ID D2HPB7_AILME Unreviewed; 295 AA.
AC D2HPB7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Apolipoprotein E {ECO:0000256|ARBA:ARBA00019891};
DE Flags: Fragment;
GN ORFNames=PANDA_013610 {ECO:0000313|EMBL:EFB13033.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB13033.1};
RN [1] {ECO:0000313|EMBL:EFB13033.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- SUBUNIT: Homotetramer. May interact with ABCA1; functionally associated
CC with ABCA1 in the biogenesis of HDLs. May interact with APP/A4 amyloid-
CC beta peptide; the interaction is extremely stable in vitro but its
CC physiological significance is unclear. May interact with MAPT. May
CC interact with MAP2. In the cerebrospinal fluid, interacts with secreted
CC SORL1. Interacts with PMEL; this allows the loading of PMEL luminal
CC fragment on ILVs to induce fibril nucleation.
CC {ECO:0000256|ARBA:ARBA00034326}.
CC -!- SUBCELLULAR LOCATION: Endosome, multivesicular body
CC {ECO:0000256|ARBA:ARBA00004559}. Extracellular vesicle
CC {ECO:0000256|ARBA:ARBA00034305}. Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000256|ARBA:ARBA00008788}.
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DR EMBL; GL193124; EFB13033.1; -; Genomic_DNA.
DR RefSeq; XP_019660445.1; XM_019804886.1.
DR AlphaFoldDB; D2HPB7; -.
DR GeneID; 100477661; -.
DR KEGG; aml:100477661; -.
DR CTD; 348; -.
DR HOGENOM; CLU_066029_0_0_1; -.
DR InParanoid; D2HPB7; -.
DR OrthoDB; 4591103at2759; -.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005771; C:multivesicular body; IEA:UniProtKB-SubCell.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Chylomicron {ECO:0000256|ARBA:ARBA00022513};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW HDL {ECO:0000256|ARBA:ARBA00022850};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW VLDL {ECO:0000256|ARBA:ARBA00023313}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..295
FT /note="Apolipoprotein E"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003031174"
FT COILED 69..126
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 238..272
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 295
FT /evidence="ECO:0000313|EMBL:EFB13033.1"
SQ SEQUENCE 295 AA; 34300 MW; 5E65B1BBCD092A7E CRC64;
MKVLWAALVV ALLAGCWADV EPELKLEPEA GWQTGQPWEL ALARFWDYLR WVQTMSEQVQ
EEMLSNRVIQ ELTALMEDTL KEVKTYTEEV EEQLGPMTSE MQARVMKELQ AAQARLRSDM
EDVRSRLTQY RGELQGMLGQ SGDELRARLT SHLRKLRKRL LRDAEDLQKR LAVYRAGVHE
GTERTMDTIT EHLWPLLMNV RTRQAIASSP GMQPLHERAE ALGQHLRGQL EEVGSRARSQ
LDEALEQVEV MRAKLEEQAE HMRQQAEAFQ ARLRSWFEPL VEDMQRQWAE LVEKV
//
