ID   CAPA_CAMFO              Reviewed;         181 AA.
AC   E2AYH6;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 2.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=CAPA peptides {ECO:0000303|PubMed:25641051};
DE   Contains:
DE     RecName: Full=Periviscerokinin 1 {ECO:0000303|PubMed:25641051};
DE   Contains:
DE     RecName: Full=Periviscerokinin 2 {ECO:0000303|PubMed:25641051};
DE   Flags: Precursor;
GN   ORFNames=EAG_11747 {ECO:0000312|EMBL:EFN61511.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 32-41 AND 56-65, TISSUE SPECIFICITY, MASS SPECTROMETRY,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT ILE-41 AND ILE-65.
RX   PubMed=25641051; DOI=10.1021/pr5011636;
RA   Schmitt F., Vanselow J.T., Schlosser A., Kahnt J., Roessler W., Wegener C.;
RT   "Neuropeptidomics of the carpenter ant Camponotus floridanus.";
RL   J. Proteome Res. 14:1504-1514(2015).
CC   -!- FUNCTION: Periviscerokinins mediate visceral muscle contractile
CC       activity (myotropic activity). {ECO:0000250|UniProtKB:P83923}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25641051}.
CC   -!- TISSUE SPECIFICITY: Periviscerokinin 1 and 2 are expressed in central
CC       brain, antennal lobes and gnathal, thoracic and abominal ganglia.
CC       Periviscerokinin 2 is also expressed in the retrocerebral complex (at
CC       protein level). {ECO:0000269|PubMed:25641051}.
CC   -!- PTM: A pyrokinin potentially constituted by residues Asn-158 to Gly-170
CC       has so far not been detected and might be completely absent in ants.
CC       {ECO:0000305|PubMed:25641051}.
CC   -!- MASS SPECTROMETRY: [Periviscerokinin 1]: Mass=1071.63; Method=MALDI;
CC       Note=Periviscerokinin 1.; Evidence={ECO:0000269|PubMed:25641051};
CC   -!- MASS SPECTROMETRY: [Periviscerokinin 2]: Mass=1116.70; Method=MALDI;
CC       Note=Periviscerokinin 2.; Evidence={ECO:0000269|PubMed:25641051};
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DR   EMBL; GL443910; EFN61511.1; -; Genomic_DNA.
DR   RefSeq; XP_011266256.1; XM_011267954.2.
DR   AlphaFoldDB; E2AYH6; -.
DR   GeneID; 105257373; -.
DR   KEGG; cfo:105257373; -.
DR   InParanoid; E2AYH6; -.
DR   OrthoDB; 1475080at2759; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Neuropeptide; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..29
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT                   /id="PRO_0000434198"
FT   PEPTIDE         32..41
FT                   /note="Periviscerokinin 1"
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT                   /id="PRO_0000434199"
FT   PROPEP          44..54
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT                   /id="PRO_0000434200"
FT   PEPTIDE         56..65
FT                   /note="Periviscerokinin 2"
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT                   /id="PRO_0000434201"
FT   PROPEP          68..181
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT                   /id="PRO_0000434202"
FT   REGION          159..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         41
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT   MOD_RES         65
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:25641051"
SQ   SEQUENCE   181 AA;  20956 MW;  10DBA043A5009BD3 CRC64;
     MQDNRFFILM ILLVFSTSLN QGQKLKANDR RSAGLVPYPR IGRNSEISSF SRSERALGLI
     HQPRIGRSDV SSFDNLNRFH DLSSDADIEF YAMDMDPLLS PDYEDYASKP IALKYADKLQ
     KDNSWLMPDH IHGYKDFHFA QKINDPRLYY SILRDSRNTQ GQGGYTPRLG RENERDTANF
     L