P51910 (APOD_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

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 transcript 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 By similarity.
Subcellular location	Secreted.
Tissue specificity	Highest levels of expression in brain, testis, virgin mammary gland and salivary gland. Moderate levels in skeletal muscle, lactating mammary gland and thymus. Low levels in lung and lymph node. No expression in kidney, pancreas, liver or spleen.
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 Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from sequence or structural similarity. Source: UniProtKB brain development Inferred from sequence or structural similarity. Source: UniProtKB 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 mutant phenotype PubMed 18419796. 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 sequence or structural similarity. Source: UniProtKB response to drug Inferred from sequence or structural similarity. Source: UniProtKB response to reactive oxygen species Inferred from mutant phenotype PubMed 18419796. Source: UniProtKB tissue regeneration Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosolic ribosome Inferred from sequence or structural similarity. Source: UniProtKB dendrite Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from sequence or structural similarity. Source: UniProtKB neuronal cell body Inferred from sequence or structural similarity. Source: UniProtKB 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	By similarity
	Chain	21 – 189	169	Apolipoprotein D		PRO_0000017874
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
Natural variations
	Natural variant	146	1	V → F in strain: Swiss Webster.

Sequences

	Sequence		Length	Mass (Da)
	P51910 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: C10109F1D56D69A0	FASTA	189	21,530
	10 20 30 40 50 60 MVTMLMFLAT LAGLFTTAKG QNFHLGKCPS PPVQENFDVK KYLGRWYEIE KIPASFEKGN 70 80 90 100 110 120 CIQANYSLME NGNIEVLNKE LSPDGTMNQV KGEAKQSNVS EPAKLEVQFF PLMPPAPYWI 130 140 150 160 170 180 LATDYENYAL VYSCTTFFWL FHVDFVWILG RNPYLPPETI TYLKDILTSN GIDIEKMTTT DQANCPDFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization and differential mRNA tissue distribution of mouse apolipoprotein D." Seguin D., Desforges M., Rassart E. Brain Res. Mol. Brain Res. 30:242-250(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c. Tissue: Brain.
[2]	"The murine gene encoding apolipoprotein D exhibits a unique expression pattern as compared to other species." Cofer S., Ross R.R. Gene 171:261-263(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss Webster. Tissue: Mammary gland.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Diencephalon, Embryonic head, Inner ear and Olfactory bulb.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L39123 Genomic DNA. Translation: AAA67892.1. X82648 mRNA. Translation: CAA57974.1. AK135046 mRNA. Translation: BAE22397.1. AK157917 mRNA. Translation: BAE34262.1. AK158118 mRNA. Translation: BAE34364.1. AK158405 mRNA. Translation: BAE34491.1. AK160729 mRNA. Translation: BAE35974.1. AK162392 mRNA. Translation: BAE36889.1. BC145907 mRNA. Translation: AAI45908.1. BC145909 mRNA. Translation: AAI45910.1.
IPI	IPI00314309.
PIR	S49581.
RefSeq	NP_031496.2. NM_007470.3.
UniGene	Mm.2082.
3D structure databases
ProteinModelPortal	P51910.
SMR	P51910. Positions 23-186.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000119827.
PTM databases
PhosphoSite	P51910.
Proteomic databases
PaxDb	P51910.
PRIDE	P51910.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000115230; ENSMUSP00000110885; ENSMUSG00000022548. ENSMUST00000130560; ENSMUSP00000119827; ENSMUSG00000022548.
GeneID	11815.
KEGG	mmu:11815.
UCSC	uc007yxf.1. mouse.
Organism-specific databases
CTD	347.
MGI	MGI:88056. Apod.
Phylogenomic databases
eggNOG	COG3040.
GeneTree	ENSGT00510000046981.
HOGENOM	HOG000061525.
HOVERGEN	HBG018734.
InParanoid	Q3TZE7.
OMA	QANYSLM.
OrthoDB	EOG4G7C0M.
Gene expression databases
Bgee	P51910.
CleanEx	MM_APOD.
Genevestigator	P51910.
GermOnline	ENSMUSG00000022548. Mus musculus.
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	PF08212. Lipocalin_2. 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
ChiTaRS	APOD. mouse.
NextBio	279699.
SOURCE	Search...

Entry information

Entry name

APOD_MOUSE

Accession

Primary (citable) accession number: P51910
Secondary accession number(s): Q3TZE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program