FMRF_SEPOF
ID FMRF_SEPOF Reviewed; 331 AA.
AC P91889;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=FMRFamide-related neuropeptides {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498, ECO:0000312|EMBL:CAA72116.1};
DE Contains:
DE RecName: Full=FIRF-amide {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=ALSGDAFLRF-amide {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FLRF-amide {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 1 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 2 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 3 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 4 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 5 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 6 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 7 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 8 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 9 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 10 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Contains:
DE RecName: Full=FMRF-amide 11 {ECO:0000303|PubMed:11060217, ECO:0000303|PubMed:9192498};
DE Flags: Precursor;
GN Name=FMRFa {ECO:0000303|PubMed:11060217};
OS Sepia officinalis (Common cuttlefish).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Sepiida; Sepiina; Sepiidae; Sepia.
OX NCBI_TaxID=6610;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA72116.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain {ECO:0000269|PubMed:9192498};
RX PubMed=9192498; DOI=10.1242/jeb.200.10.1483;
RA Loi P.K., Tublitz N.;
RT "Molecular analysis of FMRFamide- and FMRFamide-related peptides (FaRPS) in
RT the cuttlefish Sepia officinalis.";
RL J. Exp. Biol. 200:1483-1489(1997).
RN [2] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9319020; DOI=10.1242/jeb.199.5.1177;
RA Loi P., Saunders R., Young D., Tublitz N.;
RT "Peptidergic regulation of chromatophore function in the European
RT cuttlefish Sepia officinalis.";
RL J. Exp. Biol. 199:1177-1187(1996).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10805923;
RX DOI=10.1002/(sici)1096-9861(20000515)420:4<499::aid-cne7>3.0.co;2-e;
RA Loi P.K., Tublitz N.J.;
RT "Roles of glutamate and FMRFamide-related peptides at the chromatophore
RT neuromuscular junction in the cuttlefish, Sepia officinalis.";
RL J. Comp. Neurol. 420:499-511(2000).
RN [4] {ECO:0000305}
RP MASS SPECTROMETRY.
RX PubMed=11060217; DOI=10.1242/jeb.203.23.3565;
RA Sweedler J.V., Li L., Floyd P., Gilly W.;
RT "Mass spectrometric survey of peptides in cephalopods with an emphasis on
RT the FMRFamide-related peptides.";
RL J. Exp. Biol. 203:3565-3573(2000).
CC -!- FUNCTION: Excitatory neurotransmitters that directly modulate
CC chromatophore function by activating chromatophore expansion at the
CC chromatophore neuromuscular junction. {ECO:0000269|PubMed:10805923,
CC ECO:0000269|PubMed:9192498, ECO:0000269|PubMed:9319020}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10805923}.
CC -!- TISSUE SPECIFICITY: Present ubiquitously in the brain and regions of
CC the central nervous system as well as in the periphery and throughout
CC the dermal chromatophore layer (at protein level).
CC {ECO:0000269|PubMed:10805923, ECO:0000269|PubMed:9319020}.
CC -!- MASS SPECTROMETRY: [FIRF-amide]: Mass=581.33; Method=MALDI; Note=FIRF-
CC amide.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [ALSGDAFLRF-amide]: Mass=1095.6; Method=MALDI;
CC Note=ALSGDAFLRF-amide.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FLRF-amide]: Mass=581.33; Method=MALDI; Note=FLRF-
CC amide.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 1]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 1.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 2]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 2.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 3]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 3.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 4]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 4.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 5]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 5.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 6]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 6.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 7]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 7.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 8]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 8.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 9]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 9.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 10]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 10.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- MASS SPECTROMETRY: [FMRF-amide 11]: Mass=599.29; Method=MALDI;
CC Note=FMRF-amide 11.; Evidence={ECO:0000269|PubMed:11060217};
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000255}.
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DR EMBL; Y11246; CAA72116.1; -; mRNA.
DR AlphaFoldDB; P91889; -.
DR PRIDE; P91889; -.
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 1: Evidence at protein 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:0000269|PubMed:11060217"
FT /id="PRO_0000404053"
FT PEPTIDE 68..71
FT /note="FIRF-amide"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404054"
FT PEPTIDE 74..83
FT /note="ALSGDAFLRF-amide"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404055"
FT PROPEP 86..94
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404056"
FT PEPTIDE 97..100
FT /note="FLRF-amide"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404057"
FT PROPEP 103..168
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404058"
FT PEPTIDE 171..174
FT /note="FMRF-amide 1"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404059"
FT PEPTIDE 178..181
FT /note="FMRF-amide 2"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404060"
FT PROPEP 184..194
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404061"
FT PEPTIDE 197..200
FT /note="FMRF-amide 3"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404062"
FT PROPEP 203..205
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404063"
FT PEPTIDE 208..211
FT /note="FMRF-amide 4"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404064"
FT PROPEP 214..216
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404065"
FT PEPTIDE 219..222
FT /note="FMRF-amide 5"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404066"
FT PROPEP 225..236
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404067"
FT PEPTIDE 239..242
FT /note="FMRF-amide 6"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404068"
FT PROPEP 245..254
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404069"
FT PEPTIDE 257..260
FT /note="FMRF-amide 7"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404070"
FT PROPEP 263..265
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404071"
FT PEPTIDE 268..271
FT /note="FMRF-amide 8"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404072"
FT PROPEP 274..277
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404073"
FT PEPTIDE 280..283
FT /note="FMRF-amide 9"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404074"
FT PROPEP 286..293
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404075"
FT PEPTIDE 296..299
FT /note="FMRF-amide 10"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404076"
FT PROPEP 302..312
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404077"
FT PEPTIDE 315..318
FT /note="FMRF-amide 11"
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404078"
FT PROPEP 321..331
FT /evidence="ECO:0000269|PubMed:11060217"
FT /id="PRO_0000404079"
FT REGION 122..153
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; 38594 MW; 157A15EAD2DBD86B CRC64;
MRCWSPCSLL VVIAIYCLSS HTSEAFDLAQ ACVESQRLSL LPICDTIFAV QQEGAQQSAD
DGLRSKRFIR FGRALSGDAF LRFGKNVPDL PFEDKRFLRF GRAAPQLDDL LKQALQRVES
LQKSDDTSVR RKRSTDAAPQ SNTDSAEQKN DSAKITKRYV DDVEDSDVKR FMRFGKRFMR
FGRNPSDVGS KLTEKRFMRF GRDPEKRFMR FGKSDDKKFM RFGRNPGDAE DELEEDKRFM
RFGRGDEEDE EEAEKRFMRF GRDPEKKFMR FGKNGEEKRF MRFGRNPEEP EADKRFMRFG
RGGEEDDVNT EEKRFMRFGR SAEKCKGCLE G
