ID   FMRF_CAMFO              Reviewed;         184 AA.
AC   E1ZZF9;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=FMRFamide-related peptides {ECO:0000305|PubMed:25641051};
DE   Contains:
DE     RecName: Full=FMRFamide 1 {ECO:0000303|PubMed:25641051};
DE     AltName: Full=STMGSSFIRF-amide {ECO:0000305|PubMed:25641051};
DE   Contains:
DE     RecName: Full=FMRFamide 2 {ECO:0000303|PubMed:25641051};
DE     AltName: Full=WKSPDIVIRF-amide {ECO:0000305|PubMed:25641051};
DE   Contains:
DE     RecName: Full=FMRFamide 3 {ECO:0000303|PubMed:25641051};
DE     AltName: Full=GKNDLNFIRF-amide {ECO:0000305|PubMed:25641051};
GN   ORFNames=EAG_11727 {ECO:0000312|EMBL:EFN73451.1};
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 47-56; 85-94 AND 110-119, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT PHE-56;
RP   PHE-94 AND PHE-119.
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: In insects, FMRFamide and related peptides have modulatory
CC       actions at skeletal neuromuscular junctions, and peptides that are
CC       immunologically related to FMRFamide are released into the circulation
CC       from neurohemal organs. {ECO:0000250|UniProtKB:P10552}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:25641051}.
CC   -!- TISSUE SPECIFICITY: Expressed throughout the central nervous system.
CC       {ECO:0000269|PubMed:25641051}.
CC   -!- MASS SPECTROMETRY: [FMRFamide 1]: Mass=1131.56; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:25641051};
CC   -!- MASS SPECTROMETRY: [FMRFamide 2]: Mass=1259.73; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:25641051};
CC   -!- MASS SPECTROMETRY: [FMRFamide 3]: Mass=1222.59; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:25641051};
CC   -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC       {ECO:0000305}.
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DR   EMBL; GL435343; EFN73451.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1ZZF9; -.
DR   InParanoid; E1ZZF9; -.
DR   OMA; WKSPDIV; -.
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.
FT   CHAIN           1..184
FT                   /note="FMRFamide-related peptides"
FT                   /id="PRO_0000434212"
FT   PROPEP          1..44
FT                   /evidence="ECO:0000305|PubMed:25641051"
FT                   /id="PRO_0000434213"
FT   PEPTIDE         47..56
FT                   /note="FMRFamide 1"
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT                   /id="PRO_0000434214"
FT   PROPEP          59..83
FT                   /evidence="ECO:0000305|PubMed:25641051"
FT                   /id="PRO_0000434215"
FT   PEPTIDE         85..94
FT                   /note="FMRFamide 2"
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT                   /id="PRO_0000434216"
FT   PROPEP          97..107
FT                   /evidence="ECO:0000305|PubMed:25641051"
FT                   /id="PRO_0000434217"
FT   PEPTIDE         110..119
FT                   /note="FMRFamide 3"
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT                   /id="PRO_0000434218"
FT   PROPEP          122..184
FT                   /evidence="ECO:0000305|PubMed:25641051"
FT                   /id="PRO_0000434219"
FT   MOD_RES         56
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT   MOD_RES         94
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:25641051"
FT   MOD_RES         119
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:25641051"
SQ   SEQUENCE   184 AA;  21082 MW;  7CCFFC2F94892EA7 CRC64;
     MLVSSSVLKD DSSLRIFKES PNEFEYIIKR HDMDDRKEDT ESKERRSTMG SSFIRFGRGQ
     SFFNNLDNSA FDNEIDSKVS RHPRWKSPDI VIRFGRSGMK STNDEQPKRG KNDLNFIRFG
     RNIQIVPTDF DLSAVCSALM SNDAISDAGL HPDVTRLFRL CNNLNKITGE ISLDSLETNS
     NHRE