AMPL_CAEEL
ID AMPL_CAEEL Reviewed; 491 AA.
AC P34629;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Leucine aminopeptidase 1;
DE EC=3.4.11.1;
GN Name=lap-1; ORFNames=ZK353.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11295176; DOI=10.1016/s0166-6851(01)00221-3;
RA Joshua G.W.;
RT "Functional analysis of leucine aminopeptidase in Caenorhabditis elegans.";
RL Mol. Biochem. Parasitol. 113:223-232(2001).
CC -!- FUNCTION: Probably acts as a digestive enzyme.
CC {ECO:0000269|PubMed:11295176}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC P34629; P34629: lap-1; NbExp=5; IntAct=EBI-332157, EBI-332157;
CC P34629; O01812: lbp-6; NbExp=2; IntAct=EBI-332157, EBI-327961;
CC -!- TISSUE SPECIFICITY: Expressed in the buccal cavity, pharynx, anterior
CC gut and rectum. {ECO:0000269|PubMed:11295176}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; FO081668; CCD73205.1; -; Genomic_DNA.
DR PIR; S44657; S44657.
DR RefSeq; NP_498854.1; NM_066453.3.
DR PDB; 2HB6; X-ray; 2.00 A; A/B=1-491.
DR PDB; 2HC9; X-ray; 1.85 A; A=1-491.
DR PDBsum; 2HB6; -.
DR PDBsum; 2HC9; -.
DR AlphaFoldDB; P34629; -.
DR SMR; P34629; -.
DR BioGRID; 41389; 33.
DR DIP; DIP-27312N; -.
DR IntAct; P34629; 3.
DR STRING; 6239.ZK353.6; -.
DR MEROPS; M17.A05; -.
DR EPD; P34629; -.
DR PaxDb; P34629; -.
DR PeptideAtlas; P34629; -.
DR EnsemblMetazoa; ZK353.6.1; ZK353.6.1; WBGene00002249.
DR GeneID; 176185; -.
DR KEGG; cel:CELE_ZK353.6; -.
DR UCSC; ZK353.6.1; c. elegans.
DR CTD; 176185; -.
DR WormBase; ZK353.6; CE00390; WBGene00002249; lap-1.
DR eggNOG; KOG2597; Eukaryota.
DR GeneTree; ENSGT00530000063255; -.
DR HOGENOM; CLU_013734_3_1_1; -.
DR InParanoid; P34629; -.
DR OMA; IFDMATL; -.
DR OrthoDB; 562530at2759; -.
DR PhylomeDB; P34629; -.
DR SignaLink; P34629; -.
DR EvolutionaryTrace; P34629; -.
DR PRO; PR:P34629; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002249; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0040009; P:regulation of growth rate; IMP:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR CDD; cd00433; Peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR041417; NPEPL1_N.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF18295; Pdase_M17_N2; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..491
FT /note="Leucine aminopeptidase 1"
FT /id="PRO_0000165831"
FT ACT_SITE 264
FT /evidence="ECO:0000255"
FT ACT_SITE 338
FT /evidence="ECO:0000255"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:2HC9"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 61..77
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 157..178
FT /evidence="ECO:0007829|PDB:2HC9"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 186..199
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 246..257
FT /evidence="ECO:0007829|PDB:2HC9"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:2HC9"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 296..307
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 367..371
FT /evidence="ECO:0007829|PDB:2HC9"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 383..396
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 433..442
FT /evidence="ECO:0007829|PDB:2HC9"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:2HC9"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:2HC9"
FT TURN 459..462
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 473..480
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:2HC9"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:2HC9"
SQ SEQUENCE 491 AA; 52449 MW; AECC10758180D1EF CRC64;
MTQVLVRNGI QAVGDGLTSL IIVGKKSVLK NVTFEGKFKE VAQKFVTDGD SWNSMISRIP
ASGRHPLHYE LAHLITVPDA SSRGNTPTNA HSIYKELKPI NYPEDTKNVH FVLFAEYPDV
LSHVAAIART FCKFSMKTSG IRELNVNIDV VCDKLTNEDA VFLTDLSESV RETARLIDTP
ANILTTDALV DEAVKVGNAT GSKITVIRGE ELLKAGFGGI YHVGKAGPTP PAFVVLSHEV
PGSTEHIALV GKGVVYDTGG LQIKTKTGMP NMKRDMGGAA GMLEAYSALV KHGFSQTLHA
CLCIVENNVS PIANKPDDII KMLSGKTVEI NNTDAEGRLI LADGVFYAKE TLKATTIFDM
ATLTGAQAWL SGRLHGAAMT NDEQLENEII KAGKASGDLV APMLFAPDLF FGDLKSSIAD
MKNSNLGKMD GPPSAVAGLF IGAHIGFGEG LRWLHLDIAA PAEVGDRGTG YGPALFSTLL
GKYTSVPMLK Q
