FAR2_CORAP
ID FAR2_CORAP Reviewed; 346 AA.
AC P41870;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=FMRFamide-related peptides type HF-1;
DE AltName: Full=TetraFaRP;
DE Contains:
DE RecName: Full=QFYRF-amide;
DE Contains:
DE RecName: Full=FLRF-amide;
DE Contains:
DE RecName: Full=FMRF-amide;
DE Flags: Precursor;
OS Cornu aspersum (Brown garden snail) (Helix aspersa).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC Helicina; Helicoidea; Helicidae; Cornu; Cornu.
OX NCBI_TaxID=6535;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-115; PHE-209; PHE-216;
RP PHE-232; PHE-249; PHE-256; PHE-273; PHE-290; PHE-307; PHE-314; PHE-331 AND
RP PHE-338.
RC TISSUE=Ganglion;
RX PubMed=19912881; DOI=10.1016/1044-7431(92)90049-8;
RA Lutz E.M., Macdonald M., Hettle S., Price D.A., Cottrell G.A.,
RA Sommerville J.;
RT "Structure of cDNA clones and genomic DNA FMRFamide-related peptides
RT (FaRPs) in Helix.";
RL Mol. Cell. Neurosci. 3:373-382(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-51 AND PHE-100.
RA Price D.A., Doble K.E., Lesser W., Greenberg M.J., Cottrell G.A.,
RA Swiderek K.M., Lee T.D., Lutz E.M., Sommerville J.;
RT "Isolation of pQFYRFamide from snail ganglia.";
RL Abstr. - Soc. Neurosci. 0:0-0(1993).
RN [3]
RP PARTIAL PROTEIN SEQUENCE (FLRF-AMIDE AND FMRF-AMIDE).
RC TISSUE=Ganglion;
RX PubMed=1980513; DOI=10.1242/jeb.154.1.421;
RA Price D.A., Lesser W., Lee T.D., Doble K.E., Greenberg M.J.;
RT "Seven FMRFamide-related and two SCP-related cardioactive peptides from
RT Helix.";
RL J. Exp. Biol. 154:421-437(1990).
CC -!- FUNCTION: Can function as both cardioregulatory hormones and
CC transmitters and may regulate cardiovascular function.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Central nervous system.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000305}.
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DR EMBL; L20768; AAA57461.1; -; mRNA.
DR PIR; S77971; S77971.
DR AlphaFoldDB; P41870; -.
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; 15.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..45
FT /id="PRO_0000009582"
FT PEPTIDE 47..51
FT /note="QFYRF-amide"
FT /id="PRO_0000009583"
FT PROPEP 54..94
FT /id="PRO_0000009584"
FT PEPTIDE 96..100
FT /note="QFYRF-amide"
FT /id="PRO_0000009585"
FT PROPEP 103..109
FT /id="PRO_0000009586"
FT PEPTIDE 112..115
FT /note="FLRF-amide"
FT /id="PRO_0000009587"
FT PROPEP 118..203
FT /id="PRO_0000009588"
FT PEPTIDE 206..209
FT /note="FMRF-amide"
FT /id="PRO_0000009589"
FT PEPTIDE 213..216
FT /note="FMRF-amide"
FT /id="PRO_0000009590"
FT PROPEP 219..226
FT /id="PRO_0000009591"
FT PEPTIDE 229..232
FT /note="FMRF-amide"
FT /id="PRO_0000009592"
FT PROPEP 235..243
FT /id="PRO_0000009593"
FT PEPTIDE 246..249
FT /note="FMRF-amide"
FT /id="PRO_0000009594"
FT PEPTIDE 253..256
FT /note="FMRF-amide"
FT /id="PRO_0000009595"
FT PROPEP 259..267
FT /id="PRO_0000009596"
FT PEPTIDE 270..273
FT /note="FLRF-amide"
FT /id="PRO_0000009597"
FT PROPEP 276..283
FT /id="PRO_0000009598"
FT PEPTIDE 287..290
FT /note="FMRF-amide"
FT /id="PRO_0000009599"
FT PROPEP 293..301
FT /id="PRO_0000009600"
FT PEPTIDE 304..307
FT /note="FMRF-amide"
FT /id="PRO_0000009601"
FT PEPTIDE 311..314
FT /note="FMRF-amide"
FT /id="PRO_0000009602"
FT PROPEP 317..325
FT /id="PRO_0000009603"
FT PEPTIDE 328..331
FT /note="FMRF-amide"
FT /id="PRO_0000009604"
FT PEPTIDE 335..338
FT /note="FMRF-amide"
FT /id="PRO_0000009605"
FT PROPEP 341..346
FT /id="PRO_0000009606"
FT REGION 137..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 100
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 115
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 209
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 216
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 232
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 249
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 256
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 273
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 290
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 307
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 314
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 331
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
FT MOD_RES 338
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:19912881"
SQ SEQUENCE 346 AA; 41156 MW; E294F48B9A4FC794 CRC64;
MTSLCLTIAP AVLSLICLSS YGWAEDNNGI HTLDDGDNDP FFRHNRQFYR FGRAFVPLWD
NADDSLVRKN LLTHWSEFPL SPALSSSDVF SRNSRQFYRF GRSYPPYQDK RFLRFGRSHQ
PDIDEYLQAL NSDQALYRKR RSEDGDSKED GLNRVARSAD ANQQSKNTQS NKFGKDLQKR
ETKKEKLNAN DDLEILSNED DLEKKFMRFG KRFMRFGRGD EDESYDKRFM RFGKSLRHDQ
EFEKRFMRFG KRFMRFGRGD EDDAREEKRF LRFGKSSNED EDIKKRFMRF GKSGNEDGDV
DKRFMRFGKR FMRFGKSEKE DGDVDKRFMR FGKRFMRFGR GDSETS
