LLPH_APLKU
ID LLPH_APLKU Reviewed; 120 AA.
AC B0FRH7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Protein LLP;
DE AltName: Full=Protein LAPS18-like;
GN Name=LLP {ECO:0000303|PubMed:12759182};
OS Aplysia kurodai (Kuroda's sea hare).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC Aplysiidae; Aplysia.
OX NCBI_TaxID=6501;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABY66901.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=12759182; DOI=10.1016/s0304-3940(03)00269-6;
RA Kim H., Chang D.-J., Lee J.-A., Lee Y.-S., Kaang B.-K.;
RT "Identification of nuclear/nucleolar localization signal in Aplysia
RT learning associated protein of slug with a molecular mass of 18 kDa
RT homologous protein.";
RL Neurosci. Lett. 343:134-138(2003).
RN [2] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16504946; DOI=10.1016/j.neuron.2006.01.035;
RA Kim H., Lee S.-H., Han J.-H., Lee J.-A., Cheang Y.-H., Chang D.-J.,
RA Lee Y.-S., Kaang B.-K.;
RT "A nucleolar protein ApLLP induces ApC/EBP expression required for long-
RT term synaptic facilitation in aplysia neurons.";
RL Neuron 49:707-718(2006).
CC -!- FUNCTION: Acts as a transcriptional activator of C/EBP. Required for
CC long-term synaptic facilitation at the sensory motor synapse. May
CC function in noxious stimulus-facilitated memory formation.
CC {ECO:0000269|PubMed:16504946}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12759182,
CC ECO:0000269|PubMed:16504946}.
CC -!- SIMILARITY: Belongs to the learning-associated protein family.
CC {ECO:0000255, 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; EU346889; ABY66901.1; -; mRNA.
DR AlphaFoldDB; B0FRH7; -.
DR SMR; B0FRH7; -.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IMP:CAFA.
DR GO; GO:0007613; P:memory; IEP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:UniProtKB.
DR DisProt; DP00544; -.
DR InterPro; IPR018784; LAPS18-like.
DR InterPro; IPR019434; UPF0642.
DR PANTHER; PTHR34253; PTHR34253; 1.
DR Pfam; PF10338; DUF2423; 1.
DR Pfam; PF10169; Laps; 1.
PE 2: Evidence at transcript level;
KW Activator; Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..120
FT /note="Protein LLP"
FT /id="PRO_0000365621"
FT REGION 79..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..120
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 120 AA; 14075 MW; 9B2C0F17F8DEBA26 CRC64;
MAKSIRSKHR RQMRNVKREH FAKKDLDRLK RLASKAQELD LDNVVTMKSA EEIKNKPSTS
ASDADKGMEV DNTKKVFKKK TQQNEDGHYP QWMNQRAVKK QKVKVAKLKT KKKIGKKIKW