FMRF_DORPE
ID FMRF_DORPE Reviewed; 331 AA.
AC B6E465;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=FMRFamide-related neuropeptides {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FIRF-amide {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=ALSGDAFLRF-amide {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FLRF-amide {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 1 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 2 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 3 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 4 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 5 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 6 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 7 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 8 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 9 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 10 {ECO:0000250|UniProtKB:P91889};
DE Contains:
DE RecName: Full=FMRF-amide 11 {ECO:0000250|UniProtKB:P91889};
DE Flags: Precursor;
GN Name=FMRFa {ECO:0000250|UniProtKB:P91889};
OS Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Doryteuthis.
OX NCBI_TaxID=1051067;
RN [1] {ECO:0000312|EMBL:ACI22791.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Burbach J.P.H., Hellemons A.J.C.G.M., Grant P., DeGiorgis J.A., Pant H.C.;
RT "Expression of the FMRF-amide precursor in the nervous system of the squid
RT Loligo pealei.";
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=1362646; DOI=10.1113/expphysiol.1992.sp003655;
RA Cottrell G.A., Lin J.W., Llinas R., Price D.A., Sugimori M., Stanley E.F.;
RT "FMRFamide-related peptides potentiate transmission at the squid giant
RT synapse.";
RL Exp. Physiol. 77:881-889(1992).
CC -!- FUNCTION: Excitatory neurotransmitters that directly modulate
CC chromatophore function by activating chromatophore expansion at the
CC chromatophore neuromuscular junction. {ECO:0000250|UniProtKB:P91889,
CC ECO:0000269|PubMed:1362646}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P91889}.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000255}.
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DR EMBL; FJ205479; ACI22791.1; -; mRNA.
DR AlphaFoldDB; B6E465; -.
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; 14.
PE 2: Evidence at transcript level;
KW Amidation; Cleavage on pair of basic residues; Neuropeptide; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..65
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404026"
FT PEPTIDE 68..71
FT /note="FIRF-amide"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404027"
FT PEPTIDE 74..83
FT /note="ALSGDAFLRF-amide"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404028"
FT PROPEP 86..94
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404029"
FT PEPTIDE 97..100
FT /note="FLRF-amide"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404030"
FT PROPEP 103..168
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404031"
FT PEPTIDE 171..174
FT /note="FMRF-amide 1"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404032"
FT PEPTIDE 178..181
FT /note="FMRF-amide 2"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404033"
FT PROPEP 184..194
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404034"
FT PEPTIDE 197..200
FT /note="FMRF-amide 3"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404035"
FT PROPEP 203..205
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404036"
FT PEPTIDE 208..211
FT /note="FMRF-amide 4"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404037"
FT PROPEP 214..216
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404038"
FT PEPTIDE 219..222
FT /note="FMRF-amide 5"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404039"
FT PROPEP 225..236
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404040"
FT PEPTIDE 239..242
FT /note="FMRF-amide 6"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404041"
FT PROPEP 245..254
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404042"
FT PEPTIDE 257..260
FT /note="FMRF-amide 7"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404043"
FT PROPEP 263..265
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404044"
FT PEPTIDE 268..271
FT /note="FMRF-amide 8"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404045"
FT PROPEP 274..277
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404046"
FT PEPTIDE 280..283
FT /note="FMRF-amide 9"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404047"
FT PROPEP 286..293
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404048"
FT PEPTIDE 296..299
FT /note="FMRF-amide 10"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404049"
FT PROPEP 302..312
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404050"
FT PEPTIDE 315..318
FT /note="FMRF-amide 11"
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404051"
FT PROPEP 321..331
FT /evidence="ECO:0000250|UniProtKB:P91889"
FT /id="PRO_0000404052"
FT REGION 122..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 83
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 100
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 174
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 181
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 200
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 211
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 222
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 242
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 260
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 271
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 283
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 299
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
FT MOD_RES 318
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9GSL0"
SQ SEQUENCE 331 AA; 38650 MW; 055CE1F4B40211BD CRC64;
MRCWSPCSLL VVIVIYCLSS HTSEAFDLAQ ACVESQRLSL LPICDTIFAV QQEGAQQSAD
DGMRSKRFIR FGRALSGDAF LRFGKNVPDL PFEDKRFLRF GRAAPQLDDL LKQALQRVES
LQKADETSVR RKRSTDAAPQ NNAENPEQKN DSAKITKRYI DDVEDSDVKR FMRFGKRFMR
FGRNPSDAGN KLTEKRFMRF GRDPEKRFMR FGKSDDKRFM RFGRNPSDVE DELEEDKRFM
RFGRGGEDDE EEAEKRFMRF GRDPEKKFMR FGKSGEDKRF MRFGRNPDEQ EADKRFMRFG
RGGEDDEVST EDKRFMRFGR SADKCKGCLE G
