AMP1_CAEEL
ID AMP1_CAEEL Reviewed; 609 AA.
AC G5EFT4; A3QMC1; A3QMC2;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Aminopeptidase ltah-1.1 {ECO:0000305};
DE EC=3.4.11.6 {ECO:0000305|PubMed:9774412};
DE AltName: Full=Aminopeptidase-1 {ECO:0000303|PubMed:9774412};
DE Short=AP-1 {ECO:0000303|PubMed:9774412};
DE AltName: Full=Arginine aminopeptidase 1 {ECO:0000305};
DE AltName: Full=Leukotriene A4 hydrolase homolog ltah-1.1 {ECO:0000312|WormBase:C42C1.11a};
GN Name=ltah-1.1 {ECO:0000303|PubMed:9774412, ECO:0000312|WormBase:C42C1.11a};
GN ORFNames=C42C1.11 {ECO:0000312|WormBase:C42C1.11a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAC70927.1};
RN [1] {ECO:0000312|EMBL:AAC70927.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM A), FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=9774412; DOI=10.1074/jbc.273.43.27978;
RA Abdel Baset H., Ford-Hutchinson A.W., O'Neill G.P.;
RT "Molecular cloning and functional expression of a Caenorhabditis elegans
RT aminopeptidase structurally related to mammalian leukotriene A4
RT hydrolases.";
RL J. Biol. Chem. 273:27978-27987(1998).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Aminopeptidase which preferentially removes N-terminal Arg
CC and Lys residues from peptides and proteins.
CC {ECO:0000269|PubMed:9774412}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal Arg and Lys from oligopeptides when P1'
CC is not Pro. Also acts on arylamides of Arg and Lys.; EC=3.4.11.6;
CC Evidence={ECO:0000305|PubMed:9774412};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P09960};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P09960};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.39 mM for L-Lys-pNitroaniline {ECO:0000269|PubMed:9774412};
CC KM=0.43 mM for L-Arg-pNitroaniline {ECO:0000269|PubMed:9774412};
CC KM=0.46 mM for L-Met-pNitroaniline {ECO:0000269|PubMed:9774412};
CC KM=0.90 mM for L-Val-pNitroaniline {ECO:0000269|PubMed:9774412};
CC KM=1.90 mM for L-Pro-pNitroaniline {ECO:0000269|PubMed:9774412};
CC KM=2.00 mM for L-Leu-pNitroaniline {ECO:0000269|PubMed:9774412};
CC KM=5.53 mM for L-Ala-pNitroaniline {ECO:0000269|PubMed:9774412};
CC Note=No activity with L-Asp-pNA, L-Glu-pNA or D-Leu-pNA.
CC {ECO:0000269|PubMed:9774412};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9774412}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:C42C1.11a};
CC IsoId=G5EFT4-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C42C1.11b};
CC IsoId=G5EFT4-2; Sequence=VSP_058996, VSP_058997;
CC Name=c {ECO:0000312|WormBase:C42C1.11c};
CC IsoId=G5EFT4-3; Sequence=VSP_058995;
CC -!- MISCELLANEOUS: Despite its similarity to leukotriene hydrolases, AP-1
CC does not have leukotriene hydrolase activity. One of the mammalian
CC leukotriene binding sites, 'Tyr-378', is replaced by a Phe residue in
CC AP-1. {ECO:0000269|PubMed:9774412}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; AF068201; AAC70927.1; -; mRNA.
DR EMBL; AF068200; AAC72891.1; -; Genomic_DNA.
DR EMBL; BX284604; CAM36352.1; -; Genomic_DNA.
DR EMBL; BX284604; CAM36353.1; -; Genomic_DNA.
DR EMBL; BX284604; CAM36354.1; -; Genomic_DNA.
DR PIR; T32899; T32899.
DR RefSeq; NP_001023056.1; NM_001027885.2. [G5EFT4-1]
DR RefSeq; NP_001023057.1; NM_001027886.3.
DR RefSeq; NP_001023058.1; NM_001027887.3. [G5EFT4-3]
DR AlphaFoldDB; G5EFT4; -.
DR SMR; G5EFT4; -.
DR STRING; 6239.C42C1.11a; -.
DR MEROPS; M01.025; -.
DR EPD; G5EFT4; -.
DR PaxDb; G5EFT4; -.
DR PeptideAtlas; G5EFT4; -.
DR EnsemblMetazoa; C42C1.11a.1; C42C1.11a.1; WBGene00016589. [G5EFT4-1]
DR EnsemblMetazoa; C42C1.11a.2; C42C1.11a.2; WBGene00016589. [G5EFT4-1]
DR EnsemblMetazoa; C42C1.11b.1; C42C1.11b.1; WBGene00016589. [G5EFT4-2]
DR EnsemblMetazoa; C42C1.11b.2; C42C1.11b.2; WBGene00016589. [G5EFT4-2]
DR EnsemblMetazoa; C42C1.11c.1; C42C1.11c.1; WBGene00016589. [G5EFT4-3]
DR GeneID; 178176; -.
DR KEGG; cel:CELE_C42C1.11; -.
DR UCSC; C42C1.11a.2; c. elegans.
DR CTD; 178176; -.
DR WormBase; C42C1.11a; CE24840; WBGene00016589; ltah-1.1. [G5EFT4-1]
DR WormBase; C42C1.11b; CE33564; WBGene00016589; ltah-1.1. [G5EFT4-2]
DR WormBase; C42C1.11c; CE33565; WBGene00016589; ltah-1.1. [G5EFT4-3]
DR eggNOG; KOG1047; Eukaryota.
DR GeneTree; ENSGT00940000156375; -.
DR InParanoid; G5EFT4; -.
DR OMA; YHPICRQ; -.
DR OrthoDB; 775595at2759; -.
DR PhylomeDB; G5EFT4; -.
DR Reactome; R-CEL-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-9018676; Biosynthesis of D-series resolvins.
DR Reactome; R-CEL-9018681; Biosynthesis of protectins.
DR Reactome; R-CEL-9018896; Biosynthesis of E-series 18(S)-resolvins.
DR Reactome; R-CEL-9020265; Biosynthesis of aspirin-triggered D-series resolvins.
DR Reactome; R-CEL-9023661; Biosynthesis of E-series 18(R)-resolvins.
DR PRO; PR:G5EFT4; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00016589; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:WormBase.
DR GO; GO:0004301; F:epoxide hydrolase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043171; P:peptide catabolic process; IDA:WormBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09599; M1_LTA4H; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.40.320; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; PTHR45726; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM01263; Leuk-A4-hydro_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..609
FT /note="Aminopeptidase ltah-1.1"
FT /id="PRO_0000440800"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT ACT_SITE 387
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 137..139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 268..273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 564..566
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT VAR_SEQ 130
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058995"
FT VAR_SEQ 131..157
FT /note="APYLFSQCQAINARSIVPCMDTPSVKS -> VIFKFKVHFSKIFDNSGSLSI
FT LSMPSN (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058996"
FT VAR_SEQ 158..609
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058997"
SQ SEQUENCE 609 AA; 68249 MW; CE619691165C19A4 CRC64;
MAPPHPRDPS TAANYEQVTV SHYALKWKVD FEKKHIAGDV SITLDVKQDT ERIVLDTRDL
SVQSVALNLN GEPKKAGFTL EDNQALGQKL VITTESLKSG DRPVLEIKYE SSNNAAALQF
LTAEQTTDRV APYLFSQCQA INARSIVPCM DTPSVKSTYE AEVCVPIGLT CLMSAIGQGS
TPSECGKRTI FSFKQPVSIP SYLLAIVVGH LERKEISERC AVWAEPSQAE ASFYEFAETE
KILKVAEDVA GPYVWGRYDL VVLPATFPFG GMENPCLTFI TPTLLAGDRS LVNVIAHEIS
HSWTGNLVTN FSWEHFWLNE GFTVFLERKI HGKMYGELER QFESESGYEE ALVRTVNDVF
GPDHEYTKLV QNLGNADPDD AFSSVPYEKG SALLFTIEQA LGDNSRFEQF LRDYIQKYAY
KTVSTEEWKE YLYDSFTDKK VILDNIDWNL WLHKAGLPPK PKYDSTPMQA CKDLAAKWTT
EGSEAPTDGE VFAKMSNSQK LAVLDAVRVN KTMFGDRMPA LTATYKLDQA KNAELKFSWL
MLGLETKWSP IVDASLAFAL AVGRMKYCKP IYRSLFGWSA TRDRAISQFK ANIPNMHPIT
VKAIQSLLK
