ALLSA_CAMFO
ID ALLSA_CAMFO Reviewed; 193 AA.
AC E2ADX8;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Allatostatin A {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Allatostatin A1 {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Allatostatin A2 {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Allatostatin A3 {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Allatostatin A4 {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Allatostatin A5 {ECO:0000303|PubMed:25641051};
DE Flags: Precursor;
GN ORFNames=EAG_13122 {ECO:0000312|EMBL:EFN68211.1};
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] {ECO:0000312|EMBL:DAA35076.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=22448224; DOI=10.1371/journal.pone.0032559;
RA Gruber C.W., Muttenthaler M.;
RT "Discovery of defense- and neuropeptides in social ants by genome-mining.";
RL PLoS ONE 7:E32559-E32559(2012).
RN [2]
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 [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 67-74; 87-94; 98-105; 142-150 AND 154-165, TISSUE
RP SPECIFICITY, AMIDATION AT ILE-74; ILE-94; ILE-105; ILE-150 AND SER-165,
RP MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
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: May act as a neurotransmitter or neuromodulator.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25641051}.
CC -!- TISSUE SPECIFICITY: Allatostatins A1, A2 and A3 are expressed in brain,
CC antennal lobes, optical lobes, gnathal ganglia, the retrocerebral
CC complex and thoracic, abdominal and ventral ganglia. Allatostain A4 is
CC expressed in brain (at protein level). {ECO:0000269|PubMed:25641051}.
CC -!- MASS SPECTROMETRY: [Allatostatin A1]: Mass=935.54; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:25641051};
CC -!- MASS SPECTROMETRY: [Allatostatin A2]: Mass=923.51; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:25641051};
CC -!- MASS SPECTROMETRY: [Allatostatin A3]: Mass=1038.58;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:25641051};
CC -!- MASS SPECTROMETRY: [Allatostatin A4]: Mass=908.46; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:25641051};
CC -!- MASS SPECTROMETRY: [Allatostatin A5]: Mass=1306.65;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:25641051};
CC -!- SIMILARITY: Belongs to the allatostatin family. {ECO:0000305}.
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DR EMBL; BK008412; DAA35076.1; -; Genomic_DNA.
DR EMBL; GL438827; EFN68211.1; -; Genomic_DNA.
DR RefSeq; XP_011256308.1; XM_011258006.2.
DR RefSeq; XP_011256309.1; XM_011258007.1.
DR AlphaFoldDB; E2ADX8; -.
DR STRING; 104421.E2ADX8; -.
DR PRIDE; E2ADX8; -.
DR GeneID; 105251311; -.
DR KEGG; cfo:105251311; -.
DR InParanoid; E2ADX8; -.
DR OMA; EKRAYAY; -.
DR OrthoDB; 1309198at2759; -.
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; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..64
FT /evidence="ECO:0000305|PubMed:25641051"
FT /id="PRO_0000434185"
FT PEPTIDE 67..74
FT /note="Allatostatin A1"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434186"
FT PROPEP 78..84
FT /evidence="ECO:0000305|PubMed:25641051"
FT /id="PRO_0000434187"
FT PEPTIDE 87..94
FT /note="Allatostatin A2"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434188"
FT PEPTIDE 98..105
FT /note="Allatostatin A3"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434189"
FT PROPEP 109..139
FT /evidence="ECO:0000305|PubMed:25641051"
FT /id="PRO_0000434190"
FT PEPTIDE 142..150
FT /note="Allatostatin A4"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434191"
FT PEPTIDE 154..165
FT /note="Allatostatin A5"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434192"
FT PROPEP 169..193
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434193"
FT MOD_RES 74
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:25641051"
FT MOD_RES 94
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:25641051"
FT MOD_RES 105
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:25641051"
FT MOD_RES 150
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:25641051"
FT MOD_RES 165
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:25641051"
SQ SEQUENCE 193 AA; 21922 MW; 27560FFCDA1B753A CRC64;
MKTSSLIAMR LIIFYLLSVV GRSTAAVEEA PASSLHIPRL NPLSSNLEYD EPSEKRAYAY
ISEYKRLPLY NFGIGKRWID NSEDKRTRPF SFGIGKRLRD YRFGIGKRNS GYRPLGMDFS
VDNMDFHSRE DNLDDFIDDK RGGQPFSFGI GKRGWKLPMG EMAVSGRRLN DVVGPKYLLG
LGKGLSENEN LIQ
