ID   APOD_RABIT              Reviewed;         189 AA.
AC   P37153;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Apolipoprotein D;
DE            Short=Apo-D;
DE            Short=ApoD;
DE   Flags: Precursor;
GN   Name=APOD;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2086704;
RA   Provost P.R., Weech P.K., Tremblay N.M., Marcel Y.L., Rassart E.;
RT   "Molecular characterization and differential mRNA tissue distribution of
RT   rabbit apolipoprotein D.";
RL   J. Lipid Res. 31:2057-2065(1990).
CC   -!- FUNCTION: APOD occurs in the macromolecular complex with lecithin-
CC       transport and binding of bilin. Appears to be able to transport a
CC       variety of ligands in a number of different contexts.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Most heavily expressed in adrenal gland, lung,
CC       brain, testis and spleen.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; L42979; AAC41624.1; -; mRNA.
DR   PIR; A60954; A60954.
DR   RefSeq; NP_001075727.1; NM_001082258.2.
DR   AlphaFoldDB; P37153; -.
DR   SMR; P37153; -.
DR   STRING; 9986.ENSOCUP00000016728; -.
DR   GeneID; 100009080; -.
DR   KEGG; ocu:100009080; -.
DR   CTD; 347; -.
DR   eggNOG; KOG4824; Eukaryota.
DR   InParanoid; P37153; -.
DR   OrthoDB; 1631943at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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; PF00061; Lipocalin; 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..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..189
FT                   /note="Apolipoprotein D"
FT                   /id="PRO_0000017875"
FT   MOD_RES         22
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P05090"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..186
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   189 AA;  21478 MW;  12E405A236FCC104 CRC64;
     MAPTLLLLLP ALAGLISVAQ GQAFHLGRCP TPPVQENFDV HKYLGRWYEI EKIPVSFEKG
     NCIQANYSLM ENGNIKVLNQ ELRPDGTVNQ IEGQATQSNL TEPAKLGVKF FQLMPTAPYW
     VLATDYENYA LVYSCTTIIW LFHMDHVWIL GRNRYLPPET VTYLKDILTA NNIDIEKMTV
     TDQVNCPEF