ID   APOD_CAVPO              Reviewed;         189 AA.
AC   P51909;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Apolipoprotein D;
DE            Short=Apo-D;
DE            Short=ApoD;
DE   Flags: Precursor;
GN   Name=APOD;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RX   PubMed=7664986; DOI=10.1016/0303-7207(95)03506-3;
RA   Provost P.R., Tremblay Y., El-Amine M., Belanger A.;
RT   "Guinea pig apolipoprotein D RNA diversity, and developmental and
RT   gestational modulation of mRNA levels.";
RL   Mol. Cell. Endocrinol. 109:225-236(1995).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; S79402; AAB35199.1; -; mRNA.
DR   RefSeq; XP_003477147.1; XM_003477099.3.
DR   AlphaFoldDB; P51909; -.
DR   SMR; P51909; -.
DR   STRING; 10141.ENSCPOP00000003643; -.
DR   PRIDE; P51909; -.
DR   Ensembl; ENSCPOT00000004082; ENSCPOP00000003643; ENSCPOG00000004038.
DR   GeneID; 100735684; -.
DR   KEGG; cpoc:100735684; -.
DR   CTD; 347; -.
DR   eggNOG; KOG4824; Eukaryota.
DR   GeneTree; ENSGT00510000046981; -.
DR   HOGENOM; CLU_068449_2_1_1; -.
DR   InParanoid; P51909; -.
DR   OMA; YSCTTIV; -.
DR   OrthoDB; 1631943at2759; -.
DR   TreeFam; TF324836; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000004038; Expressed in ovary and 13 other tissues.
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..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..189
FT                   /note="Apolipoprotein D"
FT                   /id="PRO_0000017871"
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;  21610 MW;  BCBE8A7660AD932A CRC64;
     MGMMLLLLSM LAGLVAEAEG QAFHFGKCPN PPVQENFDLN KYLGRWYEIE KIPVSFEKGN
     CIQANYSLKE NGRVKVLNQE LRPDGTVNQI EGEATHSNIT EPAKLGVKFF QLMPSAPYWV
     LATDYDNYAL VYSCTNIIWL FHVDHIWILG RNRYLPQETV TYLKDILTSN NIDIEKMTLT
     DQANCPDFL