FARX_LYMST
ID FARX_LYMST Reviewed; 360 AA.
AC P42565;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=FMRFamide-related neuropeptides;
DE Contains:
DE RecName: Full=EFFPL-amide;
DE Contains:
DE RecName: Full=GDPFLRF-amide 1;
DE Contains:
DE RecName: Full=GDPFLRF-amide 2;
DE Contains:
DE RecName: Full=GDPFLRF-amide 3;
DE Contains:
DE RecName: Full=GDPFLRF-amide 4;
DE Contains:
DE RecName: Full=GDPFLRF-amide 5;
DE Contains:
DE RecName: Full=GDPFLRF-amide 6;
DE Contains:
DE RecName: Full=GDPFLRF-amide 7;
DE Contains:
DE RecName: Full=SDPFLRF-amide 1;
DE Contains:
DE RecName: Full=SDPFLRF-amide 2;
DE Contains:
DE RecName: Full=SDPFLRF-amide 3;
DE Contains:
DE RecName: Full=SDPFLRF-amide 4;
DE Contains:
DE RecName: Full=SDPFLRF-amide 5;
DE Contains:
DE RecName: Full=SDPFLRF-amide 6;
DE Contains:
DE RecName: Full=SDPYLRF-amide;
DE Contains:
DE RecName: Full=SDPFFRF-amide;
DE Contains:
DE RecName: Full=SKPYMRF-amide;
DE Contains:
DE RecName: Full=SSFPRY-amide;
DE Contains:
DE RecName: Full=HDYMRF-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-77; PHE-86; PHE-95;
RP PHE-104; PHE-113; PHE-122; PHE-131; PHE-140; PHE-149; PHE-158; PHE-167;
RP PHE-176; PHE-185; PHE-194; PHE-203; PHE-282; TYR-323 AND PHE-336.
RC TISSUE=CNS;
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 [2]
RP PARTIAL NUCLEOTIDE SEQUENCE.
RX PubMed=2002360; DOI=10.1523/jneurosci.11-03-00740.1991;
RA Saunders S.E., Bright K., Kellett E., Benjamin P.R., Burke J.F.;
RT "Neuropeptides Gly-Asp-Pro-Phe-Leu-Arg-Phe-amide (GDPFLRFamide) and Ser-
RT Asp-Pro-Phe-Leu-Arg-Phe-amide (SDPFLRFamide) are encoded by an exon 3' to
RT Phe-Met-Arg-Phe-NH2 (FMRFamide) in the snail Lymnaea stagnalis.";
RL J. Neurosci. 11:740-745(1991).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE.
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 276-282 (SKPYMRF-AMIDE), AND AMIDATION AT PHE-203.
RX PubMed=1421117; DOI=10.1097/00001756-199207000-00017;
RA de With N.D., van der Schors R.C.;
RT "SKPYMRFamide, a novel FMRFamide-related peptide in the snail Lymnaea
RT stagnalis.";
RL NeuroReport 3:612-614(1992).
CC -!- FUNCTION: SDPFLRF-amide inhibits neurons.
CC -!- FUNCTION: SKPYMRF-amide excites neurons.
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=2; Synonyms=FMRFamide-related;
CC IsoId=P42565-1; Sequence=Displayed;
CC Name=1; Synonyms=FMRFamide;
CC IsoId=P19802-1; Sequence=External;
CC Name=3;
CC IsoId=P19802-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in 57 cells including a cardiorespiratory
CC cell and the visceral white interneuron (VWI).
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U03137; AAA62864.1; -; mRNA.
DR EMBL; S38684; AAB21765.1; -; mRNA.
DR PIR; G44840; G44840.
DR AlphaFoldDB; P42565; -.
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 InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF01581; FARP; 17.
DR SUPFAM; SSF51120; SSF51120; 1.
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..43
FT /id="PRO_0000009695"
FT PEPTIDE 44..48
FT /note="EFFPL-amide"
FT /id="PRO_0000009696"
FT PROPEP 49..70
FT /id="PRO_0000009697"
FT PEPTIDE 71..77
FT /note="GDPFLRF-amide 1"
FT /id="PRO_0000009698"
FT PEPTIDE 80..86
FT /note="GDPFLRF-amide 2"
FT /id="PRO_0000009699"
FT PEPTIDE 89..95
FT /note="GDPFLRF-amide 3"
FT /id="PRO_0000009700"
FT PEPTIDE 98..104
FT /note="GDPFLRF-amide 4"
FT /id="PRO_0000009701"
FT PROPEP 106
FT /id="PRO_0000009702"
FT PEPTIDE 107..113
FT /note="SDPFLRF-amide 1"
FT /id="PRO_0000009703"
FT PEPTIDE 116..122
FT /note="GDPFLRF-amide 5"
FT /id="PRO_0000009704"
FT PEPTIDE 125..131
FT /note="GDPFLRF-amide 6"
FT /id="PRO_0000009705"
FT PEPTIDE 134..140
FT /note="SDPFLRF-amide 2"
FT /id="PRO_0000009706"
FT PEPTIDE 143..149
FT /note="SDPFLRF-amide 3"
FT /id="PRO_0000009707"
FT PEPTIDE 152..158
FT /note="SDPFLRF-amide 4"
FT /id="PRO_0000009708"
FT PEPTIDE 161..167
FT /note="SDPFLRF-amide 5"
FT /id="PRO_0000009709"
FT PEPTIDE 170..176
FT /note="SDPFLRF-amide 6"
FT /id="PRO_0000009710"
FT PEPTIDE 179..185
FT /note="SDPYLRF-amide"
FT /id="PRO_0000009711"
FT PEPTIDE 188..194
FT /note="GDPFLRF-amide 7"
FT /id="PRO_0000009712"
FT PEPTIDE 197..203
FT /note="SDPFFRF-amide"
FT /id="PRO_0000009713"
FT PROPEP 205..275
FT /evidence="ECO:0000269|PubMed:1421117"
FT /id="PRO_0000009714"
FT PEPTIDE 276..282
FT /note="SKPYMRF-amide"
FT /id="PRO_0000009715"
FT PROPEP 284..317
FT /id="PRO_0000009716"
FT PEPTIDE 318..323
FT /note="SSFPRY-amide"
FT /id="PRO_0000009717"
FT PROPEP 327..330
FT /id="PRO_0000009718"
FT PEPTIDE 331..336
FT /note="HDYMRF-amide"
FT /id="PRO_0000009719"
FT PROPEP 338..360
FT /id="PRO_0000009720"
FT REGION 227..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 86
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 95
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 104
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 113
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 122
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 131
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 140
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 149
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 158
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 167
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 176
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 185
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 194
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 203
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:1421117,
FT ECO:0000269|PubMed:7965060"
FT MOD_RES 282
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 323
FT /note="Tyrosine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
FT MOD_RES 336
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:7965060"
SQ SEQUENCE 360 AA; 41785 MW; 1593084FAE6542D2 CRC64;
MKTWSHVALL ACLSIKWLTC VMADSIYCDD PDMCSNSVDL DRKEFFPLGR HDGVYQTPEE
DGDLEDRQTR GDPFLRFGRG DPFLRFGRGD PFLRFGRGDP FLRFGQSDPF LRFGRGDPFL
RFGRGDPFLR FGKSDPFLRF GRSDPFLRFG RSDPFLRFGK SDPFLRFGKS DPFLRFGKSD
PYLRFGRGDP FLRFGRSDPF FRFGKQQVAT DDSGELDDEI LSRVSDDDKN IRRKRSTDSA
ENAHTRHERE ASAPRAKGKV GEVKSSDDFQ SREIRSKPYM RFGRNNLNNY ALEDEDCKLT
SDIIDDQFQR YQRGPSRSSF PRYGKRQDKR HDYMRFGRTS GGDFMGYDKS PENVGAEQSR