AFP_PENCH
ID AFP_PENCH Reviewed; 92 AA.
AC D0EXD3;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Antifungal protein {ECO:0000312|EMBL:ACX54052.1};
DE Flags: Precursor;
GN Name=afp {ECO:0000312|EMBL:ACX54052.1};
OS Penicillium chrysogenum (Penicillium notatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=5076;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACX54052.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-53; 57-69; 79-84
RP AND 88-92, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=RP42C {ECO:0000312|EMBL:ACX54052.1};
RX PubMed=19914321; DOI=10.1016/j.peptides.2009.11.002;
RA Rodriguez-Martin A., Acosta R., Liddell S., Nunez F., Benito M.J.,
RA Asensio M.A.;
RT "Characterization of the novel antifungal protein PgAFP and the encoding
RT gene of Penicillium chrysogenum.";
RL Peptides 31:541-547(2010).
RN [2] {ECO:0000305}
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=19683356; DOI=10.1016/j.ijfoodmicro.2009.07.020;
RA Acosta R., Rodriguez-Martin A., Martin A., Nunez F., Asensio M.A.;
RT "Selection of antifungal protein-producing molds from dry-cured meat
RT products.";
RL Int. J. Food Microbiol. 135:39-46(2009).
CC -!- FUNCTION: Strong antifungal activity against the molds P.commune Pc332,
CC P.echinulatum Pe321, and A.niger An261. {ECO:0000269|PubMed:19683356,
CC ECO:0000269|PubMed:19914321}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19914321}.
CC -!- MASS SPECTROMETRY: Mass=6494; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19914321};
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DR EMBL; GQ911150; ACX54052.1; -; Genomic_DNA.
DR PDB; 2NC2; NMR; -; A=37-92.
DR PDBsum; 2NC2; -.
DR AlphaFoldDB; D0EXD3; -.
DR BMRB; D0EXD3; -.
DR SMR; D0EXD3; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.60; -; 1.
DR InterPro; IPR023112; Antifungal-protein_dom_sf.
DR InterPro; IPR022706; Antifungal_prot.
DR Pfam; PF11402; Antifungal_prot; 1.
DR SUPFAM; SSF57598; SSF57598; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Fungicide; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..34
FT /evidence="ECO:0000269|PubMed:19914321"
FT /id="PRO_0000391701"
FT CHAIN 35..92
FT /note="Antifungal protein"
FT /evidence="ECO:0000269|PubMed:19914321"
FT /id="PRO_0000391702"
FT DISULFID 42..70
FT /evidence="ECO:0000250|UniProtKB:P17737"
FT DISULFID 49..77
FT /evidence="ECO:0000250|UniProtKB:P17737"
FT DISULFID 62..88
FT /evidence="ECO:0000250|UniProtKB:P17737"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2NC2"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2NC2"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2NC2"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2NC2"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2NC2"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2NC2"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:2NC2"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2NC2"
SQ SEQUENCE 92 AA; 10119 MW; 8F7DF4D5B4473E5A CRC64;
MQITSIAIVF FAAMGAVANP IARESDDLDA RDVQLSKFGG ECSLKHNTCT YLKGGKNHVV
NCGSAANKKC KSDRHHCEYD EHHKRVDCQT PV
