ID   SECP2_APIME             Reviewed;          77 AA.
AC   I1VC85;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Secapin-2 {ECO:0000303|PubMed:25017240};
DE   Flags: Precursor;
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:0000312|EMBL:AFI40557.1};
RN   [1] {ECO:0000312|EMBL:AFI40557.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hou C.S., Guo L.Q., Wang J.R., You L.F., Lin J.F., Wang C.S., Wu W.H.,
RA   Wang T.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 53-77, SYNTHESIS, FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, MASS SPECTROMETRY, AMIDATION AT PRO-77, AND DISULFIDE
RP   BOND.
RC   TISSUE=Venom {ECO:0000303|PubMed:25017240};
RX   PubMed=25017240; DOI=10.1016/j.peptides.2014.07.004;
RA   Mourelle D., Brigatte P., Bringanti L.D., De Souza B.M., Arcuri H.A.,
RA   Gomes P.C., Baptista-Saidemberg N.B., Ruggiero Neto J., Palma M.S.;
RT   "Hyperalgesic and edematogenic effects of Secapin-2, a peptide isolated
RT   from Africanized honeybee (Apis mellifera) venom.";
RL   Peptides 59:42-52(2014).
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). Induces hyperalgesia and edema mediated by leukotrienes
CC       when injected into mice (PubMed:25017240). Does not induce hemolytic
CC       activity, mast cell degranulation, or chemotactic activity for
CC       polymorphonucleated leukocytes (PMNL) (PubMed:25017240).
CC       {ECO:0000250|UniProtKB:A0A0K1YW63, ECO:0000269|PubMed:25017240}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25017240}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:25017240}.
CC   -!- MASS SPECTROMETRY: [Secapin-2]: Mass=2872.58; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:25017240};
CC   -!- SIMILARITY: Belongs to the secapin family. {ECO:0000305}.
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DR   EMBL; JQ900379; AFI40557.1; -; mRNA.
DR   AlphaFoldDB; I1VC85; -.
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:0044742; P:envenomation resulting in modulation of sensory perception of pain in another organism; IDA:UniProtKB.
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   Amidation; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Immunity; Innate immunity; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   PROPEP          33..52
FT                   /evidence="ECO:0000305|PubMed:25017240"
FT                   /id="PRO_0000453149"
FT   PEPTIDE         53..77
FT                   /note="Secapin-2"
FT                   /evidence="ECO:0000269|PubMed:25017240"
FT                   /id="PRO_5003653388"
FT   MOD_RES         77
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:25017240"
FT   DISULFID        61..72
FT                   /evidence="ECO:0000269|PubMed:25017240"
SQ   SEQUENCE   77 AA;  8763 MW;  DE0421ABD552B840 CRC64;
     MKNYSKNATY LITVLLFSFV TMLLIIPSKC EAVSNDMQPL EARTADLVQQ PRYIIDVPPR
     CPPGSKFVHK RCRVIVP