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Database: UniProt
Entry: A0A1S3LGN1_SALSA
LinkDB: A0A1S3LGN1_SALSA
Original site: A0A1S3LGN1_SALSA 
ID   A0A1S3LGN1_SALSA        Unreviewed;      1513 AA.
AC   A0A1S3LGN1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Ubiquitin carboxyl-terminal hydrolase 19-like isoform X1 {ECO:0000313|RefSeq:XP_013989990.1};
GN   Name=LOC106566460 {ECO:0000313|RefSeq:XP_013989990.1};
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_013989990.1};
RN   [1] {ECO:0000313|RefSeq:XP_013989990.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013989990.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_013989990.1; XM_014134515.1.
DR   KEGG; sasa:106566460; -.
DR   OrthoDB; 5474185at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa13.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06466; p23_CS_SGT1_like; 1.
DR   CDD; cd06463; p23_like; 1.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 2.60.40.790; -; 2.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF74; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 19; 1.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF16602; USP19_linker; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 2.
DR   PROSITE; PS51203; CS; 2.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|RefSeq:XP_013989990.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   TRANSMEM        1488..1508
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          49..139
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   DOMAIN          443..545
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   DOMAIN          661..1400
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   DOMAIN          960..1002
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1050..1168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1117..1138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1513 AA;  168221 MW;  AB971D8E485E1B55 CRC64;
     MASSSESGRR NGGQRSADDS TSKKKQKDRA NQESREAKRA AAGANAEHKK DVFVDWKQNA
     NEVIARLRCG DGVQRVEDVT TTFTDTYCQA RFPDGRQWDC HLHEEIEGSC SKVQYKEKSG
     FLLLVMHKKI PFHSWPSLMQ NKKEKQPVKV EAKNGKDQKQ LPLVKPVVKP EKSVPKTADM
     AELSAQTSAP PAQCEQRRGK AERGVKRIMN YKPADKPESG VKAGGEGQTK PVSVSKGDLP
     QEPSAKRTVH PPKDPTSEMP RDTHSKSTSN GKPHSPTGRD LQTSTAGDNR AELLGNGHEG
     TTPEVAISHT QQELKVQMED NKAPESDFKA GAEEVIIPAA TVSSAQISPK AGASTNRTER
     PGEAERTDSE MLVRQPPNEA DQATETLTPT IQSGSGKPVT ATATKQAEPP NSSSTQEEKR
     DRSKEEPLEM KQEEAVPEPM VNLKLLKNDS YEKGTDLMVV NVYMKGIFRE TARVIFREQD
     FTLIFQTSDA NFLRLHADCG ANTVFKWQVK LRNLIQPEQS TYAFTPSRLD ITLKKRHSQR
     WGGLEAPATQ GAVGGAKVAV PSAPSSQASQ PGSSKHSLPA KEEPPWVGEG KPKPPRTVDG
     CLDSVSSRTV SDHVPIKQEP AVTPKPTCMV QPMTHAPPAG SQRSVEEEEE EEEKVCLPGF
     TGLVNLGNTC FMNSVIQSLS NTRELRDYFH DRAFENEINC NNPLGTGGRL AIGFAVLLRA
     LWKGTHHAFQ PSKLKAIVAS KASQFTGYAQ HDAQEFMAFL LDGLHEDLNR IQNKPYTETV
     DSDGRLDEVG EIKVVADEAW QRHKMRNDSF IVDLFQGQYK SKLVCPVCSK VSITFDPFLY
     LPVPLPQKQK VLTVFYFAKE PHKKPMKFLV SVSKENSSTA EVLESISRSV RIKAENLRLA
     EVVKSRFHRI FLPSNSLDTV SSSDMLFCFE VLSKELAKER VVVLRVQQRP QVPSIPISKC
     AACLKPPLSD EEKLKRCTRC YRVGYCNQVC QKKHWSSHKV LCGPNIENVG LPFLVSVPES
     RLTYARLSQL LEGYSRYSVN VFQPPFQSGR TSPEVTQCLA DLPPPAETPE GVGSGEKARG
     GGGGAGDSEQ EDSSLVPESP LETAQASAHP AGDPDALSTH TTDSGFIEPS SGSQDSQGEK
     ETSCEKAVRP EGKAAVTGYQ QPSESASSHT SQFYITILHS NSKEQTLEEK EEAVLDLPED
     SSLELVWKNN ERLKEYVLVR SKELEFEEDP GSVNETARAG HFTLEQCLNL FTRPEVLAPE
     EAWYCPKCQQ HREASKQLLL WRLPNVLIIQ LKRFSFRSFI WRDKINDMVD FPIRNLDLSK
     FCIGQKDDMQ QPPIYDLYAV INHYGGMIGG HYTAYARLPS AQNSQRSDVG WRLFDDSTVT
     MVEESQVVTR YAYVLFYRRR NSPVERPPRL LGPLGAESPT AAGATASQAS LIWQELEQEE
     EGVEEGPRGL FRPRLGRRRA ARREEGVEGQ VWRLLRQRIP HYSDDDCVRY FVLGTLAALL
     ALLVNLLYRA NWG
//
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