FMRF_LYMST
ID FMRF_LYMST Reviewed; 306 AA.
AC P19802;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=FMRFamide neuropeptides;
DE Contains:
DE RecName: Full=FLRF-amide 1;
DE Contains:
DE RecName: Full=QFYRI-amide;
DE Contains:
DE RecName: Full=FLRF-amide 2;
DE Contains:
DE RecName: Full=PN;
DE AltName: Full=SEEPLY;
DE Contains:
DE RecName: Full=FMRF-amide 1;
DE Contains:
DE RecName: Full=FMRF-amide 2;
DE Contains:
DE RecName: Full=FMRF-amide 3;
DE Contains:
DE RecName: Full=FMRF-amide 4;
DE Contains:
DE RecName: Full=FMRF-amide 5;
DE Contains:
DE RecName: Full=FMRF-amide 6;
DE Contains:
DE RecName: Full=FMRF-amide 7;
DE Contains:
DE RecName: Full=FMRF-amide 8;
DE Contains:
DE RecName: Full=FMRF-amide 9;
DE Contains:
DE RecName: Full=EFLRI-amide;
DE Flags: Precursor;
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-43; ILE-63; PHE-79;
RP PHE-155; PHE-169; PHE-176; PHE-190; PHE-197; PHE-210; PHE-223; PHE-257;
RP PHE-269 AND ILE-285.
RC TISSUE=Brain;
RX PubMed=1968092; DOI=10.1523/jneurosci.10-02-00412.1990;
RA Linacre A., Kellett E., Saunders S., Bright K., Benjamin P.R., Burke J.F.;
RT "Cardioactive neuropeptide Phe-Met-Arg-Phe-NH2 (FMRFamide) and novel
RT related peptides are encoded in multiple copies by a single gene in the
RT snail Lymnaea stagnalis.";
RL J. Neurosci. 10:412-419(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=7965060; DOI=10.1523/jneurosci.14-11-06564.1994;
RA Kellett E., Saunders S.E., Li K.W., Staddon J.W., Benjamin P.R.,
RA Burke J.F.;
RT "Genomic organization of the FMRFamide gene in Lymnaea: multiple exons
RT encoding novel neuropeptides.";
RL J. Neurosci. 14:6564-6570(1994).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=CNS;
RX PubMed=1347559; DOI=10.1523/jneurosci.12-03-01033.1992;
RA Saunders S.E., Kellett E., Bright K., Benjamin P.R., Burke J.F.;
RT "Cell-specific alternative RNA splicing of an FMRFamide gene transcript in
RT the brain.";
RL J. Neurosci. 12:1033-1039(1992).
RN [4]
RP PROTEIN SEQUENCE OF 82-103 (PN).
RC TISSUE=CNS;
RX PubMed=7904219; DOI=10.1111/j.1460-9568.1993.tb00952.x;
RA Santama N., Li K.W., Bright K.E., Yeoman M., Geraerts W.P.M.,
RA Benjamin P.R., Burke J.F.;
RT "Processing of the FMRFamide precursor protein in the snail Lymnaea
RT stagnalis: characterization and neuronal localization of a novel peptide,
RT 'SEEPLY'.";
RL Eur. J. Neurosci. 5:1003-1016(1993).
CC -!- FUNCTION: FMRFamide induces contractions in visceral and somatic
CC musculature as well as in the heart. May play a role as cotransmitters
CC or modulators in a number of significant neuronal systems.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Isoform 1 and isoform 2 only share the N-terminal signal
CC sequence.;
CC Name=1; Synonyms=FMRFamide;
CC IsoId=P19802-1; Sequence=Displayed;
CC Name=2; Synonyms=FMRFamide-related;
CC IsoId=P42565-1; Sequence=External;
CC Name=3;
CC IsoId=P19802-2; Sequence=VSP_001564;
CC -!- TISSUE SPECIFICITY: Expressed in 280 cells of the CNS including the EGP
CC heart excitatory motoneurons.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000305}.
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DR EMBL; M37629; AAA63280.1; -; mRNA.
DR EMBL; M87479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S38686; AAB21767.1; -; mRNA.
DR EMBL; S94982; AAB21764.1; -; Genomic_DNA.
DR PIR; A37016; A37016.
DR PIR; F44840; F44840.
DR AlphaFoldDB; P19802; -.
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; 13.
PE 1: Evidence at protein level;
KW Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Neuropeptide; Repeat; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT PROPEP 36..37
FT /id="PRO_0000009668"
FT PEPTIDE 40..43
FT /note="FLRF-amide 1"
FT /id="PRO_0000009669"
FT PROPEP 46..56
FT /id="PRO_0000009670"
FT PEPTIDE 59..63
FT /note="QFYRI-amide"
FT /id="PRO_0000009671"
FT PROPEP 66..73
FT /id="PRO_0000009672"
FT PEPTIDE 76..79
FT /note="FLRF-amide 2"
FT /id="PRO_0000009673"
FT PEPTIDE 82..103
FT /note="PN"
FT /id="PRO_0000009674"
FT PROPEP 108..149
FT /id="PRO_0000009675"
FT PEPTIDE 152..155
FT /note="FMRF-amide 1"
FT /id="PRO_0000009676"
FT PROPEP 158..163
FT /id="PRO_0000009677"
FT PEPTIDE 166..169
FT /note="FMRF-amide 2"
FT /id="PRO_0000009678"
FT PROPEP 171..172
FT /id="PRO_0000009679"
FT PEPTIDE 173..176
FT /note="FMRF-amide 3"
FT /id="PRO_0000009680"
FT PROPEP 179..184
FT /id="PRO_0000009681"
FT PEPTIDE 187..190
FT /note="FMRF-amide 4"
FT /id="PRO_0000009682"
FT PEPTIDE 194..197
FT /note="FMRF-amide 5"
FT /id="PRO_0000009683"
FT PROPEP 200..204
FT /id="PRO_0000009684"
FT PEPTIDE 207..210
FT /note="FMRF-amide 6"
FT /id="PRO_0000009685"
FT PROPEP 213..217
FT /id="PRO_0000009686"
FT PEPTIDE 220..223
FT /note="FMRF-amide 7"
FT /id="PRO_0000009687"
FT PROPEP 226..251
FT /id="PRO_0000009688"
FT PEPTIDE 254..257
FT /note="FMRF-amide 8"
FT /id="PRO_0000009689"
FT PROPEP 260..263
FT /id="PRO_0000009690"
FT PEPTIDE 266..269
FT /note="FMRF-amide 9"
FT /id="PRO_0000009691"
FT PROPEP 272..278
FT /id="PRO_0000009692"
FT PEPTIDE 281..285
FT /note="EFLRI-amide"
FT /id="PRO_0000009693"
FT PROPEP 289..306
FT /id="PRO_0000009694"
FT REGION 104..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 63
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 79
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 155
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 169
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 176
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 190
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 197
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 210
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 223
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 257
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 269
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT MOD_RES 285
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:1968092"
FT VAR_SEQ 1..36
FT /note="MKTWSHVALLACLSIKWLTCVMADSIYCDDPDMCSM -> MYSPTLIVCLSF
FT FHSAVTKRFLRFGRALDTT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001564"
FT CONFLICT 91
FT /note="L -> P (in Ref. 1; AAA63280)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="E -> Q (in Ref. 1; AAA63280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 36351 MW; AB2361EFF2C4EF18 CRC64;
MKTWSHVALL ACLSIKWLTC VMADSIYCDD PDMCSMTKRF LRFGRALDTT DPFIRLRRQF
YRIGRGGYQP YQDKRFLRFG RSEQPDVDDY LRDVVLQSEE PLYRKRRSTE AGGQSEEMTH
RTARSAPEPA AENREIMKRE TGAEDLDEEK RFMRFGRGDE EAEKRFMRFG KSFMRFGRDM
SDVDKRFMRF GKRFMRFGRE PGTDKRFMRF GREPGADKRF MRFGKSFDGE EENDDDLYYN
ESDADSNDDV DKRFMRFGKS AEEKRFMRFG KSEDASRDKK EFLRIGKRES RSAEVENNIQ
IAAKQS
