APOEB_DANRE
ID APOEB_DANRE Reviewed; 281 AA.
AC O42364;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Apolipoprotein Eb;
DE Short=Apo-Eb;
DE Flags: Precursor;
GN Name=apoeb; Synonyms=apoe;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9238027; DOI=10.1073/pnas.94.16.8622;
RA Babin P.J., Thisse C., Durliat M., Andre M., Akimenko M.-A., Thisse B.;
RT "Both apolipoprotein E and A-I genes are present in a nonmammalian
RT vertebrate and are highly expressed during embryonic development.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8622-8627(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10632725; DOI=10.1046/j.1432-1327.2000.01033.x;
RA Durliat M., Andre M., Babin P.J.;
RT "Conserved protein motifs and structural organization of a fish gene
RT homologous to mammalian apolipoprotein E.";
RL Eur. J. Biochem. 267:549-559(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- DEVELOPMENTAL STAGE: Highly expressed in the yolk syncytial layer
CC during embryonic (starting at the blastula stage) and early larval
CC development, an extraembryonic structure implicated in embryonic and
CC larval nutrition. Also observed in the deep cell layer during blastula
CC stage, in numerous ectodermal derivatives after gastrulation, and after
CC 3 days of development in a limited number of cells both in brain and in
CC the eyes.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; Y13652; CAA74003.1; -; mRNA.
DR EMBL; AJ236882; CAB64946.1; -; Genomic_DNA.
DR EMBL; BC065592; AAH65592.1; -; mRNA.
DR RefSeq; NP_571173.1; NM_131098.1.
DR RefSeq; XP_005158143.1; XM_005158086.3.
DR AlphaFoldDB; O42364; -.
DR SMR; O42364; -.
DR BioGRID; 78524; 1.
DR STRING; 7955.ENSDARP00000058964; -.
DR PaxDb; O42364; -.
DR Ensembl; ENSDART00000058965; ENSDARP00000058964; ENSDARG00000040295.
DR Ensembl; ENSDART00000192754; ENSDARP00000155792; ENSDARG00000040295.
DR GeneID; 30314; -.
DR KEGG; dre:30314; -.
DR CTD; 30314; -.
DR ZFIN; ZDB-GENE-980526-368; apoeb.
DR eggNOG; ENOG502QVD6; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_066029_1_0_1; -.
DR InParanoid; O42364; -.
DR OMA; TYMGEIQ; -.
DR OrthoDB; 1314660at2759; -.
DR PhylomeDB; O42364; -.
DR TreeFam; TF334458; -.
DR Reactome; R-DRE-3000480; Scavenging by Class A Receptors.
DR Reactome; R-DRE-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DRE-8957275; Post-translational protein phosphorylation.
DR Reactome; R-DRE-8963901; Chylomicron remodeling.
DR Reactome; R-DRE-8964026; Chylomicron clearance.
DR Reactome; R-DRE-975634; Retinoid metabolism and transport.
DR PRO; PR:O42364; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000040295; Expressed in pharyngeal gill and 72 other tissues.
DR ExpressionAtlas; O42364; baseline and differential.
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:0006707; P:cholesterol catabolic process; IBA:GO_Central.
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:0042159; P:lipoprotein catabolic process; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IBA:GO_Central.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IBA:GO_Central.
DR GO; GO:1900221; P:regulation of amyloid-beta clearance; IBA:GO_Central.
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; 2.
PE 2: Evidence at transcript level;
KW Extracellular matrix; Lipid transport; Lipid-binding; Reference proteome;
KW Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250|UniProtKB:P02649"
FT PROPEP 19..24
FT /evidence="ECO:0000255"
FT /id="PRO_0000002000"
FT CHAIN 25..281
FT /note="Apolipoprotein Eb"
FT /id="PRO_0000002001"
FT REPEAT 67..88
FT /note="1"
FT REPEAT 89..110
FT /note="2"
FT REPEAT 111..132
FT /note="3"
FT REPEAT 133..154
FT /note="4"
FT REPEAT 155..176
FT /note="5"
FT REPEAT 177..199
FT /note="6"
FT REPEAT 200..227
FT /note="7"
FT REPEAT 228..249
FT /note="8"
FT REPEAT 254..281
FT /note="9"
FT REGION 34..66
FT /note="3 X approximate tandem repeats"
FT REGION 67..281
FT /note="9 X 22 AA approximate tandem repeats"
SQ SEQUENCE 281 AA; 31674 MW; 54121E5A065BD453 CRC64;
MRSLVVFFAL AVLTGCQARS LFQADAPQPR WEEMVDRFWQ YVSELNTQTD GMVQNIKGSQ
LSRELDTLIT DTMAELSSYS ENLQTQMTPY ASDAAGQLSK DLQLLAGKLQ TDMTDAKERS
TQYLQELKTM MEQNADDVKN RVGTYTRKLK KRLNKDTEEI RNTVATYMSE MQSRASQNAD
AVKDRFQPYM SQAQDGATQK LGAISELMKA QAQEVSEQLE VQAGALKEKL EETAENLRTS
LEGRVDELTS LLAPYSQKIR EQLQEVMDKI KEATAALPTQ A
