P23593 (APOD_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Apolipoprotein D
Short name=Apo-D
Short name=ApoD

Gene names

Name:

Apod

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	189 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	APOD occurs in the macromolecular complex with lecithin-transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts.
Subunit structure	Homodimer.
Subcellular location	Secreted.
Tissue specificity	Expressed in liver, kidney, bladder, adrenal, cerebrum, duodenum, testis, lung, spleen, pancreas, heart and skin. Ref.2
Sequence similarities	Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Secreted
Domain	Signal
Ligand	Lipid-binding
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from expression pattern PubMed 19189975. Source: RGD brain development Inferred from expression pattern PubMed 10218791. Source: RGD glucose metabolic process Inferred from sequence or structural similarity. Source: UniProtKB lipid metabolic process Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of T cell migration Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cytokine production involved in inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of focal adhesion assembly Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of lipoprotein lipid oxidation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of monocyte chemotactic protein-1 production Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of platelet-derived growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein import into nucleus Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of smooth muscle cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of smooth muscle cell-matrix adhesion Inferred from sequence or structural similarity. Source: UniProtKB peripheral nervous system axon regeneration Inferred from expression pattern PubMed 2120218. Source: RGD response to drug Inferred from expression pattern PubMed 12911617. Source: RGD response to reactive oxygen species Inferred from sequence or structural similarity. Source: UniProtKB tissue regeneration Inferred from expression pattern Ref.1. Source: RGD
Cellular_component	cytosolic ribosome Inferred from direct assay PubMed 10218791. Source: RGD dendrite Inferred from direct assay PubMed 10218791. Source: RGD endoplasmic reticulum Inferred from direct assay PubMed 10218791. Source: RGD extracellular space Inferred from sequence or structural similarity. Source: UniProtKB neuronal cell body Inferred from direct assay PubMed 10218791. Source: RGD perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	cholesterol binding Inferred from sequence or structural similarity. Source: UniProtKB transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20
	Chain	21 – 189	169	Apolipoprotein D		PRO_0000017876
Amino acid modifications
	Modified residue	21	1	Pyrrolidone carboxylic acid By similarity
	Glycosylation	65	1	N-linked (GlcNAc...) Potential
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Disulfide bond	28 ↔ 134		By similarity
	Disulfide bond	61 ↔ 185		By similarity
Experimental info
	Sequence conflict	180	1	K → T AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P23593 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 1E4823A45E38B4C0	FASTA	189	21,635
	10 20 30 40 50 60 MATMLLLLAT LAGLFTTTEG QSFHLGKCPS PPVQENFDVK KYLGRWYEIE KIPVSFEKGN 70 80 90 100 110 120 CIQANYSLME NGNIKVLNKE LRPDGTLNQV EGEAKQSNMS EPAKLEVQFF SLMPPAPYWI 130 140 150 160 170 180 LATDYESYAL VYSCTTFFWF FHVDYVWILG RNPYLPPETI TYLKYILTSN DIDIAKITTK DQANCPDFL

References

[1]	"Regeneration-associated high level expression of apolipoprotein D mRNA in endoneurial fibroblasts of peripheral nerve." Spreyer P., Schaal H., Kuhn G., Rothe T., Unterbeck A., Olek K., Mueller H.W. EMBO J. 9:2479-2484(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar.
[2]	"Identification, characterization, and tissue distribution of apolipoprotein D in the rat." Boyles J.K., Notterpek L.M., Wardell M.R., Rall S.C. Jr. J. Lipid Res. 31:2243-2256(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 69-87; 98-132 AND 179-189, TISSUE SPECIFICITY.
[3]	Lubec G., Kang S.U., Lubec S. Submitted (SEP-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 28-95 AND 152-176, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X55572 mRNA. Translation: CAA39158.1.
IPI	IPI00212005.
PIR	A60958. S12556.
RefSeq	NP_036909.1. NM_012777.1.
UniGene	Rn.11339.
3D structure databases
ProteinModelPortal	P23593.
ModBase	Search...
Proteomic databases
PRIDE	P23593.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	25239.
KEGG	rno:25239.
Organism-specific databases
CTD	347.
RGD	2137. Apod.
Phylogenomic databases
HOVERGEN	HBG018734.
Gene expression databases
Genevestigator	P23593.
Family and domain databases
Gene3D	2.40.128.20. 1 hit.
InterPro	IPR026222. ApoD_vertbrte. IPR002969. ApolipopD. IPR012674. Calycin. IPR011038. Calycin-like. IPR002345. Lipocalin. IPR022271. Lipocalin_ApoD. IPR022272. Lipocalin_CS. IPR000566. Lipocln_cytosolic_FA-bd_dom. [Graphical view]
Pfam	PF00061. Lipocalin. 1 hit. [Graphical view]
PIRSF	PIRSF036893. Lipocalin_ApoD. 1 hit.
PRINTS	PR02058. APODVERTBRTE. PR01219. APOLIPOPROTD. PR00179. LIPOCALIN.
SUPFAM	SSF50814. Calycin. 1 hit.
PROSITE	PS00213. LIPOCALIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	605819.

Entry information

Entry name

APOD_RAT

Accession

Primary (citable) accession number: P23593

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program