ID   LPS18_LEHMA             Reviewed;         121 AA.
AC   Q9GNQ1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=18 kDa learning-associated protein of slug;
GN   Name=LAPS18 {ECO:0000303|PubMed:11168596};
OS   Lehmannia marginata (Tree slug) (Limax marginatus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC   Helicina; Limacoidea; Limacidae; Lehmannia.
OX   NCBI_TaxID=381128;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAG35713.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=11168596; DOI=10.1046/j.1365-2443.2001.00397.x;
RA   Nakaya T., Kawahara S., Watanabe S., Lee D.-S., Suzuki T., Kirino Y.;
RT   "Identification and expression of a novel gene in odour-taste associative
RT   learning in the terrestrial slug.";
RL   Genes Cells 6:43-56(2001).
CC   -!- FUNCTION: May be involved in modulating long-term memory formation and
CC       retention, at least with respect to odor-taste associative learning.
CC       {ECO:0000269|PubMed:11168596}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11168596}. Secreted
CC       {ECO:0000269|PubMed:11168596}. Note=Secreted to the cell surface, and
CC       to the terminals of neurites. {ECO:0000269|PubMed:11168596}.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in cerebral ganglia (at
CC       protein level). The mRNA is highly expressed in cerebral ganglia, and
CC       is detected at lower levels in visceral-pedal ganglia, head, and body,
CC       but is not detected in the tail. {ECO:0000269|PubMed:11168596}.
CC   -!- INDUCTION: Up-regulated in the somata of the procerebral neurons after
CC       associative conditioning with paired presentation of a carrot juice
CC       odor and an aversive quinidine taste. {ECO:0000269|PubMed:11168596}.
CC   -!- SIMILARITY: Belongs to the learning-associated protein family.
CC       {ECO:0000255, ECO:0000305}.
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DR   EMBL; AF207694; AAG35713.1; -; mRNA.
DR   AlphaFoldDB; Q9GNQ1; -.
DR   SMR; Q9GNQ1; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007611; P:learning or memory; IEP:UniProtKB.
DR   GO; GO:0007616; P:long-term memory; IEP:UniProtKB.
DR   InterPro; IPR018784; LAPS18-like.
DR   PANTHER; PTHR34253; PTHR34253; 1.
DR   Pfam; PF10169; Laps; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Secreted.
FT   CHAIN           1..121
FT                   /note="18 kDa learning-associated protein of slug"
FT                   /id="PRO_0000365622"
FT   REGION          44..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..121
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   121 AA;  14152 MW;  3383A907646234A7 CRC64;
     MAKGLRCKHR IRMRNIKRQH YAKKDLERLK KIVSKSSELK DVVTMKTTEP IQENKTSEGT
     STDGSMEVDK MAKVINKKTL QDENGHYPEW MNQRAVKKQK QKLNKLKIKK KSGKVSKAIK
     W