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ELHA_APLCA
ID   ELHA_APLCA              Reviewed;         173 AA.
AC   P01360; P11923;
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=Atrial gland and califin peptides;
DE   AltName: Full=ELH-18;
DE   Contains:
DE     RecName: Full=Atrial gland peptide A;
DE   Contains:
DE     RecName: Full=Califin-A;
DE   Contains:
DE     RecName: Full=Califin-A large subunit;
DE   Contains:
DE     RecName: Full=Califin-A small subunit;
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 [GENOMIC DNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [3]
RP   PROTEIN SEQUENCE OF 36-69 (PEPTIDE A).
RX   PubMed=6929554; DOI=10.1073/pnas.77.4.2328;
RA   Heller E., Kaczmarek L.K., Hunkapiller M.W., Hood L.E., Strumwasser F.;
RT   "Purification and primary structure of two neuroactive peptides that cause
RT   bag cell afterdischarge and egg-laying in Aplysia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:2328-2332(1980).
RN   [4]
RP   PROTEIN SEQUENCE OF 117-173 (CALIFIN A), AND AMIDATION AT LEU-152.
RC   TISSUE=Atrial gland;
RX   PubMed=3753705; DOI=10.1016/s0021-9258(17)35984-7;
RA   Rothman B.S., Hawke D.H., Brown R.O., Lee T.D., Dehghan A.A., Shively J.E.,
RA   Mayeri E.;
RT   "Isolation and primary structure of the califins, three biologically active
RT   egg-laying hormone-like peptides from the atrial gland of Aplysia
RT   californica.";
RL   J. Biol. Chem. 261:1616-1623(1986).
RN   [5]
RP   PROTEIN SEQUENCE OF 22-34; 131-152 AND 156-173, AND AMIDATION AT ILE-69.
RX   PubMed=3379066; DOI=10.1016/s0021-9258(19)76529-6;
RA   Nagle G.T., Painter S.D., Blankenship J.E., Kurosky A.;
RT   "Proteolytic processing of egg-laying hormone-related precursors in
RT   Aplysia. Identification of peptide regions critical for biological
RT   activity.";
RL   J. Biol. Chem. 263:9223-9237(1988).
CC   -!- FUNCTION: The atrial gland peptide A and peptide B precursors are the
CC       source of the 2 peptides that, upon release from this reproductive
CC       system gland, initiate the egg-laying process by exciting the bag cell
CC       neurons. These neurons, clustered in neural connectives near the
CC       abdominal ganglion, in turn release other peptides that act directly on
CC       the ganglion and also, via the circulating hemolymph, on many other
CC       organs to control the physiological processes of egg-laying. One of
CC       these other peptides is the egg-laying hormone.
CC   -!- FUNCTION: Injected in sexually mature animals califin A excites LB and
CC       LC cells of the abdominal ganglion and causes egg-laying.
CC   -!- SUBUNIT: Califin A consists of a 36-residue large subunit bound by a
CC       single disulfide bond to a 18-residue small subunit.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the molluscan ELH family. {ECO:0000305}.
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DR   EMBL; M29350; AAA27750.1; -; Genomic_DNA.
DR   EMBL; J01017; AAA27742.1; -; Genomic_DNA.
DR   PIR; A01630; GOGAAA.
DR   AlphaFoldDB; P01360; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR003424; ELH.
DR   Pfam; PF02323; ELH; 2.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Neuropeptide; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000305|PubMed:3379066"
FT   PROPEP          22..34
FT                   /id="PRO_0000001800"
FT   PEPTIDE         36..69
FT                   /note="Atrial gland peptide A"
FT                   /id="PRO_0000001801"
FT   PROPEP          73..114
FT                   /id="PRO_0000001802"
FT   CHAIN           117..173
FT                   /note="Califin-A"
FT                   /id="PRO_0000001803"
FT   PEPTIDE         117..152
FT                   /note="Califin-A large subunit"
FT                   /id="PRO_0000001804"
FT   PEPTIDE         156..173
FT                   /note="Califin-A small subunit"
FT                   /id="PRO_0000001805"
FT   REGION          75..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         69
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:3379066"
FT   MOD_RES         152
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:3753705"
FT   DISULFID        141..172
FT   CONFLICT        172..173
FT                   /note="CS -> PQLKTISNLLD (in Ref. 2; AAA27750)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   173 AA;  19283 MW;  E71D0A340427B0B6 CRC64;
     MKANTMFIIL CLSLSTLCVS SQSTSVHGKI FVPNRAVKLS SDGNYPFDLS KEDGAQPYFM
     TPRLRFYPIG KRAAGEMEQS EGQNPETKSH SWRKRSVLTP SLSSLGESLE SGISKRISIN
     QDLKAITDML LTEQIQARRR CLDALRQRLL DLGKRDSDVS LFNGDLLPNG RCS
 
 
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