AMPL_DICDI
ID AMPL_DICDI Reviewed; 520 AA.
AC Q5V9F0; Q54WC1;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Leucine aminopeptidase;
DE Short=LAP;
DE AltName: Full=Leucyl aminopeptidase;
DE AltName: Full=Proline aminopeptidase;
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase;
GN Name=lap; ORFNames=DDB_G0279793;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Huang J., Mullapudi N., Lancto C., Scott M., Abrahamsen M., Kissinger J.C.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 74-91; 127-155; 193-226; 249-257; 265-286; 347-360;
RP 436-443; 451-460 AND 510-517, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Veltman D.M., Insall R.H.;
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC intracellular proteins. Catalyzes the removal of unsubstituted N-
CC terminal amino acids from various peptides (By similarity).
CC {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
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 -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; AY581145; AAT92029.1; -; Genomic_DNA.
DR EMBL; AAFI02000032; EAL67576.1; -; Genomic_DNA.
DR RefSeq; XP_641537.1; XM_636445.1.
DR AlphaFoldDB; Q5V9F0; -.
DR SMR; Q5V9F0; -.
DR STRING; 44689.DDB0231024; -.
DR MEROPS; M17.001; -.
DR PaxDb; Q5V9F0; -.
DR PRIDE; Q5V9F0; -.
DR EnsemblProtists; EAL67576; EAL67576; DDB_G0279793.
DR GeneID; 8622210; -.
DR KEGG; ddi:DDB_G0279793; -.
DR dictyBase; DDB_G0279793; lap.
DR eggNOG; KOG2597; Eukaryota.
DR HOGENOM; CLU_013734_1_2_1; -.
DR InParanoid; Q5V9F0; -.
DR OMA; AFLMIAK; -.
DR PhylomeDB; Q5V9F0; -.
DR PRO; PR:Q5V9F0; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Zinc.
FT CHAIN 1..520
FT /note="Cytosol aminopeptidase"
FT /id="PRO_0000328614"
FT ACT_SITE 298
FT /evidence="ECO:0000250"
FT ACT_SITE 372
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 520 AA; 56410 MW; EE9ECBB8B54C0E85 CRC64;
MLKNIINKKN LFINNQQNIF QIIKRNKMTD STVDNKGYIV GIYENEEFTP LGQQLNEKTN
GHLLKSIKLS DTKGKVGDNL VLYNVTPEVS RVAIVGLGKK ENNNSTTYEK NENTRKAIGS
GVKALKSKNA THLTIDSNIG DAKQTAEGAF LSNFKFDFKT GTSGKTANST NESIQVQLSP
SPSSEECFKE GKILAESQNF ARVLMETPAN LLTPTNFVQH VSSQMKELID SGKVEMIVRE
EQWVKDQKMG MFWGVAKGSD EPLKFLELHY RGASADGKDS IVYVGKGITF DSGGISIKPS
ANMGLMKGDM GGAATAVSAM FGVASLGLKV NLITITPLCE NMPSGKATKP GDILTAANGK
TVEVDNTDAE GRLILGDALH YACSFKPTHI IDIATLTGAI DVALGQHYAG CFTTTDSLWD
QLNECGNISG ERLWRMPLIP EYRKQMETSK VADLINSAGR SGGACCAAGF LKEFITADQS
WSHLDIAGVM SSSEDGPYIR KGMTGKPTRT LIEFAKKNQQ
