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Database: UniProt
Entry: A0A1S3NE97_SALSA
LinkDB: A0A1S3NE97_SALSA
Original site: A0A1S3NE97_SALSA 
ID   A0A1S3NE97_SALSA        Unreviewed;       420 AA.
AC   A0A1S3NE97;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=AMSH-like protease isoform X2 {ECO:0000313|RefSeq:XP_014013764.1};
GN   Name=LOC106578960 {ECO:0000313|RefSeq:XP_014013764.1};
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_014013764.1};
RN   [1] {ECO:0000313|RefSeq:XP_014013764.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014013764.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M67C family.
CC       {ECO:0000256|ARBA:ARBA00010981}.
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DR   RefSeq; XP_014013764.1; XM_014158289.1.
DR   AlphaFoldDB; A0A1S3NE97; -.
DR   STRING; 8030.ENSSSAP00000113185; -.
DR   PaxDb; 8030-ENSSSAP00000113185; -.
DR   Ensembl; ENSSSAT00000148222; ENSSSAP00000113185; ENSSSAG00000115451.
DR   GeneID; 106578960; -.
DR   OMA; THNELTI; -.
DR   OrthoDB; 5490729at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa19.
DR   Bgee; ENSSSAG00000079011; Expressed in head kidney and 14 other cell types or tissues.
DR   GO; GO:0061578; F:K63-linked deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08066; MPN_AMSH_like; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR   InterPro; IPR015063; USP8_dimer.
DR   PANTHER; PTHR12947; AMSH-LIKE PROTEASE; 1.
DR   PANTHER; PTHR12947:SF7; AMSH-LIKE PROTEASE; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF08969; USP8_dimer; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR   SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|RefSeq:XP_014013764.1};
KW   Protease {ECO:0000313|RefSeq:XP_014013764.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          253..381
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          202..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   420 AA;  47714 MW;  5AA34E2FB12489D1 CRC64;
     MEQGFSFSTL KKLAAEPDHT DVSLTAAERV LALSKMGCSV EINEEITPRR YFRSGVEMER
     MAAVYLEEGS LENAYVLYNK FITLFVEKLP SHRDYRECSV PEKQVIMKKL QDVAFPRKDQ
     LRKLLHEKFN KEHAAYLMSQ SQAVVVDGCG QQLQRTSLVE QERLRVAQLR RMQMEAEQFR
     YFEDQLRRQE LANRRDEAVA KVPEQTDGSC LSHSSKNHVR LDPNRNQPCL PSSKPAATLA
     GVHTQLVEGL RRVVIPRDLT YKFLLLADSN TARGIETCGV LCGKLTQNEF LLTHVVVPKQ
     SAGPDYCDME NVEELFSFQD HHSLLTLGWI HTHPTQTAFL SSVDLHTHGS YQLMLPEAIA
     IVCSPKHNDT GVFRLTSSGM GEVARCRLKG FHPHSKDPPL FSICRHVVIK DLKTTVLDLR
//
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