ARNP_MYTED
ID ARNP_MYTED Reviewed; 196 AA.
AC Q25461;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=APGW-amide-related neuropeptide {ECO:0000303|PubMed:10799681, ECO:0000303|PubMed:8852595};
DE Contains:
DE RecName: Full=RPGW-amide {ECO:0000303|PubMed:10799681, ECO:0000303|PubMed:8852595};
DE Contains:
DE RecName: Full=KPGW-amide {ECO:0000303|PubMed:10799681, ECO:0000303|PubMed:8852595};
DE Contains:
DE RecName: Full=TPGW-amide {ECO:0000303|PubMed:10799681, ECO:0000303|PubMed:8852595};
DE Flags: Precursor;
OS Mytilus edulis (Blue mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=6550;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA63116.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Cerebral ganglion {ECO:0000269|PubMed:8852595};
RX PubMed=8852595; DOI=10.1016/0304-3940(96)12390-9;
RA Favrel P., Mathieu M.;
RT "Molecular cloning of a cDNA encoding the precursor of APGWamide related
RT neuropeptides from the bivalve mollusc Mytilus edulis.";
RL Neurosci. Lett. 205:210-214(1996).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AMIDATION AT TRP-54; TRP-74; TRP-94; TRP-111;
RP TRP-135; TRP-151 AND TRP-158, AND MASS SPECTROMETRY.
RX PubMed=10799681; DOI=10.1016/s0006-8993(00)02108-9;
RA Henry J., Zatylny C., Favrel P.;
RT "HPLC and electrospray ionization mass spectrometry as tools for the
RT identification of APGWamide-related peptides in gastropod and bivalve
RT mollusks: comparative activities on Mytilus muscles.";
RL Brain Res. 862:162-170(2000).
CC -!- FUNCTION: RPGW-amide, KPGW-amide and TPGW-amide tetrapeptides are
CC involved in control of muscle contraction and may function as
CC neurotransmitters. These peptides increase tension of the pedal
CC retractor muscle and, in conjunction with FMRF-amide, increase peak
CC tension of the anterior byssus retractor muscle (ABRM).
CC {ECO:0000269|PubMed:10799681}.
CC -!- TISSUE SPECIFICITY: Expressed in cerebral, pedal and visceral ganglia.
CC TPGW-amide is found in pedal and cerebral ganglia and in shell adductor
CC muscle (at protein level). RPGW-amide and KPGW-amide are found in pedal
CC retractor muscle, ABRM and shell adductor muscle (at protein level).
CC {ECO:0000269|PubMed:10799681, ECO:0000269|PubMed:8852595}.
CC -!- MASS SPECTROMETRY: [RPGW-amide]: Mass=514.2; Method=Electrospray;
CC Note=The measured mass is that of RPGW-amide.;
CC Evidence={ECO:0000269|PubMed:10799681};
CC -!- MASS SPECTROMETRY: [KPGW-amide]: Mass=486.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10799681};
CC -!- MASS SPECTROMETRY: [TPGW-amide]: Mass=459.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10799681};
CC -!- MISCELLANEOUS: Tetrapeptides may be further processed to GW-amide,
CC which is found in cerebral and pedal ganglia, by a dipeptidyl
CC aminopeptidase. {ECO:0000269|PubMed:10799681}.
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DR EMBL; X92372; CAA63116.1; -; mRNA.
DR AlphaFoldDB; Q25461; -.
DR SMR; Q25461; -.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Neuropeptide; Repeat;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255, ECO:0000305"
FT PROPEP 23..48
FT /evidence="ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391442"
FT PEPTIDE 51..54
FT /note="RPGW-amide"
FT /evidence="ECO:0000269|PubMed:10799681,
FT ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391443"
FT PROPEP 58..68
FT /evidence="ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391444"
FT PEPTIDE 71..74
FT /note="RPGW-amide"
FT /evidence="ECO:0000269|PubMed:10799681,
FT ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391445"
FT PROPEP 78..88
FT /evidence="ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391446"
FT PEPTIDE 91..94
FT /note="RPGW-amide"
FT /evidence="ECO:0000269|PubMed:10799681,
FT ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391447"
FT PROPEP 98..105
FT /evidence="ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391448"
FT PEPTIDE 108..111
FT /note="KPGW-amide"
FT /evidence="ECO:0000269|PubMed:10799681,
FT ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391449"
FT PROPEP 115..129
FT /evidence="ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391450"
FT PEPTIDE 132..135
FT /note="RPGW-amide"
FT /evidence="ECO:0000269|PubMed:10799681,
FT ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391451"
FT PROPEP 139..146
FT /evidence="ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391452"
FT PEPTIDE 148..151
FT /note="RPGW-amide"
FT /evidence="ECO:0000269|PubMed:10799681,
FT ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391453"
FT PEPTIDE 155..158
FT /note="TPGW-amide"
FT /evidence="ECO:0000269|PubMed:10799681,
FT ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391454"
FT PROPEP 162..196
FT /evidence="ECO:0000269|PubMed:8852595"
FT /id="PRO_0000391455"
FT MOD_RES 54
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:10799681"
FT MOD_RES 74
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:10799681"
FT MOD_RES 94
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:10799681"
FT MOD_RES 111
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:10799681"
FT MOD_RES 135
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:10799681"
FT MOD_RES 151
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:10799681"
FT MOD_RES 158
FT /note="Tryptophan amide"
FT /evidence="ECO:0000269|PubMed:10799681"
SQ SEQUENCE 196 AA; 22716 MW; A552F5468FFBE6A4 CRC64;
METLNIFLVI FSLLGTIIIA SSSDESSERK KRDLDTIDDT NNDFLTADKR RPGWGKRSFD
DDILNNLDKR RPGWGKRSDM LFDSEEIEKR RPGWGKRSSS LYDDEKRKPG WGKRSSALLD
DLSLYNSIVK RRPGWGKRSD TFKVDIRRPG WGKRTPGWGK RSGPNMCMDF QDEILQLYKL
LNEAEKLHSE CEALNI
