AMP23_MACIN
ID AMP23_MACIN Reviewed; 625 AA.
AC Q9SPL3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Vicilin-like antimicrobial peptides 2-3;
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; Fragment;
GN Name=AMP2-3 {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:0000305, ECO:0000312|EMBL:AAD54246.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-41; 77-82 AND 145-149,
RP FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Kernel {ECO:0000312|EMBL:AAD54246.1};
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:0000269|PubMed:10571855}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10571855}.
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 2b]: Mass=5139;
CC Method=Unknown; Evidence={ECO:0000269|PubMed:10571855};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 2c-1]: Mass=5931;
CC Method=Unknown; Evidence={ECO:0000269|PubMed:10571855};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 2c-2]: Mass=6216;
CC Method=Unknown; Evidence={ECO:0000269|PubMed:10571855};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 2c-3]: Mass=8818;
CC Method=Unknown; Evidence={ECO:0000269|PubMed:10571855};
CC -!- MASS SPECTROMETRY: [Antimicrobial peptide 2d]: Mass=4576;
CC Method=Unknown; Evidence={ECO:0000269|PubMed:10571855};
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000255}.
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DR EMBL; AF161885; AAD54246.1; -; mRNA.
DR AlphaFoldDB; Q9SPL3; -.
DR SMR; Q9SPL3; -.
DR PRIDE; Q9SPL3; -.
DR GO; GO:0043245; C:extraorganismal space; NAS:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; NAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; 2.60.120.10; -; 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 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Direct protein sequencing; Fungicide;
KW Plant defense; Secreted; Seed storage protein; Storage protein.
FT CHAIN <1..625
FT /note="Vicilin-like antimicrobial peptides 2-3"
FT /id="PRO_0000250402"
FT PEPTIDE <1..35
FT /note="Antimicrobial peptide 2a"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10571855"
FT /id="PRO_0000250403"
FT PEPTIDE 36..76
FT /note="Antimicrobial peptide 2b"
FT /evidence="ECO:0000269|PubMed:10571855"
FT /id="PRO_0000250404"
FT PEPTIDE 77..143
FT /note="Antimicrobial peptide 2c-3"
FT /evidence="ECO:0000269|PubMed:10571855"
FT /id="PRO_0000250405"
FT PEPTIDE 77..123
FT /note="Antimicrobial peptide 2c-2"
FT /evidence="ECO:0000269|PubMed:10571855"
FT /id="PRO_0000250406"
FT PEPTIDE 77..121
FT /note="Antimicrobial peptide 2c-1"
FT /evidence="ECO:0000269|PubMed:10571855"
FT /id="PRO_0000250407"
FT PEPTIDE 145..179
FT /note="Antimicrobial peptide 2d"
FT /evidence="ECO:0000269|PubMed:10571855"
FT /id="PRO_0000250408"
FT DOMAIN 230..369
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 414..584
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 120..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAD54246.1"
SQ SEQUENCE 625 AA; 73587 MW; 415808A89D370296 CRC64;
QCMQLETSGQ MRRCVSQCDK RFEEDIDWSK YDNQEDPQTE CQQCQRRCRQ QESDPRQQQY
CQRRCKEICE EEEEYNRQRD PQQQYEQCQK RCQRRETEPR HMQICQQRCE RRYEKEKRKQ
QKRYEEQQRE DEEKYEERMK EGDNKRDPQQ REYEDCRRHC EQQEPRLQYQ CQRRCQEQQR
QHGRGGDLMN PQRGGSGRYE EGEEKQSDNP YYFDERSLST RFRTEEGHIS VLENFYGRSK
LLRALKNYRL VLLEANPNAF VLPTHLDADA ILLVIGGRGA LKMIHRDNRE SYNLECGDVI
RIPAGTTFYL INRDNNERLH IAKFLQTIST PGQYKEFFPA GGQNPEPYLS TFSKEILEAA
LNTQTERLRG VLGQQREGVI IRASQEQIRE LTRDDSESRR WHIRRGGESS RGPYNLFNKR
PLYSNKYGQA YEVKPEDYRQ LQDMDVSVFI ANITQGSMMG PFFNTRSTKV VVVASGEADV
EMACPHLSGR HGGRGGGKRH EEEEEVHYEQ VRARLSKREA IVVLAGHPVV FVSSGNENLL
LFAFGINAQN NHENFLAGRE RNVLQQIEPQ AMELAFAASR KEVEELFNSQ DESIFFPGPR
QHQQQSPRST KQQQPLVSIL DFVGF
