FMRF_DROVI
ID FMRF_DROVI Reviewed; 339 AA.
AC P41876;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=FMRFamide-related peptides;
DE Contains:
DE RecName: Full=SLQDNFMHF-amide;
DE Contains:
DE RecName: Full=DPKQDFMRF-amide;
DE Contains:
DE RecName: Full=APPSDFMRF-amide;
DE Contains:
DE RecName: Full=APSDFMRF-amide;
DE Contains:
DE RecName: Full=DPSQDFMRF-amide;
DE Contains:
DE RecName: Full=SDNFMRF-amide;
DE Contains:
DE RecName: Full=SPKQDFMRF-amide;
DE Contains:
DE RecName: Full=PDNFMRF-amide;
DE Contains:
DE RecName: Full=SAPTEFERN-amide;
DE Contains:
DE RecName: Full=MDSNFMRF-amide;
DE Flags: Precursor;
GN Name=FMRFa {ECO:0000250|UniProtKB:P10552};
GN Synonyms=Fmrf {ECO:0000250|UniProtKB:P10552};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND AMIDATION AT PHE-122; PHE-161; PHE-172; PHE-182;
RP PHE-193; PHE-202; PHE-222; PHE-231; ASN-242 AND PHE-252.
RX PubMed=2113087; DOI=10.1523/jneurosci.10-06-01929.1990;
RA Taghert P.H., Schneider L.E.;
RT "Interspecific comparison of a Drosophila gene encoding FMRFamide-related
RT neuropeptides.";
RL J. Neurosci. 10:1929-1942(1990).
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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: This precursor includes 10 peptides that have FMRF or related
CC sequences at their C-termini.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000305}.
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DR EMBL; M32643; AAA03162.1; -; Unassigned_DNA.
DR PIR; A60918; A60918.
DR AlphaFoldDB; P41876; -.
DR STRING; 7244.FBpp0236899; -.
DR eggNOG; ENOG502SDD0; Eukaryota.
DR GO; GO:0005615; C:extracellular space; IEA:EnsemblMetazoa.
DR GO; GO:0071855; F:neuropeptide receptor binding; IEA:EnsemblMetazoa.
DR GO; GO:0048018; F:receptor ligand activity; IEA:EnsemblMetazoa.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0002209; P:behavioral defense response; IEA:EnsemblMetazoa.
DR GO; GO:0008345; P:larval locomotory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0010459; P:negative regulation of heart rate; IEA:EnsemblMetazoa.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:EnsemblMetazoa.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IEA:EnsemblMetazoa.
DR GO; GO:0006942; P:regulation of striated muscle contraction; IEA:EnsemblMetazoa.
DR InterPro; IPR002544; FMRFamid-related_peptide-like.
DR Pfam; PF01581; FARP; 9.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Neuropeptide; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..110
FT /id="PRO_0000009739"
FT PEPTIDE 114..122
FT /note="SLQDNFMHF-amide"
FT /id="PRO_0000009740"
FT PROPEP 126..151
FT /id="PRO_0000009741"
FT PEPTIDE 153..161
FT /note="DPKQDFMRF-amide"
FT /id="PRO_0000009742"
FT PEPTIDE 164..172
FT /note="APPSDFMRF-amide"
FT /id="PRO_0000009743"
FT PEPTIDE 175..182
FT /note="APSDFMRF-amide"
FT /id="PRO_0000009744"
FT PEPTIDE 185..193
FT /note="DPSQDFMRF-amide"
FT /id="PRO_0000009745"
FT PEPTIDE 196..202
FT /note="SDNFMRF-amide"
FT /id="PRO_0000009746"
FT PROPEP 205..212
FT /id="PRO_0000009747"
FT PEPTIDE 214..222
FT /note="SPKQDFMRF-amide"
FT /id="PRO_0000009748"
FT PEPTIDE 225..231
FT /note="PDNFMRF-amide"
FT /id="PRO_0000009749"
FT PEPTIDE 234..242
FT /note="SAPTEFERN-amide"
FT /id="PRO_0000009750"
FT PEPTIDE 245..252
FT /note="MDSNFMRF-amide"
FT /id="PRO_0000009751"
FT PROPEP 256..339
FT /id="PRO_0000009752"
FT REGION 38..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
FT MOD_RES 161
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
FT MOD_RES 172
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
FT MOD_RES 182
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
FT MOD_RES 193
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
FT MOD_RES 202
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
FT MOD_RES 222
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
FT MOD_RES 231
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
FT MOD_RES 242
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
FT MOD_RES 252
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:2113087"
SQ SEQUENCE 339 AA; 39379 MW; A7245C06B231ABB5 CRC64;
MGIALMFLLA LYQMQSAIHS EIIETPSSYN DNSLLEAAAE EPNSRATASE SDLLDGLMST
DNPNPEQQTE LEFRYPISAI GIGYAKNSVV LRFQKHARKQ NFKYDPDYEM KRKSLQDNFM
HFGKRQAEQL PQATGPGYYE CIKRSAMDRY GRDPKQDFMR FGRAPPSDFM RFGRAPSDFM
RFGRDPSQDF MRFGRSDNFM RFGRNLNFHE ELRSPKQDFM RFGRPDNFMR FGRSAPTEFE
RNGKMDSNFM RFGKRSGVMA KLTKSQLQQN KLTTADGKQQ PAEEGNPTDK AISMLFNKHQ
QQQQQQQGQR LQQEDRQQMK SSAEQNNLEE ASVEQFYEP
