FMRF_MUSDO
ID FMRF_MUSDO Reviewed; 388 AA.
AC A6P3B2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=FMRFamide neuropeptides;
DE Contains:
DE RecName: Full=MudFMRFamide-2;
DE Contains:
DE RecName: Full=MudFMRFamide-3;
DE Contains:
DE RecName: Full=MudFMRFamide-4;
DE Contains:
DE RecName: Full=MudFMRFamide-5;
DE Contains:
DE RecName: Full=MudFMRFamide-6;
DE Contains:
DE RecName: Full=MudFMRFamide-7;
DE Contains:
DE RecName: Full=MudFMRFamide-8;
DE AltName: Full=MudFMRFamide-10;
DE Contains:
DE RecName: Full=MudFMRFamide-9;
DE AltName: Full=MudFMRFamide-11;
DE AltName: Full=MudFMRFamide-12;
DE AltName: Full=MudFMRFamide-13;
DE Contains:
DE RecName: Full=MudFMRFamide-14;
DE Contains:
DE RecName: Full=MudFMRFamide-15;
DE Contains:
DE RecName: Full=MudFMRFamide-17;
DE Contains:
DE RecName: Full=MudFMRFamide-16;
DE Contains:
DE RecName: Full=MudFMRFamide-18;
DE Flags: Precursor;
GN Name=fmrf {ECO:0000312|EMBL:BAF73475.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF73475.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000312|EMBL:BAF73475.1};
RX PubMed=17426155; DOI=10.1093/jb/mvm094;
RA Matsuhima A., Takano K., Yoshida T., Takeda Y., Yokotani S.,
RA Shimohigashi Y., Shimohigashi M.;
RT "Double-labelled in situ hybridization reveals the lack of co-localization
RT of mRNAs for the circadian neuropeptide PDF and FMRFamide in brains of the
RT flies Musca domestica and Drosophila melanogaster.";
RL J. Biochem. 141:867-877(2007).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 173-179; 182-196; 199-208; 211-219; 222-230; 233-241;
RP 244-253; 256-265; 268-277; 280-289; 292-301; 304-313; 316-325; 328-337;
RP 340-346; 349-359 AND 362-372, MASS SPECTROMETRY, AND AMIDATION AT PHE-179;
RP PHE-196; PHE-208; PHE-219; PHE-230; PHE-241; PHE-253; PHE-265; PHE-277;
RP PHE-289; PHE-301; PHE-313; PHE-325; PHE-337; PHE-346; PHE-359 AND PHE-372.
RC TISSUE=Dorsal ganglionic sheath {ECO:0000269|PubMed:18789334};
RX PubMed=18789334; DOI=10.1016/j.ygcen.2008.08.006;
RA Rahman M.M., Fromm B., Neupert S., Kreusch S., Predel R.;
RT "Extended FMRFamides in dipteran insects: conservative expression in the
RT neuroendocrine system is accompanied by rapid sequence evolution.";
RL Gen. Comp. Endocrinol. 162:52-58(2009).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In the brain, expressed in 2 large cells in the
CC lateral neurons in each optic lobe, 2 slightly bigger cells on both
CC sides of the tritocerebrum, around 14 small cells in the dorsal area,
CC around 13 cells in the subesophageal ganglion, and in the central
CC brain. {ECO:0000269|PubMed:17426155}.
CC -!- MASS SPECTROMETRY: [MudFMRFamide-2]: Mass=885.40; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-3]: Mass=1558.67; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-4]: Mass=1103.49; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-5]: Mass=1084.50; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-6]: Mass=1041.49; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-7]: Mass=1043.47; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-8]: Mass=1170.54; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-9]: Mass=1170.54; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-8]: Mass=1197.55; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-9]: Mass=1197.55; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-14]: Mass=114.51; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-15]: Mass=1154.54; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-17]: Mass=1285.60; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-16]: Mass=925.43; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- MASS SPECTROMETRY: [MudFMRFamide-18]: Mass=1315.61; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18789334};
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000255}.
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DR EMBL; AB214648; BAF73475.1; -; mRNA.
DR AlphaFoldDB; A6P3B2; -.
DR STRING; 7370.XP_005182209.1; -.
DR PRIDE; A6P3B2; -.
DR VEuPathDB; VectorBase:MDOA012531; -.
DR eggNOG; ENOG502SDD0; Eukaryota.
DR Proteomes; UP000095301; Whole Genome Shotgun Assembly.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR002544; FMRFamid-related_peptide-like.
DR Pfam; PF01581; FARP; 17.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..172
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371776"
FT PEPTIDE 173..179
FT /note="MudFMRFamide-2"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371777"
FT PEPTIDE 182..196
FT /note="MudFMRFamide-3"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371778"
FT PEPTIDE 199..208
FT /note="MudFMRFamide-4"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371779"
FT PEPTIDE 211..219
FT /note="MudFMRFamide-5"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371780"
FT PEPTIDE 222..230
FT /note="MudFMRFamide-6"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371781"
FT PEPTIDE 233..241
FT /note="MudFMRFamide-7"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371782"
FT PEPTIDE 244..253
FT /note="MudFMRFamide-8"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371783"
FT PEPTIDE 256..265
FT /note="MudFMRFamide-9"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371784"
FT PEPTIDE 268..277
FT /note="MudFMRFamide-8"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371785"
FT PEPTIDE 280..289
FT /note="MudFMRFamide-9"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371786"
FT PEPTIDE 292..301
FT /note="MudFMRFamide-9"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371787"
FT PEPTIDE 304..313
FT /note="MudFMRFamide-9"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371788"
FT PEPTIDE 316..325
FT /note="MudFMRFamide-14"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371789"
FT PEPTIDE 328..337
FT /note="MudFMRFamide-15"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371790"
FT PEPTIDE 340..346
FT /note="MudFMRFamide-17"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371791"
FT PEPTIDE 349..359
FT /note="MudFMRFamide-16"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371792"
FT PEPTIDE 362..372
FT /note="MudFMRFamide-18"
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371793"
FT PROPEP 375..388
FT /evidence="ECO:0000269|PubMed:18789334"
FT /id="PRO_0000371794"
FT REGION 40..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 179
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 196
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 208
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 219
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 230
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 241
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 253
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 265
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 277
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 289
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 301
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 313
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 325
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 337
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 346
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 359
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
FT MOD_RES 372
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18789334"
SQ SEQUENCE 388 AA; 43972 MW; 50D12A83BF57A296 CRC64;
MVAPLLVFLF SLQLCHTTSW AYVGGNSLNS NSLHASYSEF PAGTSNEVPE DAANGQDDND
DSQLTEPNDN NAPLVQSIDD ETEMQFPKPI QWVSIDHLRN SIILRFQNPT PKILNKLDPE
EMKRLRSLQE NAMRWGKRSY ESYPLNRNGL ADKSSVGRMG FLSNHQVIRD SRGDNFMRFG
RSVGGSGGND DNFMRFGRAS GSSDFMRFGR AGQDNFMRFG RAAGQDFMRF GRGSGQDFMR
FGRSPGSQDF MRFGRNPGSQ DFMRFGRSPG SQDFMRFGRN PGSQDFMRFG RNPGSQDFMR
FGRNPGSQDF MRFGRASGGQ DFMRFGRAPS GQDFMRFGRP DNFMRFGRTP AQSSDFMRFG
RTPTQSSDFM RFGKSLDKSE NKTSDLQK
