ID APOE_CAMDR Reviewed; 317 AA. AC P0DOC3; DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2016, sequence version 1. DT 10-MAY-2017, entry version 5. DE RecName: Full=Apolipoprotein E; DE Short=Apo-E; DE Flags: Precursor; GN Name=APOE; OS Camelus dromedarius (Dromedary) (Arabian camel). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda; OC Camelidae; Camelus. OX NCBI_TaxID=9838; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fitak R., Mohandesan E., Burger P.A., Jukka C.; RT "The de novo genome assembly and annotation of a female domestic RT dromedary of North African origin."; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. RN [2] RP IDENTIFICATION. RA Puppione D.L.; RL Unpublished observations (JUL-2016). CC -!- FUNCTION: Mediates the binding, internalization, and catabolism of CC lipoprotein particles. It can serve as a ligand for the LDL (apo CC B/E) receptor and for the specific apo-E receptor (chylomicron CC remnant) of hepatic tissues (By similarity). CC {ECO:0000250|UniProtKB:P02649}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium. CC {ECO:0000250|UniProtKB:P02649}. CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family. CC {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; JWIN01034738; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; P0DOC3; -. DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW. DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW. 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:InterPro. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro. DR InterPro; IPR000074; ApoA_E. DR Pfam; PF01442; Apolipoprotein; 1. PE 3: Inferred from homology; KW Chylomicron; Glycoprotein; HDL; Heparin-binding; Lipid transport; KW Oxidation; Phosphoprotein; Repeat; Secreted; Signal; Transport; VLDL. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 317 Apolipoprotein E. FT /FTId=PRO_0000437471. FT REPEAT 79 100 1. FT REPEAT 101 122 2. FT REPEAT 123 144 3. FT REPEAT 145 166 4. FT REPEAT 167 188 5. FT REPEAT 189 210 6. FT REPEAT 211 232 7. FT REPEAT 233 254 8. FT REGION 79 254 8 X 22 AA approximate tandem repeats. FT REGION 157 167 LDL receptor binding. FT {ECO:0000250|UniProtKB:P02649}. FT REGION 161 164 Heparin-binding. FT {ECO:0000250|UniProtKB:P02649}. FT REGION 228 235 Heparin-binding. FT {ECO:0000250|UniProtKB:P02649}. FT MOD_RES 142 142 Methionine sulfoxide. FT {ECO:0000250|UniProtKB:P02649}. FT CARBOHYD 211 211 O-linked (GalNAc...) threonine. FT {ECO:0000250|UniProtKB:P02649}. FT CARBOHYD 310 310 O-linked (GalNAc...) threonine. FT {ECO:0000250|UniProtKB:P02649}. SQ SEQUENCE 317 AA; 36035 MW; 23EF479EC32DFD3E CRC64; MKALWVALVV TLLAGCRAEV EPEPEPEVQL GQEQPEWQGS QPWELALGRL WDYLRWVQTL SDQVQEELLS TQVTQELTAL MEETMKEVKA YKAELEEQLS PVAQETRARL SKELQAAQAR LGTDMEDLRS RLAHYRNEVQ AMLGQTTDEL RNRLASHLRK LRKRLLRDAE DLQKRLAVYR AGAVEGAERS VSALRERLGP LVEQGRLGTA TTSTLGSQPL RERAEAWGQK LRGRLEAVGA RAQDRLDKMR EQLEEVRAKV EEQASQMRLQ AETFQARLKG WFQPLVEDLQ RQWAGLVEKV QQLAVGTTPT PAASKNQ //