ELH1_APLCA
ID ELH1_APLCA Reviewed; 271 AA.
AC P01362; Q24868; Q99261; Q99264; Q99265; Q99266; Q99267;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=ELH;
DE Contains:
DE RecName: Full=Beta-bag cell peptide;
DE Short=Beta-BCP;
DE Contains:
DE RecName: Full=Gamma-delta-bag cell peptide;
DE Contains:
DE RecName: Full=Gamma-bag cell peptide;
DE Short=Gamma-BCP;
DE Contains:
DE RecName: Full=Delta-bag cell peptide;
DE Contains:
DE RecName: Full=Delta-bag cell peptide(1-36);
DE Contains:
DE RecName: Full=Alpha-bag cell peptide;
DE Short=Alpha-BCP;
DE Contains:
DE RecName: Full=Alpha-bag cell peptide(1-8);
DE Contains:
DE RecName: Full=Alpha-bag cell peptide(1-7);
DE Contains:
DE RecName: Full=Epsilon-bag cell peptide;
DE Contains:
DE RecName: Full=Epsilon-bag cell peptide(4-19);
DE Contains:
DE RecName: Full=Egg-laying hormone;
DE Short=ELH;
DE Contains:
DE RecName: Full=Egg-laying hormone(1-29);
DE Contains:
DE RecName: Full=Egg-laying hormone(1-14);
DE Contains:
DE RecName: Full=Egg-laying hormone(15-36);
DE Contains:
DE RecName: Full=Egg-laying hormone(30-36);
DE Contains:
DE RecName: Full=Acidic peptide;
DE Contains:
DE RecName: Full=Acidic peptide(1-20);
DE Contains:
DE RecName: Full=Acidic peptide(7-27);
DE Contains:
DE RecName: Full=Acidic peptide(8-27);
DE Contains:
DE RecName: Full=Acidic peptide(9-27);
DE Contains:
DE RecName: Full=Acidic peptide(9-26);
DE Contains:
DE RecName: Full=Acidic peptide(9-20);
DE Flags: Precursor;
OS Aplysia californica (California sea hare).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC Aplysiidae; Aplysia.
OX NCBI_TaxID=6500;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX PubMed=6687446; DOI=10.1016/0092-8674(83)90492-0;
RA Scheller R.H., Jackson J.F., McAllister L.B., Rothman B.S., Mayeri E.,
RA Axel R.;
RT "A single gene encodes multiple neuropeptides mediating a stereotyped
RT behavior.";
RL Cell 32:7-22(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP MET-26; ALA-43; TYR-62; GLU-63; GLN-64; LEU-75; ILE-119; GLU-140; ALA-143;
RP GLU-165 AND PRO-236.
RC TISSUE=Abdominal ganglion, and Atrial gland;
RX PubMed=4020422; DOI=10.1523/jneurosci.05-07-01872.1985;
RA Mahon A.C., Nambu J.R., Taussig R., Shyamala M., Roach A., Scheller R.H.;
RT "Structure and expression of the egg-laying hormone gene family in
RT Aplysia.";
RL J. Neurosci. 5:1872-1880(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Ring ganglion;
RX PubMed=3708345; DOI=10.1016/0006-8993(86)90809-7;
RA Shyamala M., Nambu J.R., Scheller R.H.;
RT "Expression of the egg-laying hormone gene family in the head ganglia of
RT Aplysia.";
RL Brain Res. 371:49-57(1986).
RN [4]
RP PROTEIN SEQUENCE OF 150-158.
RX PubMed=16593372; DOI=10.1073/pnas.80.18.5753;
RA Rothman B.S., Mayeri E., Brown R.O., Yuan P.-M., Shively J.E.;
RT "Primary structure and neuronal effects of alpha-bag cell peptide, a second
RT candidate neurotransmitter encoded by a single gene in bag cell neurons of
RT Aplysia.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:5753-5757(1983).
RN [5]
RP PROTEIN SEQUENCE OF 206-241.
RC TISSUE=Bag cell;
RX PubMed=293751; DOI=10.1073/pnas.76.12.6656;
RA Chiu A.Y., Hunkapiller M.W., Heller E., Stuart D.K., Hood L.E.,
RA Strumwasser F.;
RT "Purification and primary structure of the neuropeptide egg-laying hormone
RT of Aplysia californica.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:6656-6660(1979).
RN [6]
RP PROTEOLYTIC PROCESSING.
RX PubMed=3549995; DOI=10.1523/jneurosci.07-03-00854.1987;
RA Newcomb R., Scheller R.H.;
RT "Proteolytic processing of the Aplysia egg-laying hormone and R3-14
RT neuropeptide precursors.";
RL J. Neurosci. 7:854-863(1987).
RN [7]
RP PROTEOLYTIC PROCESSING, AMIDATION AT LYS-241, AND MASS SPECTROMETRY.
RX PubMed=9520477; DOI=10.1073/pnas.95.7.3972;
RA Garden R.W., Shippy S.A., Li L., Moroz T.P., Sweedler J.V.;
RT "Proteolytic processing of the Aplysia egg-laying hormone prohormone.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3972-3977(1998).
CC -!- FUNCTION: ELH acts as a neurotransmitter locally, upon neurons of the
CC abdominal ganglion and as a hormone by diffusing into the circulating
CC hemolymph and modulating the activity of other organs. It specifically
CC causes contraction of smooth muscle in the ovotestis and expulsion of
CC the egg string.
CC -!- FUNCTION: Alpha-BCP decreases the activity of a cluster of neurons in
CC the left upper quadrant of the abdominal ganglion.
CC -!- FUNCTION: Beta-BCP specifically excites 2 neurons, L1 and R1, in the
CC abdominal ganglion.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P01362-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P01362-2; Sequence=VSP_025432, VSP_025433;
CC -!- TISSUE SPECIFICITY: Bag cell neurons.
CC -!- MASS SPECTROMETRY: [Beta-bag cell peptide]: Mass=728.39; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Gamma-bag cell peptide]: Mass=706.36; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Gamma-delta-bag cell peptide]: Mass=5410.11;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Delta-bag cell peptide(1-36)]: Mass=4024.98;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Delta-bag cell peptide]: Mass=4409.16;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Alpha-bag cell peptide(1-7)]: Mass=922.51;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Alpha-bag cell peptide(1-8)]: Mass=1009.55;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Alpha-bag cell peptide]: Mass=1122.64;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Epsilon-bag cell peptide]: Mass=1862.75;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Epsilon-bag cell peptide(4-19)]: Mass=1563.81;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Egg-laying hormone(1-14)]: Mass=1574.86;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Egg-laying hormone(1-29)]: Mass=3461.0;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Egg-laying hormone(15-36)]: Mass=2826.64;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Egg-laying hormone(30-36)]: Mass=941.51;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Acidic peptide(1-20)]: Mass=2304.20; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Acidic peptide]: Mass=2961.31; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Acidic peptide(9-20)]: Mass=1559.80; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Acidic peptide(9-26)]: Mass=2100.14; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Acidic peptide(9-27)]: Mass=2215.20; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Acidic peptide(8-27)]: Mass=2316.24; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Acidic peptide(7-27)]: Mass=2429.32; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- MASS SPECTROMETRY: [Egg-laying hormone]: Mass=4385.15; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9520477};
CC -!- SIMILARITY: Belongs to the molluscan ELH family. {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; M29345; AAA27747.1; -; Genomic_DNA.
DR EMBL; M29347; AAA27748.1; -; mRNA.
DR EMBL; M29346; AAA27749.1; -; mRNA.
DR EMBL; M29348; AAA62575.1; -; mRNA.
DR EMBL; M29349; AAA62576.1; -; mRNA.
DR EMBL; M25886; AAA62580.1; -; mRNA.
DR PIR; A90833; ONGAPA.
DR RefSeq; NP_001191670.1; NM_001204741.1.
DR AlphaFoldDB; P01362; -.
DR SMR; P01362; -.
DR GeneID; 100533533; -.
DR CTD; 100533533; -.
DR OrthoDB; 1922216at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR003424; ELH.
DR Pfam; PF02323; ELH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW Direct protein sequencing; Hormone; Neuropeptide; Secreted; Signal.
FT SIGNAL 1..28
FT PROPEP 29..95
FT /id="PRO_0000001813"
FT PEPTIDE 96..100
FT /note="Beta-bag cell peptide"
FT /id="PRO_0000001814"
FT PEPTIDE 103..148
FT /note="Gamma-delta-bag cell peptide"
FT /id="PRO_0000287290"
FT PEPTIDE 103..107
FT /note="Gamma-bag cell peptide"
FT /id="PRO_0000001815"
FT PEPTIDE 110..148
FT /note="Delta-bag cell peptide"
FT /id="PRO_0000001816"
FT PEPTIDE 110..145
FT /note="Delta-bag cell peptide(1-36)"
FT /id="PRO_0000287291"
FT PEPTIDE 150..158
FT /note="Alpha-bag cell peptide"
FT /id="PRO_0000001817"
FT PEPTIDE 150..157
FT /note="Alpha-bag cell peptide(1-8)"
FT /id="PRO_0000287292"
FT PEPTIDE 150..156
FT /note="Alpha-bag cell peptide(1-7)"
FT /id="PRO_0000287293"
FT PROPEP 162..184
FT /id="PRO_0000001818"
FT PEPTIDE 185..203
FT /note="Epsilon-bag cell peptide"
FT /id="PRO_0000287294"
FT PEPTIDE 188..203
FT /note="Epsilon-bag cell peptide(4-19)"
FT /id="PRO_0000287295"
FT PEPTIDE 206..241
FT /note="Egg-laying hormone"
FT /id="PRO_0000001819"
FT PEPTIDE 206..234
FT /note="Egg-laying hormone(1-29)"
FT /id="PRO_0000287296"
FT PEPTIDE 206..219
FT /note="Egg-laying hormone(1-14)"
FT /id="PRO_0000287297"
FT PEPTIDE 220..241
FT /note="Egg-laying hormone(15-36)"
FT /id="PRO_0000287298"
FT PEPTIDE 235..241
FT /note="Egg-laying hormone(30-36)"
FT /id="PRO_0000287299"
FT PEPTIDE 245..271
FT /note="Acidic peptide"
FT /id="PRO_0000001820"
FT PEPTIDE 245..265
FT /note="Acidic peptide(1-20)"
FT /id="PRO_0000287300"
FT PEPTIDE 251..271
FT /note="Acidic peptide(7-27)"
FT /id="PRO_0000287301"
FT PEPTIDE 252..271
FT /note="Acidic peptide(8-27)"
FT /id="PRO_0000287302"
FT PEPTIDE 253..271
FT /note="Acidic peptide(9-27)"
FT /id="PRO_0000287303"
FT PEPTIDE 253..270
FT /note="Acidic peptide(9-26)"
FT /id="PRO_0000287304"
FT PEPTIDE 253..265
FT /note="Acidic peptide(9-20)"
FT /id="PRO_0000287305"
FT REGION 162..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 241
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:9520477"
FT VAR_SEQ 23..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:4020422"
FT /id="VSP_025432"
FT VAR_SEQ 84
FT /note="D -> H (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:4020422"
FT /id="VSP_025433"
FT VARIANT 26
FT /note="S -> M"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 43
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 62
FT /note="S -> Y"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 63
FT /note="G -> E"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 64
FT /note="E -> Q"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 75
FT /note="F -> L"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 119
FT /note="F -> I"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 140
FT /note="D -> E"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 143
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 165
FT /note="G -> E"
FT /evidence="ECO:0000269|PubMed:4020422"
FT VARIANT 236
FT /note="Q -> P"
FT /evidence="ECO:0000269|PubMed:4020422"
FT CONFLICT 3
FT /note="R -> C (in Ref. 3; AAA62580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 30827 MW; FB2F1EBE3B9113A6 CRC64;
MKRPNNRPTN TMSLILCLTL SSLCVSSQSA SVHGKNFATN RAVKSSSPFV VLSPDDNVVS
MSGENGYRSA LREAFDKSSR DYDDNGEDVF SNEKRRLRFH KRRLRFDRRD QDEGNFRRFP
TNAVSMSADE NSPFDLSNED GAVYQRDLRA PRLRFYSLRK RAAGGMEQSE GQNPETESHS
RRKRSVLTPS LSSLGESLES GISKRISINQ DLKAITDMLL TEQIRERQRY LADLRQRLLE
KGKRSSGVSL LTSNKDEEQR ELLKAISNLL D
