ID   APOD_MACFA              Reviewed;         189 AA.
AC   Q8SPI0;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Apolipoprotein D;
DE            Short=Apo-D;
DE            Short=ApoD;
DE   Flags: Precursor;
GN   Name=APOD; ORFNames=QccE-15083;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RX   PubMed=11991714; DOI=10.1006/geno.2002.6753;
RA   Osada N., Kusuda J., Hirata M., Tanuma R., Hida M., Sugano S., Hirai M.,
RA   Hashimoto K.;
RT   "Search for genes positively selected during primate evolution by 5'-end-
RT   sequence screening of cynomolgus monkey cDNAs.";
RL   Genomics 79:657-662(2002).
CC   -!- FUNCTION: APOD occurs in the macromolecular complex with lecithin-
CC       cholesterol acyltransferase. It is probably involved in the transport
CC       and binding of bilin. Appears to be able to transport a variety of
CC       ligands in a number of different contexts (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; AB072021; BAB86810.1; -; mRNA.
DR   AlphaFoldDB; Q8SPI0; -.
DR   SMR; Q8SPI0; -.
DR   STRING; 9541.XP_005545387.1; -.
DR   PRIDE; Q8SPI0; -.
DR   VEuPathDB; HostDB:ENSMFAG00000002871; -.
DR   eggNOG; KOG4824; Eukaryota.
DR   OMA; YSCTTIV; -.
DR   Proteomes; UP000233100; Chromosome 2.
DR   GO; GO:0022626; C:cytosolic ribosome; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR   GO; GO:0007568; P:aging; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; ISS:UniProtKB.
DR   GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR   GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR   GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0060588; P:negative regulation of lipoprotein lipid oxidation; ISS:UniProtKB.
DR   GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; ISS:UniProtKB.
DR   GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR   GO; GO:2000098; P:negative regulation of smooth muscle cell-matrix adhesion; ISS:UniProtKB.
DR   GO; GO:2000405; P:negative regulation of T cell migration; ISS:UniProtKB.
DR   GO; GO:0014012; P:peripheral nervous system axon regeneration; ISS:UniProtKB.
DR   GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR   GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0042246; P:tissue regeneration; ISS:UniProtKB.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR026222; ApoD_vertbrte.
DR   InterPro; IPR002969; ApolipopD.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR022271; Lipocalin_ApoD.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   Pfam; PF08212; Lipocalin_2; 1.
DR   PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR   PRINTS; PR02058; APODVERTBRTE.
DR   PRINTS; PR01219; APOLIPOPROTD.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Lipid-binding; Pyrrolidone carboxylic acid;
KW   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..189
FT                   /note="Apolipoprotein D"
FT                   /id="PRO_0000017873"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P05090"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..185
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   189 AA;  21605 MW;  BDDBBA001240BFF1 CRC64;
     MVMLLLLLSA LAGLFGAAEG QEFRLGKCTS PPVQENFDPN KYFGRWYEIE KIPTTFEKGR
     CIQANYSLKE NGKIKVLNQE LRADGTVNQI EGEASPVNIT EPAKLEVKFF WFMPSAPYWV
     LATDYENYAL VYSCVSIINL FRVDYAWILA RNRHLPSETV DFLKNILTSN NIDVKKMTVT
     DQENCPEFS