ID   SENA_APLCA              Reviewed;         113 AA.
AC   P29233;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Sensorin-A;
DE   Contains:
DE     RecName: Full=Peptide B;
DE   Contains:
DE     RecName: Full=Sensorin-A;
DE   Flags: Precursor;
GN   Name=PSC1;
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 [MRNA], PROTEIN SEQUENCE OF 33-54, AND AMIDATION AT
RP   PHE-54.
RC   TISSUE=Pleural sensory cell;
RX   PubMed=1840700; DOI=10.1126/science.1840700;
RA   Brunet J.-F., Shapiro E., Foster S.A., Kandel E.R., Iino Y.;
RT   "Identification of a peptide specific for Aplysia sensory neurons by PCR-
RT   based differential screening.";
RL   Science 252:856-859(1991).
CC   -!- FUNCTION: May function as an inhibitory cotransmitter acting in
CC       conjunction with the fast excitatory transmitter released by sensory
CC       neurons. The peptide selectively inhibits certain postsynaptic cells
CC       probably by means of sensorin A release.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Throughout the neuronal cells
CC       (cell body, axon and presynaptic terminals).
CC   -!- TISSUE SPECIFICITY: Seems to be specific to the mechanosensory neurons
CC       of the central nervous system.
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DR   EMBL; X56770; CAA40089.1; -; mRNA.
DR   PIR; S23653; S23653.
DR   RefSeq; NP_001191583.1; NM_001204654.1.
DR   AlphaFoldDB; P29233; -.
DR   SMR; P29233; -.
DR   GeneID; 100533364; -.
DR   CTD; 100533364; -.
DR   OrthoDB; 1870869at2759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   1: Evidence at protein level;
KW   Amidation; Calcium; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         33..54
FT                   /note="Peptide B"
FT                   /id="PRO_0000001927"
FT   PEPTIDE         46..54
FT                   /note="Sensorin-A"
FT                   /id="PRO_0000001928"
FT   PROPEP          58..113
FT                   /id="PRO_0000001929"
FT   DOMAIN          87..113
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         102
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         106
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         111
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         54
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:1840700"
SQ   SEQUENCE   113 AA;  12711 MW;  74350F5154B49E1A CRC64;
     MPSRAATSPL NVQMMVVLCI VCLALQAVAA NATRSKNNVP RRFPRARYRV GYMFGKRSSS
     ETYSTNLINL LSRQLVSQEE LRAILEKQPI LLDEVVKILD RNDDGYITVA DLL