ID   SECP1_APIME             Reviewed;          25 AA.
AC   C0HLU0;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Secapin-1 {ECO:0000303|Ref.1};
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Apis.
OX   NCBI_TaxID=7460 {ECO:0000303|Ref.1};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SYNTHESIS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Venom {ECO:0000303|Ref.1};
RX   DOI=10.1016/j.cclet.2012.09.003;
RA   Meng Y., Yang X.X., Sheng Y.X., Zhang J.L., Yu D.Q.;
RT   "A novel peptide from Apis mellifera and solid-phase synthesis of its
RT   analogue.";
RL   Chin. Chem. Lett. 23:1161-1164(2012).
CC   -!- FUNCTION: Serine protease inhibitor which exhibits antifibrinolytic,
CC       antielastolytic and antimicrobial activities (By similarity). Displays
CC       antimicrobial activity against bacteria and fungi (By similarity).
CC       Likely functions in the innate immune response to microbial infection
CC       and possibly in the venom, as an antifibrinolytic agent (By
CC       similarity). {ECO:0000250|UniProtKB:A0A0K1YW63}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.1}.
CC   -!- MASS SPECTROMETRY: Mass=2821.56; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the secapin family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HLU0; -.
DR   Proteomes; UP000005203; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor 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; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR020128; Secapin.
DR   Pfam; PF17521; Secapin; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Immunity; Innate immunity; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor.
FT   PEPTIDE         1..25
FT                   /note="Secapin-1"
FT                   /id="PRO_0000453150"
FT   DISULFID        9..20
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   25 AA;  2825 MW;  1702F724314AE864 CRC64;
     YIINVPPRCP PGSKFVKNKC RVIVP