IAA1_STIHL
ID IAA1_STIHL Reviewed; 44 AA.
AC A0A0X1KGZ5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Alpha-amylase inhibitor helianthamide {ECO:0000303|PubMed:27066537};
OS Stichodactyla helianthus (Sun anemone) (Stoichactis helianthus).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Stichodactylidae; Stichodactyla.
OX NCBI_TaxID=6123;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, DISULFIDE BONDS, RECOMBINANT EXPRESSION, AND
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH PORCINE PANCREATIC
RP ALPHA-AMYLASE.
RX PubMed=27066537; DOI=10.1021/acscentsci.5b00399;
RA Tysoe C., Williams L.K., Keyzers R., Nguyen N.T., Tarling C., Wicki J.,
RA Goddard-Borger E.D., Aguda A.H., Perry S., Foster L.J., Andersen R.J.,
RA Brayer G.D., Withers S.G.;
RT "Potent human alpha-amylase inhibition by the beta-defensin-like protein
RT helianthamide.";
RL ACS Cent. Sci. 2:154-161(2016).
CC -!- FUNCTION: Specific pancreatic alpha-amylase (AMY2A) inhibitor. The
CC recombinant peptide inhibits human pancreatic (Ki=0.01 nM) and porcine
CC pancreatic alpha-amylases (Ki=0.1 nM). {ECO:0000269|PubMed:27066537}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:C0HK71}.
CC -!- DOMAIN: Is structurally homologous to beta-defensins.
CC {ECO:0000305|PubMed:27066537}.
CC -!- PHARMACEUTICAL: Potential drug candidate for the treatment of the type
CC 2 diabetes mellitus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sea anemone alpha-amylase inhibitor family.
CC {ECO:0000305}.
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DR PDB; 4X0N; X-ray; 2.60 A; B=1-44.
DR PDBsum; 4X0N; -.
DR SMR; A0A0X1KGZ5; -.
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 3D-structure; Alpha-amylase inhibitor; Direct protein sequencing;
KW Disulfide bond; Pharmaceutical; Secreted.
FT CHAIN 1..44
FT /note="Alpha-amylase inhibitor helianthamide"
FT /evidence="ECO:0000269|PubMed:27066537"
FT /id="PRO_0000454102"
FT REGION 7..10
FT /note="Inhibitory motif"
FT /evidence="ECO:0000269|PubMed:27066537"
FT DISULFID 6..38
FT /evidence="ECO:0000269|PubMed:27066537,
FT ECO:0007744|PDB:4X0N"
FT DISULFID 16..33
FT /evidence="ECO:0000269|PubMed:27066537,
FT ECO:0007744|PDB:4X0N"
FT DISULFID 20..39
FT /evidence="ECO:0000269|PubMed:27066537,
FT ECO:0007744|PDB:4X0N"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:4X0N"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:4X0N"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4X0N"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:4X0N"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:4X0N"
SQ SEQUENCE 44 AA; 4690 MW; 47530BD01034114E CRC64;
ESGNSCYIYH GVSGICKASC AEDEKAMAGM GVCEGHLCCY KTPW