEE LSELDSLYQA SLQAPSLPRA PRGVSPQPTT NKQPARKLLS GLAAPGRSKT
     PTAELERHAY RTAGYTGSPT QHSKPGSCER PLADDENYSA ENLRRIARSL SGTVIGGRPE
     HLAPSRSFEI TRRETSFWLC LTGVKLSPVK TTTVLH
//
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