Apolipoprotein D

Apolipoprotein D (ApoD) is a protein that in humans is encoded by the APOD gene. Unlike other lipoproteins, which are mainly produced in the liver, apolipoprotein D is mainly produced in the brain and testes. It is a 29 kDa glycoprotein discovered in 1963 as a component of the high-density lipoprotein (HDL) fraction of human plasma. It is the major component of human mammary cyst fluid. The human gene encoding it was cloned in 1986 and the deduced protein sequence revealed that ApoD is a member of the lipocalin family, small hydrophobic molecule transporters. ApoD is 169 amino acids long, including a secretion peptide signal of 20 amino acids. It contains two glycosylation sites (aspargines 45 and 78) and the molecular weight of the mature protein varies from 20 to 32 kDa (see figure 1).

APOD
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAPOD, Apod, apolipoprotein D
External IDsOMIM: 107740 MGI: 88056 HomoloGene: 1246 GeneCards: APOD
Orthologs
SpeciesHumanMouse
Entrez

347

11815

Ensembl

ENSG00000189058

ENSMUSG00000022548

UniProt

P05090

P51910

RefSeq (mRNA)

NM_001647

NM_001301353
NM_001301354
NM_007470

RefSeq (protein)

NP_001638

NP_001288282
NP_001288283
NP_031496

Location (UCSC)Chr 3: 195.57 – 195.58 MbChr 16: 31.12 – 31.13 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

The resolved tertiary structure shows that ApoD is composed of 8 anti-parallel β-strands forming a hydrophobic cavity capable of receiving different ligands. ApoD also contains 5 cysteine residues, 4 of which are involved in intra-molecular disulfide bonds.

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