SAPE_SARPE
ID SAPE_SARPE Reviewed; 94 AA.
AC P18313;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Sapecin;
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=3182837; DOI=10.1016/s0021-9258(18)37506-9;
RA Matsuyama K., Natori S.;
RT "Molecular cloning of cDNA for sapecin and unique expression of the sapecin
RT gene during the development of Sarcophaga peregrina.";
RL J. Biol. Chem. 263:17117-17121(1988).
RN [2]
RP PROTEIN SEQUENCE OF 55-94.
RX PubMed=3182836; DOI=10.1016/s0021-9258(18)37505-7;
RA Matsuyama K., Natori S.;
RT "Purification of three antibacterial proteins from the culture medium of
RT NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina.";
RL J. Biol. Chem. 263:17112-17116(1988).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=2358424; DOI=10.1093/oxfordjournals.jbchem.a123077;
RA Kuzuhara T., Nakajima Y., Matsuyama K., Natori S.;
RT "Determination of the disulfide array in sapecin, an antibacterial peptide
RT of Sarcophaga peregrina (flesh fly).";
RL J. Biochem. 107:514-518(1990).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=2401368; DOI=10.1016/0014-5793(90)81206-4;
RA Hanzawa H., Shimada I., Kuzuhara T., Komano H., Kohda D., Inagaki F.,
RA Natori S., Arata Y.;
RT "1H nuclear magnetic resonance study of the solution conformation of an
RT antibacterial protein, sapecin.";
RL FEBS Lett. 269:413-420(1990).
CC -!- FUNCTION: Sapecins, which are potent bactericidal proteins, are
CC produced in response to injury. Sapecin is cytotoxic to Gram-positive
CC bacteria, and to a lesser extent against Gram-negative 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; J04053; AAA29984.1; -; mRNA.
DR PIR; A31792; A31792.
DR PDB; 1L4V; NMR; -; A=55-94.
DR PDBsum; 1L4V; -.
DR AlphaFoldDB; P18313; -.
DR BMRB; P18313; -.
DR SMR; P18313; -.
DR TCDB; 1.C.47.1.3; the insect/fungal defensin (insect/fungal defensin) family.
DR EvolutionaryTrace; P18313; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:UniProt.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR017982; Defensin_insect.
DR InterPro; IPR001542; Defensin_invertebrate/fungal.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR Pfam; PF01097; Defensin_2; 1.
DR PRINTS; PR00271; DEFENSIN.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Defensin; Direct protein sequencing;
KW Disulfide bond; Immunity; Innate immunity; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..54
FT /evidence="ECO:0000269|PubMed:3182836"
FT /id="PRO_0000006756"
FT PEPTIDE 55..94
FT /note="Sapecin"
FT /id="PRO_0000006757"
FT DISULFID 57..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT ECO:0000269|PubMed:2358424"
FT DISULFID 70..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT ECO:0000269|PubMed:2358424"
FT DISULFID 74..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00710,
FT ECO:0000269|PubMed:2358424"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1L4V"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:1L4V"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1L4V"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:1L4V"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1L4V"
SQ SEQUENCE 94 AA; 9915 MW; 36170AB3073EC947 CRC64;
MKSFIVLAVT LCLAAFFMGQ SVASPAAAAE ESKFVDGLHA LKTIEPELHG RYKRATCDLL
SGTGINHSAC AAHCLLRGNR GGYCNGKAVC VCRN
