ID A0A1S3SP28_SALSA Unreviewed; 963 AA.
AC A0A1S3SP28;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=LOC106610934 {ECO:0000313|RefSeq:XP_014066097.1};
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_014066097.1};
RN [1] {ECO:0000313|RefSeq:XP_014066097.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014066097.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal glutamate (and to a lesser extent
CC aspartate) from a peptide.; EC=3.4.11.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001703};
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 -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR RefSeq; XP_014066097.1; XM_014210622.1.
DR AlphaFoldDB; A0A1S3SP28; -.
DR GeneID; 106610934; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000087266; Chromosome ssa09.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF242; GLUTAMYL AMINOPEPTIDASE; 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_014066097.1};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Membrane {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 Transmembrane {ECO:0000256|RuleBase:RU364040};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364040};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364040"
FT DOMAIN 94..288
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 323..540
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 622..941
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 43..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 396
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 359..363
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 893
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-2"
FT SITE 481
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 963 AA; 110329 MW; FDC297113972C86A CRC64;
MIESMDFEKE EKHYFIRGKH VALICAVVVV SAIAVGLGVG LTRPDSTLTD PAPTEETSKP
TPNPTPPPAD RGPCKPSNNT DGDWKNFRLP DYVKPVHYDL HLEPDLTTDL YTGSVSVHLE
VSRPTRHLWL HIRETFISAV PRLVLKTPQA QREVTVAIKG CFEFKPQEYV VVEATEELVA
TKLNEVYVLS LDFQGWLNGS LVGFYRVTYT ENGAIKKIAA TDHEPTDARK SFPCFDEPNK
KATYNISITH DKDYGALANM PMEGTPETLP GNKIKTFFKR SVPMSTYLVC FAVHQFTFVE
RNSSRGIPLR IYAQRAQIRT AEYAADTTKV IFDYFEEYFN MNYSIPKLDK IAIPDFGTGA
MENWGLITYR EANLLYDENQ SSSYNKQRVA SVIAHELVHQ WFGNIVTMDW WDDLWLNEGF
ASFFEYIGVE KAEPLWGMRD IMIISDVLPV MVDDALVTSH PIIVDVSTPA EITSVFDGIS
YNKGASILRM VEDWLGRDNF RDGCRKYLKD FHFQNAKTAN FWASLANVSG LPVADVMDTW
TKQMGYPVLD LSTAGTQTKL TQRRFLLDPN ADTTQPPSPL SYKWTIPVKW HSVDSNKNMS
IMFNKSSSEQ VLADYFPATD GLLKINNDHI GFYRVNHHDS MWSTISQQLQ TNHKEFDAAD
RCSYIDDVFA LGRADVVDYG NAFNLTKYLT NETEYIVWER VSSSIAYVRD MLSDDTVLYP
KFQKLFREHV QTISRQLGWD DKGSQRDRLL RETVLGIACQ MGDQEMLNEA SVLFDQWISG
NISVGVNLRL LVYRYGMRNS GTEAKWNLMF ERYKTETLAQ EKDKLLYGLA SVENITLLFN
LLEVSKDESI VRTQDLFTVV QYVSLNRYGK TMAWDWVTLN WDYLVNRYTI NDRSLGRLLT
RISTTYNTEL QLWQMVHFFK LNPNAGAGEM PRQQALETVR NNIEWVRRNK AEISSWLESN
VAY
//
