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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}.
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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
 
 
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