ID   AMP22_MACIN             Reviewed;         666 AA.
AC   Q9SPL4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Vicilin-like antimicrobial peptides 2-2;
DE   AltName: Full=MiAMP2;
DE   Contains:
DE     RecName: Full=Antimicrobial peptide 2a;
DE     AltName: Full=MiAMP2a;
DE   Contains:
DE     RecName: Full=Antimicrobial peptide 2b;
DE     AltName: Full=MiAMP2b;
DE   Contains:
DE     RecName: Full=Antimicrobial peptide 2c-1;
DE     AltName: Full=MiAMP2c-1;
DE   Contains:
DE     RecName: Full=Antimicrobial peptide 2c-2;
DE     AltName: Full=MiAMP2c-2;
DE   Contains:
DE     RecName: Full=Antimicrobial peptide 2c-3;
DE     AltName: Full=MiAMP2c-3;
DE   Contains:
DE     RecName: Full=Antimicrobial peptide 2d;
DE     AltName: Full=MiAMP2d;
DE   Flags: Precursor;
GN   Name=AMP2-2 {ECO:0000303|PubMed:10571855};
OS   Macadamia integrifolia (Macadamia nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Proteales; Proteaceae; Macadamia.
OX   NCBI_TaxID=60698;
RN   [1] {ECO:0000312|EMBL:AAD54245.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kernel {ECO:0000312|EMBL:AAD54245.1};
RX   PubMed=10571855; DOI=10.1046/j.1365-313x.1999.00569.x;
RA   Marcus J.P., Green J.L., Goulter K.C., Manners J.M.;
RT   "A family of antimicrobial peptides is produced by processing of a 7S
RT   globulin protein in Macadamia integrifolia kernels.";
RL   Plant J. 19:699-710(1999).
CC   -!- FUNCTION: Antimicrobial peptides 2b, 2c and 2d have antibacterial and
CC       antifungal activity against a range of species.
CC       {ECO:0000250|UniProtKB:Q9SPL3}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC       {ECO:0000255}.
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; AF161884; AAD54245.1; -; mRNA.
DR   AlphaFoldDB; Q9SPL4; -.
DR   SMR; Q9SPL4; -.
DR   PRIDE; Q9SPL4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; ISS:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   InterPro; IPR006792; Vicilin_N.
DR   Pfam; PF00190; Cupin_1; 2.
DR   Pfam; PF04702; Vicilin_N; 2.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; SSF51182; 2.
PE   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Fungicide; Plant defense; Secreted;
KW   Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..666
FT                   /note="Vicilin-like antimicrobial peptides 2-2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000250395"
FT   PEPTIDE         28..76
FT                   /note="Antimicrobial peptide 2a"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:10571855"
FT                   /id="PRO_0000250396"
FT   PEPTIDE         77..117
FT                   /note="Antimicrobial peptide 2b"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPL3"
FT                   /id="PRO_0000250397"
FT   PEPTIDE         118..184
FT                   /note="Antimicrobial peptide 2c-3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPL3"
FT                   /id="PRO_0000250398"
FT   PEPTIDE         118..164
FT                   /note="Antimicrobial peptide 2c-2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPL3"
FT                   /id="PRO_0000250399"
FT   PEPTIDE         118..162
FT                   /note="Antimicrobial peptide 2c-1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPL3"
FT                   /id="PRO_0000250400"
FT   PEPTIDE         186..220
FT                   /note="Antimicrobial peptide 2d"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPL3"
FT                   /id="PRO_0000250401"
FT   DOMAIN          271..410
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          455..625
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          161..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   666 AA;  78243 MW;  0ECA22F8710F8A7B CRC64;
     MAINTSNLCS LLFLLSLFLL STTVSLAESE FDRQEYEECK RQCMQLETSG QMRRCVSQCD
     KRFEEDIDWS KYDNQDDPQT DCQQCQRRCR QQESGPRQQQ YCQRRCKEIC EEEEEYNRQR
     DPQQQYEQCQ ERCQRHETEP RHMQTCQQRC ERRYEKEKRK QQKRYEEQQR EDEEKYEERM
     KEEDNKRDPQ QREYEDCRRR CEQQEPRQQY QCQRRCREQQ RQHGRGGDLI NPQRGGSGRY
     EEGEEKQSDN PYYFDERSLS TRFRTEEGHI SVLENFYGRS KLLRALKNYR LVLLEANPNA
     FVLPTHLDAD AILLVTGGRG ALKMIHRDNR ESYNLECGDV IRIPAGTTFY LINRDNNERL
     HIAKFLQTIS TPGQYKEFFP AGGQNPEPYL STFSKEILEA ALNTQAERLR GVLGQQREGV
     IISASQEQIR ELTRDDSESR RWHIRRGGES SRGPYNLFNK RPLYSNKYGQ AYEVKPEDYR
     QLQDMDVSVF IANITQGSMM GPFFNTRSTK VVVVASGEAD VEMACPHLSG RHGGRRGGKR
     HEEEEDVHYE QVKARLSKRE AIVVPVGHPV VFVSSGNENL LLFAFGINAQ NNHENFLAGR
     ERNVLQQIEP QAMELAFAAP RKEVEELFNS QDESIFFPGP RQHQQQSSRS TKQQQPLVSI
     LDFVGF