FMRF_DROME
ID FMRF_DROME Reviewed; 347 AA.
AC P10552; Q9V5D8;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=FMRFamide-related peptides;
DE Contains:
DE RecName: Full=FMRFamide A;
DE Contains:
DE RecName: Full=Corticotropin-releasing factor-like;
DE Contains:
DE RecName: Full=AAMDRY-amide;
DE Contains:
DE RecName: Full=DPKQDFMRF-amide;
DE Contains:
DE RecName: Full=TPAEDFMRF-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=SAPQDFVRS-amide;
DE Contains:
DE RecName: Full=MDSNFIRF-amide;
DE Flags: Precursor;
GN Name=FMRFa {ECO:0000312|FlyBase:FBgn0000715};
GN Synonyms=Fmrf {ECO:0000312|FlyBase:FBgn0000715};
GN ORFNames=CG2346 {ECO:0000312|FlyBase:FBgn0000715};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2324103; DOI=10.1016/s0021-9258(19)39233-6;
RA Schneider L.E., Taghert P.H.;
RT "Organization and expression of the Drosophila Phe-Met-Arg-Phe-NH2
RT neuropeptide gene.";
RL J. Biol. Chem. 265:6890-6895(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=3162321; DOI=10.1073/pnas.85.6.1993;
RA Schneider L.E., Taghert P.H.;
RT "Isolation and characterization of a Drosophila gene that encodes multiple
RT neuropeptides related to Phe-Met-Arg-Phe-NH2 (FMRFamide).";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1993-1997(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=2350439; DOI=10.1089/dna.1990.9.263;
RA Chin A.C., Reynolds E.R., Scheller R.H.;
RT "Organization and expression of the Drosophila FMRFamide-related prohormone
RT gene.";
RL DNA Cell Biol. 9:263-271(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-157; PHE-168; PHE-179;
RP PHE-190 AND PHE-201.
RX PubMed=3272155; DOI=10.1016/0896-6273(88)90209-7;
RA Nambu J.R., Murphy-Erdosh C., Andrews P.C., Feistner G.J., Scheller R.H.;
RT "Isolation and characterization of a Drosophila neuropeptide gene.";
RL Neuron 1:55-61(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP PARTIAL PROTEIN SEQUENCE (DPKQDFMRF-AMIDE; TPAEDFMRF-AMIDE AND
RP SDNFMRF-AMIDE).
RX PubMed=1390001; DOI=10.1007/bf03380141;
RA Nichols R.;
RT "Isolation and structural characterization of Drosophila TDVDHVFLRFamide
RT and FMRFamide-containing neural peptides.";
RL J. Mol. Neurosci. 3:213-218(1992).
RN [9]
RP PROTEIN SEQUENCE OF 149-157; 160-168; 171-179; 182-190; 193-201; 204-212;
RP 215-223; 226-232 AND 253-259, AND AMIDATION AT PHE-114; TYR-146; PHE-157;
RP PHE-168; PHE-179; PHE-190; PHE-201; PHE-212; PHE-223; PHE-232; PHE-250;
RP PHE-259; SER-270 AND PHE-280.
RC TISSUE=Larva;
RX PubMed=12171930; DOI=10.1074/jbc.m206257200;
RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.;
RT "Peptidomics of the larval Drosophila melanogaster central nervous
RT system.";
RL J. Biol. Chem. 277:40368-40374(2002).
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 13 peptides that have FMRF or related
CC sequences at their C-termini, and other putative neuropeptides.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000305}.
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DR EMBL; M32641; AAA28537.1; -; Genomic_DNA.
DR EMBL; J03232; AAA28536.1; -; mRNA.
DR EMBL; M37711; AAA28538.1; -; Genomic_DNA.
DR EMBL; X53301; CAA37389.1; -; mRNA.
DR EMBL; X76204; CAA53798.1; -; mRNA.
DR EMBL; AE013599; AAF58874.1; -; Genomic_DNA.
DR EMBL; AY070639; AAL48110.1; -; mRNA.
DR PIR; A34616; A34616.
DR RefSeq; NP_523669.2; NM_078945.4.
DR AlphaFoldDB; P10552; -.
DR BioGRID; 61858; 2.
DR STRING; 7227.FBpp0087471; -.
DR PaxDb; P10552; -.
DR PRIDE; P10552; -.
DR DNASU; 36030; -.
DR EnsemblMetazoa; FBtr0088383; FBpp0087471; FBgn0000715.
DR GeneID; 36030; -.
DR KEGG; dme:Dmel_CG2346; -.
DR CTD; 36030; -.
DR FlyBase; FBgn0000715; FMRFa.
DR VEuPathDB; VectorBase:FBgn0000715; -.
DR eggNOG; ENOG502SDD0; Eukaryota.
DR HOGENOM; CLU_045740_0_0_1; -.
DR InParanoid; P10552; -.
DR PhylomeDB; P10552; -.
DR BioGRID-ORCS; 36030; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36030; -.
DR PRO; PR:P10552; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000715; Expressed in embryonic central brain neuron (Drosophila) and 3 other tissues.
DR Genevisible; P10552; DM.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0071855; F:neuropeptide receptor binding; IPI:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0002209; P:behavioral defense response; IDA:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IDA:FlyBase.
DR GO; GO:0045822; P:negative regulation of heart contraction; IDA:FlyBase.
DR GO; GO:0010459; P:negative regulation of heart rate; IDA:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:FlyBase.
DR GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IDA:FlyBase.
DR GO; GO:0006942; P:regulation of striated muscle contraction; IDA:FlyBase.
DR InterPro; IPR002544; FMRFamid-related_peptide-like.
DR Pfam; PF01581; FARP; 12.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..102
FT /id="PRO_0000009721"
FT PEPTIDE 106..114
FT /note="FMRFamide A"
FT /id="PRO_0000009722"
FT PEPTIDE 118..138
FT /note="Corticotropin-releasing factor-like"
FT /id="PRO_0000009723"
FT PEPTIDE 141..146
FT /note="AAMDRY-amide"
FT /id="PRO_0000009724"
FT PEPTIDE 149..157
FT /note="DPKQDFMRF-amide"
FT /evidence="ECO:0000269|PubMed:3272155"
FT /id="PRO_0000009725"
FT PEPTIDE 160..168
FT /note="DPKQDFMRF-amide"
FT /evidence="ECO:0000269|PubMed:3272155"
FT /id="PRO_0000009726"
FT PEPTIDE 171..179
FT /note="DPKQDFMRF-amide"
FT /evidence="ECO:0000269|PubMed:3272155"
FT /id="PRO_0000009727"
FT PEPTIDE 182..190
FT /note="DPKQDFMRF-amide"
FT /evidence="ECO:0000269|PubMed:3272155"
FT /id="PRO_0000009728"
FT PEPTIDE 193..201
FT /note="DPKQDFMRF-amide"
FT /evidence="ECO:0000269|PubMed:3272155"
FT /id="PRO_0000009729"
FT PEPTIDE 204..212
FT /note="TPAEDFMRF-amide"
FT /id="PRO_0000009730"
FT PEPTIDE 215..223
FT /note="TPAEDFMRF-amide"
FT /id="PRO_0000009731"
FT PEPTIDE 226..232
FT /note="SDNFMRF-amide"
FT /id="PRO_0000009732"
FT PROPEP 235..240
FT /id="PRO_0000009733"
FT PEPTIDE 242..250
FT /note="SPKQDFMRF-amide"
FT /id="PRO_0000009734"
FT PEPTIDE 253..259
FT /note="PDNFMRF-amide"
FT /id="PRO_0000009735"
FT PEPTIDE 262..270
FT /note="SAPQDFVRS-amide"
FT /id="PRO_0000009736"
FT PEPTIDE 273..280
FT /note="MDSNFIRF-amide"
FT /id="PRO_0000009737"
FT PROPEP 283..347
FT /id="PRO_0000009738"
FT REGION 283..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 146
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 157
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:3272155"
FT MOD_RES 168
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:3272155"
FT MOD_RES 179
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:3272155"
FT MOD_RES 190
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:3272155"
FT MOD_RES 201
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930,
FT ECO:0000269|PubMed:3272155"
FT MOD_RES 212
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 223
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 232
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 250
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 259
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 270
FT /note="Serine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT MOD_RES 280
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
FT CONFLICT 36
FT /note="A -> T (in Ref. 2; AAA28536)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="E -> Q (in Ref. 3; AAA28538/CAA37389)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="S -> P (in Ref. 5; AAF58874 and 7; AAL48110)"
FT /evidence="ECO:0000305"
FT CONFLICT 62..63
FT /note="EL -> DV (in Ref. 4; CAA53798)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="G -> E (in Ref. 1; AAA28537, 5; AAF58874 and 7;
FT AAL48110)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> A (in Ref. 3; AAA28538/CAA37389)"
FT /evidence="ECO:0000305"
FT CONFLICT 239..240
FT /note="EL -> DV (in Ref. 3; AAA28538/CAA37389 and 4;
FT CAA53798)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="A -> R (in Ref. 3; AAA28538/CAA37389 and 4;
FT CAA53798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 40100 MW; C07014CBDF39C7E8 CRC64;
MGIALMFLLA LYQMQSAIHS EIIDTPNYAG NSLQDADSEV SPSQDNDLVD ALLGNDQTER
AELEFRHPIS VIGIDYSKNA VVLHFQKHGR KPRYKYDPEL EAKRRSVQDN FMHFGKRQAE
QLPPEGSYAG SDELEGMAKR AAMDRYGRDP KQDFMRFGRD PKQDFMRFGR DPKQDFMRFG
RDPKQDFMRF GRDPKQDFMR FGRTPAEDFM RFGRTPAEDF MRFGRSDNFM RFGRSPHEEL
RSPKQDFMRF GRPDNFMRFG RSAPQDFVRS GKMDSNFIRF GKSLKPAAPE SKPVKSNQGN
PGERSPVDKA MTELFKKQEL QDQQVKNGAQ ATTTQDGSVE QDQFFGQ
