FULI_LISFU
ID FULI_LISFU Reviewed; 357 AA.
AC P35905;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Fulicin peptides;
DE Contains:
DE RecName: Full=Fulicin;
DE Contains:
DE RecName: Full=Fucilin gene-related peptide 1;
DE Short=FGRP-1;
DE Contains:
DE RecName: Full=Fucilin gene-related peptide 2;
DE Short=FGRP-2;
DE Contains:
DE RecName: Full=Fucilin gene-related peptide 3;
DE Short=FGRP-3;
DE Contains:
DE RecName: Full=Fucilin gene-related peptide 4;
DE Short=FGRP-4;
DE Contains:
DE RecName: Full=Fucilin gene-related peptide 5;
DE Short=FGRP-5;
DE Contains:
DE RecName: Full=Fucilin gene-related peptide 6;
DE Short=FGRP-6;
DE Contains:
DE RecName: Full=Fucilin gene-related peptide 7;
DE Short=FGRP-7;
DE Contains:
DE RecName: Full=Fucilin gene-related peptide 8;
DE Short=FGRP-8;
DE Contains:
DE RecName: Full=Fucilin gene-related peptide 9;
DE Short=FGRP-9;
DE Flags: Precursor;
OS Lissachatina fulica (Giant African land snail) (Achatina fulica).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC Helicina; Achatinoidea; Achatinidae; Lissachatina.
OX NCBI_TaxID=2315439;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ganglion;
RX PubMed=7722509; DOI=10.1046/j.1471-4159.1995.64052248.x;
RA Yasuda-Kamatani Y., Nakamura M., Minakata H., Nomoto K., Sakiyama F.;
RT "A novel cDNA sequence encoding the precursor of the D-amino acid-
RT containing neuropeptide fulicin and multiple alpha-amidated neuropeptides
RT from Achatina fulica.";
RL J. Neurochem. 64:2248-2255(1995).
RN [2]
RP PROTEIN SEQUENCE OF 122-126, D-AMINO ACID AT ASN-123, AND AMIDATION AT
RP VAL-126.
RC STRAIN=Ferussac; TISSUE=Ganglion;
RX PubMed=1859408; DOI=10.1016/0006-291x(91)90133-r;
RA Ohta N., Kubota I., Takao T., Shimonishi Y., Yasuda-Kamatani Y.,
RA Minakata H., Nomoto K., Muneoka Y., Kobayashi M.;
RT "Fulicin, a novel neuropeptide containing a D-amino acid residue isolated
RT from the ganglia of Achatina fulica.";
RL Biochem. Biophys. Res. Commun. 178:486-493(1991).
CC -!- FUNCTION: Potentiates tetanic contraction of the penis retractor muscle
CC at very low concentrations, and also shows modulatory actions on the
CC activity of the buccal and ventricular muscles and the central
CC ganglionic neurons.
CC -!- TISSUE SPECIFICITY: Found in central ganglia and the ventricles and
CC atria of the heart.
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; D13986; BAA03093.1; -; mRNA.
DR PIR; A44692; A44692.
DR AlphaFoldDB; P35905; -.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; D-amino acid;
KW Direct protein sequencing; Hormone; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..119
FT /id="PRO_0000021291"
FT PEPTIDE 122..126
FT /note="Fulicin"
FT /id="PRO_0000021292"
FT PROPEP 130..194
FT /id="PRO_0000021293"
FT PEPTIDE 197..201
FT /note="Fucilin gene-related peptide 1"
FT /id="PRO_0000021294"
FT PEPTIDE 205..209
FT /note="Fucilin gene-related peptide 2"
FT /id="PRO_0000021295"
FT PEPTIDE 213..217
FT /note="Fucilin gene-related peptide 3"
FT /id="PRO_0000021296"
FT PEPTIDE 221..226
FT /note="Fucilin gene-related peptide 4"
FT /id="PRO_0000021297"
FT PEPTIDE 230..233
FT /note="Fucilin gene-related peptide 5"
FT /id="PRO_0000021298"
FT PEPTIDE 237..242
FT /note="Fucilin gene-related peptide 6"
FT /id="PRO_0000021299"
FT PEPTIDE 246..250
FT /note="Fucilin gene-related peptide 7"
FT /id="PRO_0000021300"
FT PEPTIDE 254..259
FT /note="Fucilin gene-related peptide 8"
FT /id="PRO_0000021301"
FT PROPEP 263..298
FT /id="PRO_0000021302"
FT PEPTIDE 301..305
FT /note="Fucilin gene-related peptide 9"
FT /id="PRO_0000021303"
FT PROPEP 311..357
FT /id="PRO_0000021304"
FT MOD_RES 123
FT /note="D-asparagine"
FT /evidence="ECO:0000269|PubMed:1859408"
FT MOD_RES 126
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:1859408"
FT MOD_RES 201
FT /note="Valine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 209
FT /note="Valine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 217
FT /note="Leucine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 226
FT /note="Leucine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 233
FT /note="Isoleucine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 242
FT /note="Isoleucine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 250
FT /note="Valine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 259
FT /note="Valine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 305
FT /note="Leucine amide"
FT /evidence="ECO:0000255"
SQ SEQUENCE 357 AA; 40702 MW; E39B80FE3D51931D CRC64;
MQPTVLLILM TSCLTYQVIA DKPKGNHLHS RPERSPIVLF SDAPHAAASP ADENDNFPVL
KTANQYEDNN SATFSHLEEK HDFAEKQSTG DDEESVILNR VTGEVLSDTV DGSQGHLEPK
RFNEFVGKRN TLPEEAGSFD ADSQPGSLDT VRILAGLSNF GQPQIIDQGN MKNHRTLKNM
IHNLYNTMNE DEASKRQYEF VGKRSYDFVG KRTYDFLGKR SPYYFLGKRY DFIGKRSPYD
FIGKKNYDFV GKRSPYDFVG KRNQGVFTVS PSSTKISFDD NYLPYLSSVD AGDLSDVNKR
YAEFLGKRKR TAEQDETSQR SNERLVALLQ NTGFRKRLSR MLQNQRLVEH YPEFIGK
