ID AMPP1_COPC7 Reviewed; 622 AA.
AC A8P5H7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Probable Xaa-Pro aminopeptidase P;
DE Short=AMPP;
DE Short=Aminopeptidase P;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Prolidase;
GN Name=AMPP; ORFNames=CC1G_05499;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC the N-termini of peptides. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACS02000011; EAU82877.1; -; Genomic_DNA.
DR RefSeq; XP_001838946.1; XM_001838894.1.
DR AlphaFoldDB; A8P5H7; -.
DR SMR; A8P5H7; -.
DR STRING; 240176.A8P5H7; -.
DR GeneID; 6015541; -.
DR KEGG; cci:CC1G_05499; -.
DR VEuPathDB; FungiDB:CC1G_05499; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_3_1; -.
DR InParanoid; A8P5H7; -.
DR OMA; EPGMILS; -.
DR OrthoDB; 869at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR PANTHER; PTHR43763:SF21; X-PRO AMINOPEPTIDASE; 1.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 2.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW Protease; Reference proteome.
FT CHAIN 1..622
FT /note="Probable Xaa-Pro aminopeptidase P"
FT /id="PRO_0000411790"
FT BINDING 419
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 528
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 542
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 622 AA; 69966 MW; E7CEEBBB4A1D7B67 CRC64;
MGARGNHTVD TSKQLAALRE LMKKENVDVW VVPSEDQHYS EYLAHCDERR AFISGFNGSA
GCAVITLDKA YLFTDGRYFL QAEKQLDSNW TLMKQGLPDV PTWQDFLHKT LDGSLKIGID
ATIITEEDAA GLRKNLAPKK SELVPSKKNL VDIVWGSERP ARPQNPVFHL DEKYSGQSFK
EKVKKVREEI AKEKGKAFVV TMLDEVAWLF NLRGSDIDYN PVFFAYAVVT PDEVVLFINE
KQLDDAARDY LGQDVKIRGY DELYDYLKEL PKSLSLTGDK DGEKILVTSR TSLAITETIT
PPSSPESTTF HKVVRSPVGD LKAIKNAVEI EGFRQCHIRD GAALARYFAW LEEALNEGKE
VSEYAGAEVL EKYRSELDLF RGLSFTTISS TGPNGAIIHY SPDPQDCAII KKDQVYLCDS
GAQFSDGTTD VTRTWHFGTP RPEEVRAFTR VLQGHIAIDT AVFPNGTTGY LIDSWARRSL
WQDGLDYRHG TGHGVGHFLN VHEGPQGIGV RIAYNNTALK AGMTVSNEPG YYEDGQYGIR
IENIVIVKEV KLPNNFGDKG YLGFEHVTMC PIQTKLIDAS LLTEPEKKWV NDYHQEVWQK
VSPLLQNDKR ALEWLKRETT PI
//
