SECP_APICE
ID SECP_APICE Reviewed; 115 AA.
AC A0A0K1YW63;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Secapin {ECO:0000303|PubMed:27208884};
DE AltName: Full=AcSecapin-1 {ECO:0000303|PubMed:27208884};
DE Flags: Precursor;
OS Apis cerana (Indian honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7461 {ECO:0000312|EMBL:AKZ17655.1};
RN [1] {ECO:0000312|EMBL:AKZ17655.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=27208884; DOI=10.1016/j.dci.2016.05.011;
RA Lee K.S., Kim B.Y., Yoon H.J., Choi Y.S., Jin B.R.;
RT "Secapin, a bee venom peptide, exhibits anti-fibrinolytic, anti-
RT elastolytic, and anti-microbial activities.";
RL Dev. Comp. Immunol. 63:27-35(2016).
RN [2] {ECO:0000305}
RP SYNTHESIS, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1016/j.aspen.2016.12.009;
RA Kim B.Y., Lee K.S., Ok M., Jin B.R.;
RT "Synthetic secapin bee venom peptide exerts an anti-microbial effect but
RT not a cytotoxic or inflammatory response.";
RL J. Asia-Pac. Entomol. 20:151-155(2017).
CC -!- FUNCTION: Serine protease inhibitor which exhibits antifibrinolytic,
CC antielastolytic and antimicrobial activities (PubMed:27208884).
CC Displays antimicrobial activity against bacteria and fungi
CC (PubMed:27208884). Likely functions in the innate immune response to
CC microbial infection and possibly in the venom, as an antifibrinolytic
CC agent (PubMed:27208884). The recombinant form inhibits trypsin
CC (IC(50)=80.02 nM, Ki=127.25 nM), chymotrypsin (IC(50)=393.78 nM,
CC Ki=432.59 nM), the microbial serine proteases subtilisin A
CC (IC(50)=379.20 nM, Ki=492.77 nM) and proteinase K (IC(50)=189.43 nM,
CC Ki=271.76 nM), plasmin (IC(50)=457.98 nM, Ki=502.91 nM), human elastase
CC (IC(50)=347.81 nM, Ki=469.90 nM) and porcine elastase (IC(50)=94.70 nM,
CC Ki=125.62 nM) (PubMed:27208884). Does not inhibit thrombin
CC (PubMed:27208884). Binds to human plasmin and inhibits the plasmin-
CC mediated degradation of fibrin to fibrin degradation products
CC (PubMed:27208884). Also binds to bacterial and fungal surfaces and
CC exhibits antimicrobial activity against the Gram-positive bacteria
CC B.thuringiensis (MIC=4.21 uM) and P.larvae (MIC=11.13 uM), the Gram-
CC negative bacterium E.coli (MIC=6.50 uM), and the fungus B.bassiana
CC (IC(50)=2.57 uM) (PubMed:27208884). The synthetic peptide also exhibits
CC antimicrobial activity against the Gram-positive bacterium P.larvae
CC (MIC=41.12 uM), the Gram-negative bacterium P.aeruginosa (MIC=65.75
CC uM), and the fungus B.bassiana (IC(50)=44.27 uM) (Ref.2). In vitro it
CC does not induce an inflammatory response and has no cytotoxic activity
CC against mouse embryo cells (Ref.2). {ECO:0000269|PubMed:27208884,
CC ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Antibacterial activity against P.aeruginosa is retained between 25
CC and 90 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:27208884}.
CC -!- TISSUE SPECIFICITY: Expressed in the epidermis, fat body and venom
CC gland. {ECO:0000269|PubMed:27208884}.
CC -!- INDUCTION: Up-regulated in the fat body after injection with bacteria
CC (B.thuringiensis, P.larvae or E.coli) or the fungus B.bassiana.
CC {ECO:0000269|PubMed:27208884}.
CC -!- SIMILARITY: Belongs to the secapin family. {ECO:0000305}.
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DR EMBL; KR732613; AKZ17655.1; -; mRNA.
DR RefSeq; XP_016905691.1; XM_017050202.1.
DR RefSeq; XP_016905692.1; XM_017050203.1.
DR RefSeq; XP_016905693.1; XM_017050204.1.
DR RefSeq; XP_016905694.1; XM_017050205.1.
DR RefSeq; XP_016905696.1; XM_017050207.1.
DR AlphaFoldDB; A0A0K1YW63; -.
DR SMR; A0A0K1YW63; -.
DR GeneID; 107993666; -.
DR KEGG; acer:107993666; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0140367; P:antibacterial innate immune response; IDA:UniProtKB.
DR GO; GO:0061760; P:antifungal innate immune response; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0035899; P:negative regulation of blood coagulation in another organism; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR InterPro; IPR020128; Secapin.
DR Pfam; PF17521; Secapin; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Disulfide bond; Fungicide; Immunity;
KW Innate immunity; Protease inhibitor; Secreted; Serine protease inhibitor;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..90
FT /evidence="ECO:0000305"
FT /id="PRO_0000453147"
FT PEPTIDE 91..115
FT /note="Secapin"
FT /evidence="ECO:0000250|UniProtKB:P02852"
FT /id="PRO_0000453148"
FT DISULFID 99..110
FT /evidence="ECO:0000250|UniProtKB:P02852"
SQ SEQUENCE 115 AA; 13570 MW; 94B7171E22A0CA7B CRC64;
MRFQVYILHL CFFILVVLTY LSQGQSYTTT TTTSTTEQPT FLQKIHETFK KVKENAKIHN
LYIFDPPTWI YTTTTEKPVE STENFDITNR QLITVPVRCP PNYDFIKGRC REKIP
