ALL6_APICE
ID ALL6_APICE Reviewed; 87 AA.
AC A0A2R4SV19;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 25-MAY-2022, entry version 10.
DE RecName: Full=Venom serine protease inhibitor {ECO:0000303|PubMed:28917645};
DE Short=AcVSPI {ECO:0000303|PubMed:28917645};
DE Short=VSPI {ECO:0000312|EMBL:AVZ66243.1, ECO:0000312|EMBL:AVZ66244.1};
DE AltName: Full=Allergen Api m 6-like peptide {ECO:0000303|PubMed:28917645};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=28917645; DOI=10.1016/j.cbpc.2017.09.001;
RA Yang J., Lee K.S., Kim B.Y., Choi Y.S., Yoon H.J., Jia J., Jin B.R.;
RT "Anti-fibrinolytic and anti-microbial activities of a serine protease
RT inhibitor from honeybee (Apis cerana) venom.";
RL Comp. Biochem. Physiol. 201:11-18(2017).
CC -!- FUNCTION: Antifibrinolytic and antimicrobial serine protease inhibitor.
CC Inhibits trypsin, plasmin and microbial serine proteases but not
CC chymotrypsin, thrombin and elastase. Inhibits the plasmin-mediated
CC degradation of fibrin to fibrin degradation products. Also binds to
CC bacterial and fungal surfaces and exhibits antimicrobial activity
CC against fungi as well as Gram-positive and Gram-negative bacteria.
CC {ECO:0000269|PubMed:28917645}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28917645}.
CC -!- TISSUE SPECIFICITY: Specifically expressed by the venom gland.
CC {ECO:0000269|PubMed:28917645}.
CC -!- SIMILARITY: Belongs to the serine protease inhibitor-like (TIL domain-
CC containing) family. {ECO:0000305}.
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DR EMBL; MF281990; AVZ66243.1; -; mRNA.
DR EMBL; MF281991; AVZ66244.1; -; Genomic_DNA.
DR RefSeq; XP_016915259.1; XM_017059770.1.
DR AlphaFoldDB; A0A2R4SV19; -.
DR SMR; A0A2R4SV19; -.
DR GeneID; 107999756; -.
DR KEGG; acer:107999756; -.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR Pfam; PF01826; TIL; 1.
DR SUPFAM; SSF57567; SSF57567; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Disulfide bond; Fungicide; Protease inhibitor;
KW Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..87
FT /note="Venom serine protease inhibitor"
FT /evidence="ECO:0000305|PubMed:28917645"
FT /id="PRO_5015284604"
FT DOMAIN 27..81
FT /note="TIL"
FT /evidence="ECO:0000255"
FT SITE 55..56
FT /note="Reactive bond"
FT /evidence="ECO:0000305|PubMed:28917645"
FT DISULFID 27..61
FT /evidence="ECO:0000250|UniProtKB:P07851"
FT DISULFID 36..57
FT /evidence="ECO:0000250|UniProtKB:P07851"
FT DISULFID 40..53
FT /evidence="ECO:0000250|UniProtKB:P07851"
FT DISULFID 44..81
FT /evidence="ECO:0000250|UniProtKB:P07851"
FT DISULFID 63..75
FT /evidence="ECO:0000250|UniProtKB:P07851"
SQ SEQUENCE 87 AA; 9733 MW; 58FC72741D1CAE31 CRC64;
MPRLVLVSFL FLAIFSVFIG GFAKSKCPRN EIFTRCHAAC QPSCARLARK PFCIKICKPG
CICTSGYLRN KNNVCVPRSR CFSGRLL
