ID A0A1L8FNA0_XENLA Unreviewed; 275 AA.
AC A0A1L8FNA0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Apolipoprotein E L homeolog precursor {ECO:0000313|RefSeq:NP_001353643.1};
DE Flags: Precursor;
GN Name=apoe.L {ECO:0000313|RefSeq:NP_001353643.1};
GN Synonyms=ad2 {ECO:0000313|RefSeq:NP_001353643.1}, apo-e
GN {ECO:0000313|RefSeq:NP_001353643.1}, ldlcq5
GN {ECO:0000313|RefSeq:NP_001353643.1}, lpg
GN {ECO:0000313|RefSeq:NP_001353643.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:NP_001353643.1};
RN [1] {ECO:0000313|RefSeq:NP_001353643.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|RefSeq:NP_001353643.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000256|ARBA:ARBA00008788}.
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 RefSeq; NP_001353643.1; NM_001366714.1.
DR AlphaFoldDB; A0A1L8FNA0; -.
DR STRING; 8355.A0A1L8FNA0; -.
DR PaxDb; 8355-A0A1L8FNA0; -.
DR KEGG; xla:495356; -.
DR OMA; GHMTDAR; -.
DR OrthoDB; 4591103at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR Gene3D; 1.20.120.20; Apolipoprotein; 2.
DR InterPro; IPR000074; ApoA_E.
DR PANTHER; PTHR18976; APOLIPOPROTEIN; 1.
DR PANTHER; PTHR18976:SF2; APOLIPOPROTEIN E; 1.
DR Pfam; PF01442; Apolipoprotein; 1.
DR SUPFAM; SSF58113; Apolipoprotein A-I; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001353643.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001353643.1"
FT CHAIN 19..275
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001353643.1"
FT /id="PRO_5033207780"
SQ SEQUENCE 275 AA; 31407 MW; D9A79EBA5AD1CE57 CRC64;
MKVTFFLLAL GLLAGAQARS LFRDAPKTKW ESALDSFWLT VNKMEEAADE ARAQMKDSPI
SKELDGLIKD TMEELSSYAE DMKSKVSPMA QDAQQRFTEE VSALADKLKS DMEDTKNKAI
QYSGDLRMMF DQNIEDVQGK VTMYMKKLKK RLSKDSEELK KKLSQYGDDF RKSTEDKVEN
IRKAVEPYVS NIKDKGQQRL MTLKDAMDEQ GKQLRDRFLS VAKDAQAKMK KAASDVKSSV
DKLGEQFRKW FNPNVESLRN QLQALAKSLQ TKANK
//