Q00623 (APOA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Apolipoprotein A-I
Short name=Apo-AI
Short name=ApoA-I

Alternative name(s):
Apolipoprotein A1

Cleaved into the following chain:

1. Truncated apolipoprotein A-I

Gene names

Name:

Apoa1

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	264 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	Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
Subunit structure	Interacts with APOA1BP and CLU. Component of a sperm activating protein complex (SPAP), consisting of APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and albumin. Interacts with NDRG1 By similarity.
Subcellular location	Secreted.
Tissue specificity	Major protein of plasma HDL, also found in chylomicrons.
Post-translational modification	Palmitoylated By similarity. Met-109 is oxidized to methionine sulfoxide By similarity. Phosphorylation sites are present in the extracellular medium By similarity.
Sequence similarities	Belongs to the apolipoprotein A1/A4/E family.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Lipid transport Steroid metabolism Sterol metabolism Transport
Cellular component	HDL Secreted
Domain	Repeat Signal
PTM	Lipoprotein Oxidation Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara adrenal gland development Inferred from mutant phenotype PubMed 8647961. Source: MGI blood vessel endothelial cell migration Inferred from mutant phenotype PubMed 16339487. Source: MGI cholesterol biosynthetic process Inferred from mutant phenotype PubMed 8647961. Source: MGI cholesterol efflux Inferred from direct assay PubMed 11744719PubMed 12869555PubMed 15269218PubMed 9186920. Source: MGI cholesterol homeostasis Inferred from electronic annotation. Source: Compara cholesterol import Inferred from electronic annotation. Source: Compara endothelial cell proliferation Inferred from mutant phenotype PubMed 16339487. Source: MGI glucocorticoid metabolic process Inferred from mutant phenotype PubMed 8647961. Source: MGI high-density lipoprotein particle assembly Inferred from electronic annotation. Source: Compara lipid storage Inferred from mutant phenotype PubMed 8647961. Source: MGI lipoprotein biosynthetic process Inferred from mutant phenotype PubMed 16245952. Source: MGI negative regulation of cell adhesion molecule production Inferred from electronic annotation. Source: Compara negative regulation of cytokine secretion involved in immune response Inferred from electronic annotation. Source: Compara negative regulation of heterotypic cell-cell adhesion Inferred from electronic annotation. Source: Compara negative regulation of hydrolase activity Inferred from genetic interaction PubMed 15995171. Source: MGI negative regulation of inflammatory response Inferred from electronic annotation. Source: Compara negative regulation of interleukin-1 beta secretion Inferred from electronic annotation. Source: Compara negative regulation of lipase activity Inferred from electronic annotation. Source: Compara negative regulation of tumor necrosis factor-mediated signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of very-low-density lipoprotein particle remodeling Inferred from electronic annotation. Source: Compara organ regeneration Inferred from electronic annotation. Source: Compara peptidyl-methionine modification Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylcholine biosynthetic process Inferred from electronic annotation. Source: Compara phospholipid efflux Inferred from electronic annotation. Source: Compara phospholipid homeostasis Inferred from electronic annotation. Source: Compara phospholipid metabolic process Inferred from mutant phenotype PubMed 9795222. Source: MGI positive regulation of cholesterol esterification Inferred from electronic annotation. Source: Compara positive regulation of hydrolase activity Inferred from electronic annotation. Source: Compara positive regulation of transferase activity Inferred from mutant phenotype PubMed 16245952. Source: MGI protein oxidation Inferred from sequence or structural similarity. Source: UniProtKB protein stabilization Inferred from electronic annotation. Source: Compara regulation of Cdc42 protein signal transduction Inferred from electronic annotation. Source: Compara regulation of intestinal cholesterol absorption Inferred from direct assay PubMed 10073953. Source: MGI regulation of protein phosphorylation Inferred from direct assay PubMed 12869555. Source: MGI response to drug Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara reverse cholesterol transport Inferred from electronic annotation. Source: Compara triglyceride homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	endocytic vesicle Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay PubMed 10357841PubMed 11744719PubMed 12859204PubMed 14595002PubMed 1596514PubMed 6403543PubMed 7751823PubMed 7798939PubMed 9186920PubMed 9275209PubMed 9300780PubMed 9507992. Source: MGI nucleus Inferred from electronic annotation. Source: Compara spherical high-density lipoprotein particle Inferred from electronic annotation. Source: Compara very-low-density lipoprotein particle Inferred from electronic annotation. Source: Compara
Molecular_function	beta-amyloid binding Inferred from electronic annotation. Source: Compara cholesterol binding Inferred from electronic annotation. Source: Compara cholesterol transporter activity Inferred from direct assay PubMed 15269218. Source: MGI high-density lipoprotein particle binding Inferred from direct assay PubMed 11744719PubMed 14595002. Source: MGI lipase inhibitor activity Inferred from electronic annotation. Source: Compara lipid binding Inferred from direct assay PubMed 8049247. Source: MGI phosphatidylcholine-sterol O-acyltransferase activator activity Inferred from electronic annotation. Source: Compara phospholipid binding Inferred from electronic annotation. Source: Compara phospholipid transporter activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Kcnma1	Q08460	4	EBI-1634106,EBI-1633915

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

By similarity

Propeptide

19 – 24

6

By similarity

PRO_0000001945

Chain

25 – 264

240

Apolipoprotein A-I

PRO_0000001946

Chain

25 – 263

239

Truncated apolipoprotein A-I By similarity

PRO_0000416576

Regions

Repeat

67 – 88

22

1

Repeat

89 – 110

22

2

Repeat

111 – 121

11

3; half-length

Repeat

122 – 143

22

4

Repeat

144 – 165

22

5

Repeat

166 – 187

22

6

Repeat

188 – 207

20

7; truncated

Repeat

208 – 229

22

8

Repeat

230 – 240

11

9; half-length

Repeat

241 – 264

24

10

Region

67 – 264

198

10 X approximate tandem repeats

Amino acid modifications

Modified residue

109

1

Methionine sulfoxide By similarity

Experimental info

Sequence conflict

249 – 250

2

QV → KA in CAA45560. Ref.1

Sequence conflict

249 – 250

2

QV → KA in CAA45561. Ref.1

Sequence conflict

249 – 250

2

QV → KA in AAH12253. Ref.5

Sequence conflict

249 – 250

2

QV → KA in AAH19837. Ref.5

Secondary structure

1

.

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264

Helix Strand Turn

Details...

Helix

30 – 71

42

Turn

72 – 75

4

Helix

83 – 119

37

Turn

120 – 123

4

Helix

126 – 141

16

Helix

145 – 154

10

Helix

167 – 206

40

Beta strand

217 – 219

3

Helix

220 – 226

7

Helix

233 – 237

5

Sequences

	Sequence		Length	Mass (Da)
	Q00623 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: 5E33FF201963583B	FASTA	264	30,616
	10 20 30 40 50 60 MKAVVLAVAL VFLTGSQAWH VWQQDEPQSQ WDKVKDFANV YVDAVKDSGR DYVSQFESSS 70 80 90 100 110 120 LGQQLNLNLL ENWDTLGSTV SQLQERLGPL TRDFWDNLEK ETDWVRQEMN KDLEEVKQKV 130 140 150 160 170 180 QPYLDEFQKK WKEDVELYRQ KVAPLGAELQ ESARQKLQEL QGRLSPVAEE FRDRMRTHVD 190 200 210 220 230 240 SLRTQLAPHS EQMRESLAQR LAELKSNPTL NEYHTRAKTH LKTLGEKARP ALEDLRHSLM 250 260 PMLETLKTQV QSVIDKASET LTAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse apolipoprotein AI. cDNA-derived primary structure, gene organisation and complete nucleotide sequence." Stoffel W., Mueller R., Binczek E., Hofmann K. Biol. Chem. Hoppe-Seyler 373:187-193(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Characterization of the mouse apolipoprotein Apoa-1/Apoc-3 gene locus: genomic, mRNA, and protein sequences with comparisons to other species." Januzzi J.L., Azrolan N., O'Connell A., Aalto-Setala K., Breslow J.L. Genomics 14:1081-1088(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[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: Liver, Ovary, Placenta and Uterus.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	"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: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X64262 mRNA. Translation: CAA45560.1.
X64263 Genomic DNA. Translation: CAA45561.1.
L04149 Genomic DNA. No translation available.
L04151 mRNA. No translation available.
AK076187 mRNA. Translation: BAC36241.1.
AK149576 mRNA. Translation: BAE28968.1.
AK161536 mRNA. Translation: BAE36448.1.
AC116503 Genomic DNA. No translation available.
BC012253 mRNA. Translation: AAH12253.1.
BC019837 mRNA. Translation: AAH19837.1.

IPI

IPI00121209.

PIR

S22420.

RefSeq

NP_033822.2. NM_009692.3.

UniGene

Mm.26743.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LEM	NMR	-	A	25-240	[»]

ProteinModelPortal

Q00623.

SMR

Q00623. Positions 25-240.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q00623. 1 interaction.

PTM databases

PhosphoSite

Q00623.

2D gel databases

REPRODUCTION-2DPAGE

IPI00121209.
Q00623.

SWISS-2DPAGE

Q00623.

Proteomic databases

PaxDb

Q00623.

PRIDE

Q00623.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034588; ENSMUSP00000034588; ENSMUSG00000032083.

GeneID

11806.

KEGG

mmu:11806.

Organism-specific databases

CTD

335.

MGI

MGI:88049. Apoa1.

Phylogenomic databases

eggNOG

NOG39720.

GeneTree

ENSGT00530000063081.

HOGENOM

HOG000033998.

HOVERGEN

HBG105708.

InParanoid

Q00623.

KO

K08757.

OMA

QQDEPQS.

OrthoDB

EOG44J2JV.

Gene expression databases

CleanEx

MM_APOA1.

Genevestigator

Q00623.

GermOnline

ENSMUSG00000032083. Mus musculus.

Family and domain databases

InterPro

IPR013326. ApoA.
IPR000074. ApoA1_A4_E.
[Graphical view]

Pfam

PF01442. Apolipoprotein. 1 hit.
[Graphical view]

SUPFAM

SSF47162. SSF47162. 2 hits.

ProtoNet

Search...

Other

ChiTaRS

APOA1. mouse.

NextBio

279667.

SOURCE

Search...

Entry information

Entry name

APOA1_MOUSE

Accession

Primary (citable) accession number: Q00623
Secondary accession number(s): Q8BPD5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program