ID A0A1S3NMX6_SALSA Unreviewed; 944 AA.
AC A0A1S3NMX6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=LOC106580284 {ECO:0000313|RefSeq:XP_014016590.1,
GN ECO:0000313|RefSeq:XP_014016591.1};
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_014016590.1};
RN [1] {ECO:0000313|RefSeq:XP_014016590.1, ECO:0000313|RefSeq:XP_014016591.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014016590.1,
RC ECO:0000313|RefSeq:XP_014016591.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR RefSeq; XP_014016590.1; XM_014161115.1.
DR RefSeq; XP_014016591.1; XM_014161116.1.
DR STRING; 8030.ENSSSAP00000082116; -.
DR PaxDb; 8030-ENSSSAP00000082116; -.
DR Ensembl; ENSSSAT00000132679; ENSSSAP00000098252; ENSSSAG00000067672.
DR GeneID; 106580284; -.
DR KEGG; sasa:106580284; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000087266; Chromosome ssa20.
DR Bgee; ENSSSAG00000067672; Expressed in liver and 12 other cell types or tissues.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF239; ENDOPLASMIC RETICULUM AMINOPEPTIDASE 2; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|RuleBase:RU364040,
KW ECO:0000313|RefSeq:XP_014016590.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..944
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010814054"
FT DOMAIN 59..246
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 281..485
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 603..922
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 20..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 438
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 944 AA; 107553 MW; 0154F6D74E3189AF CRC64;
MFWVRFLFLA LLSLAGVTQT SSSPTQASEP PNPTEEQPPL NTGSLSFPWS HLRLPEYIVP
LHYHLLLHPN LTILSYIGTV RIELQVQNNT NWVVLHSKGL RITTATVLDQ NLAHLSDQVL
PVLHNPTHEQ VAIFSPRALT GGQKYFLFLE FGADLGEGFY GFYRSTYRTS TGETRTLAST
HFEPTSARMA FPCFDEPSIK ANYSISIRRS PAHTALSNMP VEQTEVLDDG LMEDRFAVSV
RMSSYLVAFI VCDFRSVSAT TASGVKVSVY AAPEKWQQTH YALKAAVKLL EFYEKYFNIS
YPLPKQDLVA IPDFQSGAME NWGLITFRET SLLYDPTTSS ASDRLWVTKV IAHELAHQWF
GNLVTMEWWN DIWLNEGFAT YMEYISVDTT YPKLRVEDYL LDTCFVAIGR DSLNSSRPIS
SVAESPTQIK EMFDTVSYNK GACVLHMLRH YLTDQVFQSG IMRYLRRYSY SNARNQDLWD
SLANTCPEEE FTSGGHCYSN SQAAKNAYLY AGEHLDLTTM MNTWTLQTGV PLVTVARQGS
RLVLKQERFL RTTHPSDPAW PSLQQGYLWH IPLTYRTDTS TSIHRHLMTT LTDSVEVGEE
VGWVKVNVDM AGYYLVHYDG SGWDDLIQLL KNNHTALSFM DRTHLIHNAF QLTTAGRLSL
DKALDLIGYL RSESHTVPLL QGLAYLEAFY RMVERMDIPD VTQNLSTYIL WYFRGVIDRQ
TWSDKGSVSE RRLRSELLSL ACHLGDLPCL EQAQRSFTHW LDSNSTLSLP ADVTETVFSV
GAQEDSGWAS LLHIYTLSLS ETHKHKILSA LASSRDTNKL HRLLELGLEG EVIRTQDLDS
LIVMVARNPR GHHLAWSYVQ KYWSTLVDKF QLGSFSIRNI IIGTTGQFFS TEELTEVRVF
FESIHEQASQ LRVTQVAMDN IQKNILWMQR NLGTLRSWLN QHID
//
