FMRFA_AGRIP
ID FMRFA_AGRIP Reviewed; 190 AA.
AC C0HKT6; C0HKT7; C0HKT8; C0HKT9;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=FMRFamide-related peptides {ECO:0000250|UniProtKB:Q1MX22};
DE Contains:
DE RecName: Full=SAIDRSMIRF-amide {ECO:0000305};
DE AltName: Full=RFamide 1 {ECO:0000305|PubMed:29466015};
DE Short=RFa-1 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=RFamide precursor-related peptide 2 {ECO:0000305|PubMed:29466015};
DE Short=RFs-PP-2 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=SASFVRF-amide {ECO:0000305};
DE AltName: Full=RFamide 3 {ECO:0000305|PubMed:29466015};
DE Short=RFa-3 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=ARDHFIRL-amide {ECO:0000305};
DE AltName: Full=RFamide 5 {ECO:0000305|PubMed:29466015};
DE Short=RFa-5 {ECO:0000303|PubMed:29466015};
DE Flags: Precursor;
OS Agrotis ipsilon (Black cutworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Noctuinae; Noctuini; Agrotis.
OX NCBI_TaxID=56364;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-45; 48-66; 107-113 AND
RP 151-158, TISSUE SPECIFICITY, MASS SPECTROMETRY, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND AMIDATION AT PHE-45; PHE-113 AND LEU-158.
RX PubMed=29466015; DOI=10.1021/acs.jproteome.7b00779;
RA Diesner M., Gallot A., Binz H., Gaertner C., Vitecek S., Kahnt J.,
RA Schachtner J., Jacquin-Joly E., Gadenne C.;
RT "Mating-induced differential peptidomics of neuropeptides and protein
RT hormones in Agrotis ipsilon moths.";
RL J. Proteome Res. 17:1397-1414(2018).
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: RFamide 1: Expressed in corpora cardiaca (CC),
CC corpora allata (CA), antennal lobe (AL) and gnathal ganglion (GNG) (at
CC protein level). Expression in AL detected in most animals, in CC, CA
CC and in GNG in some animals (at protein level). RFamide precursor-
CC related peptide 2: Expressed in corpora cardiaca (CC), corpora allata
CC (CA), antennal lobe (AL) and gnathal ganglion (GNG) (at protein level).
CC Expression in AL detected in some animals, expression in CC, CA and GNG
CC in few animals (at protein level). RFamide 3: Expressed in corpora
CC cardiaca (CC), corpora allata (CA), antennal lobe (AL) and gnathal
CC ganglion (GNG) (at protein level). Expression in AL detected in all
CC animals, in CC, CA and GNG in most animals (at protein level). RFamide
CC 5: Expressed in corpora cardiaca (CC), corpora allata (CA), antennal
CC lobe (AL) and gnathal ganglion (GNG) (at protein level). Expression in
CC AL detected in all animals, in CC, CA and in GNG in some animals (at
CC protein level). {ECO:0000269|PubMed:29466015}.
CC -!- MASS SPECTROMETRY: [SAIDRSMIRF-amide]: Mass=1194.62; Mass_error=0.01;
CC Method=MALDI; Note=RFamide 1.; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [RFamide precursor-related peptide 2]: Mass=2132.99;
CC Mass_error=0.01; Method=MALDI; Note=RFamide precursor-related peptide
CC 2.; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [SASFVRF-amide]: Mass=812.42; Mass_error=0.01;
CC Method=MALDI; Note=RFamide 3.; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [ARDHFIRL-amide]: Mass=1026.63; Mass_error=0.01;
CC Method=MALDI; Note=RFamide 5.; Evidence={ECO:0000269|PubMed:29466015};
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000305}.
CC -!- CAUTION: Further mature peptides might exist. {ECO:0000305}.
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DR AlphaFoldDB; C0HKT6; -.
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; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..33
FT /evidence="ECO:0000305"
FT /id="PRO_0000444229"
FT PEPTIDE 36..45
FT /note="SAIDRSMIRF-amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444230"
FT PEPTIDE 48..66
FT /note="RFamide precursor-related peptide 2"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444231"
FT PROPEP 69..104
FT /evidence="ECO:0000305"
FT /id="PRO_0000444232"
FT PEPTIDE 107..113
FT /note="SASFVRF-amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444233"
FT PROPEP 116..150
FT /evidence="ECO:0000305"
FT /id="PRO_0000444234"
FT PEPTIDE 151..158
FT /note="ARDHFIRL-amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444235"
FT PROPEP 160..190
FT /evidence="ECO:0000305"
FT /id="PRO_0000444236"
FT REGION 161..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..190
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:29466015"
FT MOD_RES 113
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 158
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
SQ SEQUENCE 190 AA; 21717 MW; 74A626C9A4167C7B CRC64;
MSCSRTVALL AALWLVVGAT SSPVRRSPDL EARRRSAIDR SMIRFGRSYP PEPSAADIRE
AFERPTRRGN SFLRFGRSQP LTLSTDDLVS LLRAYEEDYD TPMTKKSASF VRFGRDPNFI
RLGRSADDDK SAFEQNSELV VSGYPQRKSR ARDHFIRLGR DSEEVNENEF EETEESRRKR
SADSCHDCQS
