ID   APOD_RAT                Reviewed;         189 AA.
AC   P23593;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   02-SEP-2026, entry version 135.
DE   RecName: Full=Apolipoprotein D;
DE            Short=Apo-D;
DE            Short=ApoD;
DE   Flags: Precursor;
GN   Name=Apod;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RX   PubMed=1695148; DOI=10.1002/j.1460-2075.1990.tb07426.x;
RA   Spreyer P., Schaal H., Kuhn G., Rothe T., Unterbeck A., Olek K.,
RA   Mueller H.W.;
RT   "Regeneration-associated high level expression of apolipoprotein D mRNA in
RT   endoneurial fibroblasts of peripheral nerve.";
RL   EMBO J. 9:2479-2484(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 69-87; 98-132 AND 179-189, AND TISSUE SPECIFICITY.
RX   PubMed=2090718; DOI=10.1016/s0022-2275(20)42112-1;
RA   Boyles J.K., Notterpek L.M., Wardell M.R., Rall S.C. Jr.;
RT   "Identification, characterization, and tissue distribution of
RT   apolipoprotein D in the rat.";
RL   J. Lipid Res. 31:2243-2256(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 28-95 AND 152-176, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
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: Expressed in liver, kidney, bladder, adrenal,
CC       cerebrum, duodenum, testis, lung, spleen, pancreas, heart and skin.
CC       {ECO:0000269|PubMed:2090718}.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X55572; CAA39158.1; -; mRNA.
DR   PIR; S12556; A60958.
DR   RefSeq; NP_036909.2; NM_012777.2.
DR   AlphaFoldDB; P23593; -.
DR   SMR; P23593; -.
DR   BioGRID; 247279; 1.
DR   FunCoup; P23593; 78.
DR   STRING; 10116.ENSRNOP00000064368; -.
DR   GlyCosmos; P23593; 2 sites, No reported glycans.
DR   GlyGen; P23593; 2 sites.
DR   PhosphoSitePlus; P23593; -.
DR   PaxDb; 10116-ENSRNOP00000064368; -.
DR   DNASU; 25239; -.
DR   GeneID; 25239; -.
DR   KEGG; rno:25239; -.
DR   AGR; RGD:2137; -.
DR   CTD; 347; -.
DR   RGD; 2137; Apod.
DR   eggNOG; KOG4824; Eukaryota.
DR   InParanoid; P23593; -.
DR   PhylomeDB; P23593; -.
DR   Reactome; R-RNO-804914; Transport of fatty acids.
DR   PRO; PR:P23593; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; IEA:InterPro.
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; IEP:RGD.
DR   GO; GO:0048678; P:response to axon injury; IEP:UniProtKB.
DR   GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0042246; P:tissue regeneration; IEP:RGD.
DR   CDD; cd19437; lipocalin_apoD-like; 1.
DR   FunFam; 2.40.128.20:FF:000003; Apolipoprotein D; 1.
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   PANTHER; PTHR10612; APOLIPOPROTEIN D; 1.
DR   PANTHER; PTHR10612:SF34; APOLIPOPROTEIN D; 1.
DR   Pfam; PF08212; Lipocalin_2; 1.
DR   PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR   PRINTS; PR02058; APODVERTBRTE.
DR   PRINTS; PR01219; APOLIPOPROTD.
DR   PRINTS; PR00179; LIPOCALIN.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Lipid-binding;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW   Transport.
FT   SIGNAL          1..20
FT   CHAIN           21..189
FT                   /note="Apolipoprotein D"
FT                   /id="PRO_0000017876"
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"
FT   CONFLICT        180
FT                   /note="K -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   189 AA;  21635 MW;  1E4823A45E38B4C0 CRC64;
     MATMLLLLAT LAGLFTTTEG QSFHLGKCPS PPVQENFDVK KYLGRWYEIE KIPVSFEKGN
     CIQANYSLME NGNIKVLNKE LRPDGTLNQV EGEAKQSNMS EPAKLEVQFF SLMPPAPYWI
     LATDYESYAL VYSCTTFFWF FHVDYVWILG RNPYLPPETI TYLKYILTSN DIDIAKITTK
     DQANCPDFL
//