XPP3_DICDI
ID XPP3_DICDI Reviewed; 518 AA.
AC Q54T46;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Xaa-Pro aminopeptidase 3 {ECO:0000250|UniProtKB:Q9NQH7};
DE Short=X-Pro aminopeptidase 3;
DE EC=3.4.11.9;
DE AltName: Full=Aminopeptidase P3;
DE Short=APP3;
DE Flags: Precursor;
GN Name=xpnpep3; ORFNames=DDB_G0282075;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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).
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity
CC towards peptides with Ala or Ser at the P1 position.
CC {ECO:0000250|UniProtKB:Q9NQH7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9; Evidence={ECO:0000250|UniProtKB:Q9NQH7};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NQH7};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q9NQH7};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NQH7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9NQH7}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9NQH7}. Note=Mainly mitochondrial.
CC {ECO:0000250|UniProtKB:Q9NQH7}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; AAFI02000044; EAL66459.1; -; Genomic_DNA.
DR RefSeq; XP_640405.1; XM_635313.1.
DR AlphaFoldDB; Q54T46; -.
DR SMR; Q54T46; -.
DR STRING; 44689.DDB0304432; -.
DR PaxDb; Q54T46; -.
DR EnsemblProtists; EAL66459; EAL66459; DDB_G0282075.
DR GeneID; 8623360; -.
DR KEGG; ddi:DDB_G0282075; -.
DR dictyBase; DDB_G0282075; xpnpep3.
DR eggNOG; KOG2414; Eukaryota.
DR HOGENOM; CLU_017266_1_1_1; -.
DR InParanoid; Q54T46; -.
DR OMA; GWADTEL; -.
DR PhylomeDB; Q54T46; -.
DR PRO; PR:Q54T46; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; 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; IEA:UniProtKB-KW.
DR Gene3D; 3.40.350.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR007865; Aminopep_P_N.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR Pfam; PF05195; AMP_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SMART; SM01011; AMP_N; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Metalloprotease; Mitochondrion; Protease; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..48
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 49..518
FT /note="Xaa-Pro aminopeptidase 3"
FT /id="PRO_0000331199"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 434
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 434
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 461
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 485
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 485
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
FT BINDING 485
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQH7"
SQ SEQUENCE 518 AA; 58869 MW; 980F47FAAC175E9B CRC64;
MNNICKLNKF IISKSSSSLS STSSKIKTNC LIKNAKMFSS SLNLNRFYST NNTNNNKLKK
PLSIGQATFE THPYLLDKNE ITKGIKMKEF KDRREKLMKN FPIGSVVVIF TPPEPMMSYD
IPWSFRQNTN FNYLTGFNEP EAVLVLVKTS ELDHQSYLFV RERNEEKEKW DGARCGGENV
KKYFGIDFGY NLTNRDIPIL GKLLKSTTDG KLYCNTTPWN QLSNKLEPFL ENIKFYTVES
LLQQIRLIKS DAEIKMMLKS GEIAGTSFHE TMKYTGTKSS SSSSSSSSSP LNEYQVSAYF
EWCVKDKGAQ RMSYPPVVAG GDNGHTLHYI QNNQLLNYCD LLLMDAGCEY WGYTSDITRT
FPVSGKFTEA QSEVYQAVLD VNKKCIELCK PGETINSIHL KSVELIQAHL KRLGIINESN
PNDYRLYYPH SIGHYLGMDT HDTLDFDYGV TLEPGMIITI EPGIYISKYD SNVPEKYRGI
SIRVEDDVVI PNLNNSPLVL THLAPKEISE IESIMSNK
