ID   IAA1_HETMG              Reviewed;          44 AA.
AC   C0HK71;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Alpha-amylase inhibitor magnificamide {ECO:0000303|PubMed:29191747};
OS   Heteractis magnifica (Magnificent sea anemone) (Radianthus magnifica).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Stichodactylidae; Heteractis.
OX   NCBI_TaxID=38281;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=29191747; DOI=10.1016/j.jprot.2017.11.019;
RA   Sintsova O., Gladkikh I., Chausova V., Monastyrnaya M., Anastyuk S.,
RA   Chernikov O., Yurchenko E., Aminin D., Isaeva M., Leychenko E.,
RA   Kozlovskaya E.;
RT   "Peptide fingerprinting of the sea anemone Heteractis magnifica mucus
RT   revealed neurotoxins, Kunitz-type proteinase inhibitors and a new beta-
RT   defensin alpha-amylase inhibitor.";
RL   J. Proteomics 173:12-21(2018).
RN   [2]
RP   FUNCTION, 3D-STRUCTURE MODELING, AND RECOMBINANT EXPRESSION.
RX   PubMed=31546678; DOI=10.3390/md17100542;
RA   Sintsova O., Gladkikh I., Kalinovskii A., Zelepuga E., Monastyrnaya M.,
RA   Kim N., Shevchenko L., Peigneur S., Tytgat J., Kozlovskaya E.,
RA   Leychenko E.;
RT   "Magnificamide, a beta-defensin-like peptide from the mucus of the sea
RT   anemone Heteractis magnifica, is a strong inhibitor of mammalian alpha-
RT   amylases.";
RL   Mar. Drugs 17:0-0(2019).
CC   -!- FUNCTION: Mammalian alpha-amylase (AMY2A) inhibitor (PubMed:29191747,
CC       PubMed:31546678). The recombinant peptide inhibits porcine pancreatic
CC       (Ki=0.17 nM) and human saliva alpha-amylases (Ki=7.7 nM)
CC       (PubMed:31546678). It does not show antimicrobial (tested on fungi and
CC       bacteria) or channel modulating activities (tested on 18 voltage-gated
CC       sodium and potassium channles) (PubMed:31546678).
CC       {ECO:0000269|PubMed:29191747, ECO:0000269|PubMed:31546678}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29191747}.
CC   -!- DOMAIN: Is structurally homologous to beta-defensins. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=4770; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29191747};
CC   -!- PHARMACEUTICAL: Potential drug candidate for the treatment of the type
CC       2 diabetes mellitus. {ECO:0000305|PubMed:31546678}.
CC   -!- SIMILARITY: Belongs to the sea anemone alpha-amylase inhibitor family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HK71; -.
DR   SMR; C0HK71; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015066; F:alpha-amylase inhibitor activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alpha-amylase inhibitor; Direct protein sequencing; Disulfide bond;
KW   Pharmaceutical; Secreted.
FT   PEPTIDE         1..44
FT                   /note="Alpha-amylase inhibitor magnificamide"
FT                   /evidence="ECO:0000269|PubMed:29191747"
FT                   /id="PRO_0000443115"
FT   REGION          7..10
FT                   /note="Inhibitory motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0X1KGZ5"
FT   DISULFID        6..38
FT                   /evidence="ECO:0000250|UniProtKB:A0A0X1KGZ5"
FT   DISULFID        16..33
FT                   /evidence="ECO:0000250|UniProtKB:A0A0X1KGZ5"
FT   DISULFID        20..39
FT                   /evidence="ECO:0000250|UniProtKB:A0A0X1KGZ5"
SQ   SEQUENCE   44 AA;  4775 MW;  BBAA8B7B220EBF44 CRC64;
     SEGTSCYIYH GVYGICKAKC AEDMKAMAGM GVCEGDLCCY KTPW