APOE_ALLMI
ID APOE_ALLMI Reviewed; 258 AA.
AC P0DMT6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 12-AUG-2020, entry version 16.
DE RecName: Full=Apolipoprotein E;
DE Short=Apo-E;
DE Flags: Precursor;
GN Name=APOE;
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA St John J.A., Green R.E., Braun E.L., Ray D.A.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (FEB-2016).
CC -!- FUNCTION: APOE is an apolipoprotein, a protein associating with lipid
CC particles, that mainly functions in lipoprotein-mediated lipid
CC transport between organs via the plasma and interstitial fluids. APOE
CC is a core component of plasma lipoproteins and is involved in their
CC production, conversion and clearance. Apoliproteins are amphipathic
CC molecules that interact both with lipids of the lipoprotein particle
CC core and the aqueous environment of the plasma.
CC {ECO:0000250|UniProtKB:P02649}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P02649}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}.
CC Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:P02649}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; JH738485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 8496.XP_006276574.1; -.
DR eggNOG; ENOG502QVD6; Eukaryota.
DR PhylomeDB; P0DMT6; -.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISS:UniProtKB.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; ISS:UniProtKB.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISS:UniProtKB.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISS:UniProtKB.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISS:UniProtKB.
DR GO; GO:0033344; P:cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0034382; P:chylomicron remnant clearance; ISS:UniProtKB.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; ISS:UniProtKB.
DR GO; GO:0071831; P:intermediate-density lipoprotein particle clearance; ISS:UniProtKB.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; ISS:UniProtKB.
DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; ISS:UniProtKB.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISS:UniProtKB.
DR GO; GO:0071830; P:triglyceride-rich lipoprotein particle clearance; ISS:UniProtKB.
DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; ISS:UniProtKB.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
PE 3: Inferred from homology;
KW Extracellular matrix; Lipid transport; Lipid-binding; Repeat; Secreted;
KW Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..258
FT /note="Apolipoprotein E"
FT /evidence="ECO:0000255"
FT /id="PRO_0000432749"
FT REPEAT 112..133
FT /note="3"
FT REPEAT 134..155
FT /note="4"
FT REPEAT 156..173
FT /note="5"
FT REGION 112..173
FT /note="3 X 22 AA approximate tandem repeats"
SQ SEQUENCE 258 AA; 30178 MW; 959353AEA6DF05BB CRC64;
MRVWTVLLGA VLLLAACQAD VQDVETKVKA KWEETVEVFR EYVNRLSLAT DDITEQITSS
QMGKEMDMLI KDXVAELHAY RKDVEERLGP QAVVMRERLH TDVTVLGERL RVDMEEAKTR
VQQYLGEARQ VAGQNLEDVR SRVGTYLRKL RKRLAKDTEE LRRKLEAYSK EATQHLETVR
EDLEPLREKG QQRLETLQQA LRDQGQRLRE QLEVRAQEMR GSLDRAATQL QEWLEPFLED
IRTQMQGLLD KLQXKEQQ