ALLSC_CAMFO
ID ALLSC_CAMFO Reviewed; 93 AA.
AC E2A6Z3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Allatostatin C {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Peptide LRSQLDIGDLQ {ECO:0000303|PubMed:25641051};
DE Contains:
DE RecName: Full=Allatostatin C {ECO:0000303|PubMed:25641051};
DE Short=SYWKQCAFNAVSCF-amide {ECO:0000250|UniProtKB:P85798};
DE Flags: Precursor;
GN ORFNames=EAG_07220 {ECO:0000312|EMBL:EFN70796.1};
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 64-74, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS
RP 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: Inhibits juvenile hormone biosynthesis.
CC {ECO:0000250|UniProtKB:P42559}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25641051}.
CC -!- MASS SPECTROMETRY: [Peptide LRSQLDIGDLQ]: Mass=1256.67;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:25641051};
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DR EMBL; GL437208; EFN70796.1; -; Genomic_DNA.
DR RefSeq; XP_011252628.1; XM_011254326.2.
DR AlphaFoldDB; E2A6Z3; -.
DR STRING; 104421.E2A6Z3; -.
DR GeneID; 105249103; -.
DR KEGG; cfo:105249103; -.
DR InParanoid; E2A6Z3; -.
DR OMA; VISKMMS; -.
DR OrthoDB; 1549004at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..61
FT /evidence="ECO:0000305|PubMed:25641051"
FT /id="PRO_0000434182"
FT PEPTIDE 64..74
FT /note="Peptide LRSQLDIGDLQ"
FT /evidence="ECO:0000269|PubMed:25641051"
FT /id="PRO_0000434183"
FT PEPTIDE 78..91
FT /note="Allatostatin C"
FT /evidence="ECO:0000250|UniProtKB:P85798"
FT /id="PRO_0000434184"
FT DISULFID 83..90
FT /evidence="ECO:0000250|UniProtKB:P85798"
SQ SEQUENCE 93 AA; 10506 MW; 0B99B7A0FD8E9E10 CRC64;
MSSVRNIAAL ALVLLVLAEW SAAMPTTDKD KERLLNTVDL IDDDGSIETA LINYLFTKQI
VKRLRSQLDI GDLQRKRSYW KQCAFNAVSC FGK