ACALA_ACALU
ID ACALA_ACALU Reviewed; 423 AA.
AC P81592; Q76K70;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Acaloleptin A;
DE Contains:
DE RecName: Full=Acaloleptin A1;
DE Contains:
DE RecName: Full=Acaloleptin A2;
DE Contains:
DE RecName: Full=Acaloleptin A3;
DE Contains:
DE RecName: Full=Acaloleptin A4;
DE Contains:
DE RecName: Full=Acidic peptide;
DE Contains:
DE RecName: Full=Acaloleptin A5;
DE Flags: Precursor;
OS Acalolepta luxuriosa (Udo longhorn beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Cerambycidae; Lamiinae; Monochamini; Acalolepta.
OX NCBI_TaxID=85306;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 355-367, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Fat body, and Hemolymph;
RX PubMed=19527748; DOI=10.1016/j.dci.2009.06.004;
RA Imamura M., Wada S., Ueda K., Saito A., Koizumi N., Iwahana H., Sato R.;
RT "Multipeptide precursor structure of acaloleptin A isoforms, antibacterial
RT peptides from the Udo longicorn beetle, Acalolepta luxuriosa.";
RL Dev. Comp. Immunol. 33:1120-1127(2009).
RN [2]
RP PROTEIN SEQUENCE OF 173-243, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Hemolymph;
RX PubMed=10077828;
RX DOI=10.1002/(sici)1520-6327(1999)40:2<88::aid-arch3>3.0.co;2-b;
RA Imamura M., Wada S., Koizumi N., Kadotani T., Yaoi K., Sato R., Iwahana H.;
RT "Acaloleptins A: inducible antibacterial peptides from larvae of the
RT beetle, Acalolepta luxuriosa.";
RL Arch. Insect Biochem. Physiol. 40:88-98(1999).
CC -!- FUNCTION: Acaloleptins A1-A4 show antibacterial activity against Gram-
CC negative bacteria but not against Gram-positive bacteria. Acaloleptin
CC A5 shows antibacterial activity against Gram-positive bacteria but not
CC against Gram-negative bacteria, and may also have antifungal activity.
CC {ECO:0000269|PubMed:10077828, ECO:0000269|PubMed:19527748}.
CC -!- SUBCELLULAR LOCATION: [Acaloleptin A1]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Acaloleptin A2]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Acaloleptin A3]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Acaloleptin A4]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Acaloleptin A5]: Secreted.
CC -!- TISSUE SPECIFICITY: Hemolymph (at protein level). Larval fat body.
CC {ECO:0000269|PubMed:10077828, ECO:0000269|PubMed:19527748}.
CC -!- INDUCTION: By bacterial infection. Expression detected 2 hours post-
CC injection, with expression increasing until 48 hours post-injection and
CC remaining considerably high at least until 72 hours post-injection.
CC {ECO:0000269|PubMed:10077828, ECO:0000269|PubMed:19527748}.
CC -!- SIMILARITY: Belongs to the coleoptericin family. {ECO:0000305}.
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DR EMBL; AB094343; BAC82199.1; -; mRNA.
DR AlphaFoldDB; P81592; -.
DR SMR; P81592; -.
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; IPR009382; Coleoptericin.
DR Pfam; PF06286; Coleoptericin; 5.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW Direct protein sequencing; Immunity; Innate immunity; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..26
FT /id="PRO_0000413422"
FT PEPTIDE 27..97
FT /note="Acaloleptin A1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000413423"
FT PEPTIDE 100..170
FT /note="Acaloleptin A2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000413424"
FT PEPTIDE 173..243
FT /note="Acaloleptin A3"
FT /id="PRO_0000413425"
FT PEPTIDE 246..316
FT /note="Acaloleptin A4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000413426"
FT PEPTIDE 319..350
FT /note="Acidic peptide"
FT /evidence="ECO:0000305"
FT /id="PRO_0000413427"
FT PEPTIDE 355..423
FT /note="Acaloleptin A5"
FT /id="PRO_0000413428"
FT REGION 28..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 205
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48403 MW; ACA98BB10989E92D CRC64;
MITKISLILF AVLLVSGLEE EERWKRSLQP GAPNVNNNDQ PWQVSPHISR DDSGNTKTDI
NVQRHGENND FEAGWSKVVR GPNKAKPTWH IGGTHRWRRS LQPGAPNINN KDQPWQVSPH
ISRDDNGNTR TNINVQRHGE NNDFEAGWSK VVRGPNKAKP TWHIGGTHRW RRSLQPGAPN
VNNKDQPWQV SPHISRDDSG NTRTNINVQR HGENNDFEAG WSKVVRGPNK AKPTWHIGGT
HRWRRSLQPG APNVNNKDQP WQVSPHISRD DSGNTNTDIN LQRHGENHDF DAGWSKVVRG
PNKAKPTWHV GGTYRWRRSV DIPHASTDNV DETFWEFDPH TEDDDDKPVL RLRRSDDEDE
EEEEDQPWQL NPNIARGDDG NTRADVNIKR RGENHDFEAG WSKVVDGPDR AKPTWHVGGT
FRW
