FMRF_BOMMO
ID FMRF_BOMMO Reviewed; 177 AA.
AC Q1MX22;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=FMRFamide-related peptides {ECO:0000303|PubMed:16707581, ECO:0000312|EMBL:BAE93471.1};
DE Short=FaRPs {ECO:0000303|PubMed:16707581};
DE AltName: Full=Bommo-FMRFamide {ECO:0000303|PubMed:16707581};
DE Short=BRFa {ECO:0000303|PubMed:16707581};
DE Contains:
DE RecName: Full=SAIDRSMIRF-amide {ECO:0000303|PubMed:16707581};
DE AltName: Full=MIRFamide {ECO:0000303|PubMed:16707581};
DE Short=RFa-1 {ECO:0000303|PubMed:16707581};
DE Contains:
DE RecName: Full=SASFVRF-amide {ECO:0000303|PubMed:16707581};
DE AltName: Full=FVRFamide {ECO:0000303|PubMed:16707581};
DE Short=RFa-2 {ECO:0000303|PubMed:16707581};
DE Contains:
DE RecName: Full=DPSFIRF-amide {ECO:0000303|PubMed:16707581};
DE AltName: Full=FIRFamide {ECO:0000303|PubMed:16707581};
DE Short=RFa-3 {ECO:0000303|PubMed:16707581};
DE Contains:
DE RecName: Full=ARNHFIRL-amide {ECO:0000303|PubMed:16707581};
DE AltName: Full=FIRLamide {ECO:0000303|PubMed:16707581};
DE Short=RFa-4 {ECO:0000303|PubMed:16707581};
DE Flags: Precursor;
GN Name=RFa {ECO:0000303|PubMed:16707581};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE93471.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 105-112, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MASS
RP SPECTROMETRY, AND AMIDATION AT PHE-45; PHE-102; PHE-111 AND LEU-143.
RC STRAIN=Kinshu X Showa {ECO:0000312|EMBL:BAE93471.1};
RC TISSUE=Larva {ECO:0000269|PubMed:16707581};
RX PubMed=16707581; DOI=10.1073/pnas.0511196103;
RA Yamanaka N., Zitnan D., Kim Y.J., Adams M.E., Hua Y.J., Suzuki Y.,
RA Suzuki M., Suzuki A., Satake H., Mizoguchi A., Asaoka K., Tanaka Y.,
RA Kataoka H.;
RT "Regulation of insect steroid hormone biosynthesis by innervating
RT peptidergic neurons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8622-8627(2006).
CC -!- FUNCTION: Regulates ecdysteroidogenesis by direct innervation of the
CC prothoracic gland by reducing cAMP production via the receptor for
CC myosuppressin. The neurons that innervate the prothoracic gland during
CC the fifth instar are most active during days 0-4, after which they
CC reduce and then peak again on day 6. Expression suppresses the
CC biosynthesis of steroid hormones called ecdysteroids that elicit
CC molting and metamorphosis. {ECO:0000269|PubMed:16707581}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16707581}.
CC Note=Detected at the gland surface. {ECO:0000269|PubMed:16707581}.
CC -!- TISSUE SPECIFICITY: Only expressed in the CNS and predominantly in the
CC thoracic ganglia. Strongest expression is seen in two pairs of large
CC neurons in each thoracic ganglion. These neurons are ventrolateral
CC neurosecretory cells 1 and 2, they project their axons through
CC transverse nerves into the periphery where axons from the prothoracic
CC ganglion innervate the prothoracic gland.
CC {ECO:0000269|PubMed:16707581}.
CC -!- DEVELOPMENTAL STAGE: Expression is continuous throughout the
CC developmental period, but is highest during the feeding period in the
CC early half of the fifth instar stage (days 0-4). Expression decreases
CC remarkably on day 5 before larvae start wandering on day 6, but
CC stabilizes before the end of the fifth instar stage.
CC {ECO:0000269|PubMed:16707581}.
CC -!- MASS SPECTROMETRY: [SAIDRSMIRF-amide]: Mass=1194.6; Method=MALDI;
CC Note=RFa-1.; Evidence={ECO:0000269|PubMed:16707581};
CC -!- MASS SPECTROMETRY: [SASFVRF-amide]: Mass=812.4; Method=MALDI; Note=RFa-
CC 2.; Evidence={ECO:0000269|PubMed:16707581};
CC -!- MASS SPECTROMETRY: [DPSFIRF-amide]: Mass=880.5; Method=MALDI; Note=RFa-
CC 3.; Evidence={ECO:0000269|PubMed:16707581};
CC -!- MASS SPECTROMETRY: [ARNHFIRL-amide]: Mass=1025.6; Method=MALDI;
CC Note=RFa-4.; Evidence={ECO:0000269|PubMed:16707581};
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000255}.
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DR EMBL; AB234100; BAE93471.1; -; mRNA.
DR RefSeq; NP_001037000.1; NM_001043535.2.
DR AlphaFoldDB; Q1MX22; -.
DR STRING; 7091.BGIBMGA009271-TA; -.
DR GeneID; 692549; -.
DR KEGG; bmor:692549; -.
DR CTD; 14072; -.
DR eggNOG; ENOG502T7MT; Eukaryota.
DR HOGENOM; CLU_1579855_0_0_1; -.
DR InParanoid; Q1MX22; -.
DR OrthoDB; 1412744at2759; -.
DR Proteomes; UP000005204; 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; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..32
FT /evidence="ECO:0000255, ECO:0000269|PubMed:16707581"
FT /id="PRO_0000393894"
FT PEPTIDE 36..45
FT /note="SAIDRSMIRF-amide"
FT /evidence="ECO:0000269|PubMed:16707581"
FT /id="PRO_0000393895"
FT PROPEP 47..93
FT /evidence="ECO:0000269|PubMed:16707581"
FT /id="PRO_0000393896"
FT PEPTIDE 96..102
FT /note="SASFVRF-amide"
FT /evidence="ECO:0000269|PubMed:16707581"
FT /id="PRO_0000393897"
FT PEPTIDE 105..111
FT /note="DPSFIRF-amide"
FT /evidence="ECO:0000269|PubMed:16707581"
FT /id="PRO_0000393898"
FT PROPEP 113..131
FT /evidence="ECO:0000269|PubMed:16707581"
FT /id="PRO_0000393899"
FT PEPTIDE 136..143
FT /note="ARNHFIRL-amide"
FT /evidence="ECO:0000269|PubMed:16707581"
FT /id="PRO_0000393900"
FT PROPEP 145..177
FT /evidence="ECO:0000269|PubMed:16707581"
FT /id="PRO_0000393901"
FT REGION 145..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16707581"
FT MOD_RES 102
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16707581"
FT MOD_RES 111
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:16707581"
FT MOD_RES 143
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:16707581"
SQ SEQUENCE 177 AA; 20258 MW; 5656A5CA1B3F712C CRC64;
MNHPRSIAML AALWLVVSVT STPVRRSPDL EARRRSAIDR SMIRFGRSTL PVVPPAQPSF
LQRYSAPQPA ALTADDLMTF LRAYEEDYSS PVSKKSASFV RFGRDPSFIR FGRSVDEENS
GYQAETNTYP QRRHRARNHF IRLGRDNELS ESNDEDRYEV ESERTKRSVV DPCNDCA
