ID   SAPB_SARPE              Reviewed;          88 AA.
AC   P31529;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Sapecin-B;
DE   Flags: Precursor;
OS   Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Sarcophagidae; Sarcophaga; Boettcherisca.
OX   NCBI_TaxID=7386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7635204; DOI=10.1016/0014-5793(95)00717-n;
RA   Lee S.-R., Kurata S., Natori S.;
RT   "Molecular cloning of cDNA for sapecin B, an antibacterial protein of
RT   Sarcophaga, and its detection in larval brain.";
RL   FEBS Lett. 368:485-487(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 55-88, AND DISULFIDE BONDS.
RX   PubMed=8471044; DOI=10.1042/bj2910275;
RA   Yamada K., Natori S.;
RT   "Purification, sequence and antibacterial activity of two novel sapecin
RT   homologues from Sarcophaga embryonic cells: similarity of sapecin B to
RT   charybdotoxin.";
RL   Biochem. J. 291:275-279(1993).
CC   -!- FUNCTION: Sapecins, which are potent bactericidal proteins, are
CC       produced in response to injury. Sapecin B is cytotoxic to Gram-positive
CC       bacteria.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemocytes and fat body.
CC   -!- INDUCTION: By injury to the larval cell wall.
CC   -!- SIMILARITY: Belongs to the invertebrate defensin family. Type 1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00710}.
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DR   EMBL; S80571; AAB35004.1; -; mRNA.
DR   PIR; S66287; S66287.
DR   AlphaFoldDB; P31529; -.
DR   SMR; P31529; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR001542; Defensin_invertebrate/fungal.
DR   Pfam; PF01097; Defensin_2; 1.
DR   PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW   Direct protein sequencing; Disulfide bond; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..54
FT                   /evidence="ECO:0000269|PubMed:8471044"
FT                   /id="PRO_0000006758"
FT   PEPTIDE         55..88
FT                   /note="Sapecin-B"
FT                   /id="PRO_0000006759"
FT   DISULFID        57..78
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:8471044"
FT   DISULFID        64..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:8471044"
FT   DISULFID        68..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT                   ECO:0000269|PubMed:8471044"
SQ   SEQUENCE   88 AA;  10041 MW;  9459A0AF3B0EDE3D CRC64;
     MKFLTSLLLL FVVVMVSAVN LSMAKESANQ LTERLQELDG AAIQEPAELN RHKRLTCEID
     RSLCLLHCRL KGYLRAYCSQ QKVCRCVQ