APOD_RAT
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 25-MAY-2022, entry version 123.
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;
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}.
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DR EMBL; X55572; CAA39158.1; -; mRNA.
DR PIR; S12556; A60958.
DR RefSeq; NP_036909.1; NM_012777.1.
DR AlphaFoldDB; P23593; -.
DR SMR; P23593; -.
DR BioGRID; 247279; 1.
DR STRING; 10116.ENSRNOP00000064368; -.
DR GlyGen; P23593; 2 sites.
DR PaxDb; P23593; -.
DR DNASU; 25239; -.
DR GeneID; 25239; -.
DR KEGG; rno:25239; -.
DR CTD; 347; -.
DR RGD; 2137; Apod.
DR eggNOG; KOG4824; Eukaryota.
DR InParanoid; P23593; -.
DR OrthoDB; 1631943at2759; -.
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:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; 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:0007568; P:aging; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
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 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 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
