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Q00623 (APOA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein A-I

Short name=Apo-AI
Short name=ApoA-I
Alternative name(s):
Apolipoprotein A1

Cleaved into the following 2 chains:

  1. Proapolipoprotein A-I
    Short name=ProapoA-I
  2. Truncated apolipoprotein A-I
Gene names
Name:Apoa1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Glycosylated By similarity.

Palmitoylated By similarity.

May be acylated.

Phosphorylation sites are present in the extracellular medium By similarity.

Sequence similarities

Belongs to the apolipoprotein A1/A4/E family.

Mass spectrometry

Molecular mass is 27951.3±1.343 Da from positions 25 - 264. Determined by ESI. Strain C57BL/6. Without methionine sulfoxide. Ref.7

Molecular mass is 27923.8 Da from positions 25 - 264. Determined by ESI. Strain BALB/c. Without methionine sulfoxide. Ref.7

Molecular mass is 27965 Da from positions 25 - 264. Determined by ESI. Strain C57BL/6. With 1 methionine sulfoxide. Ref.7

Molecular mass is 28819.7 Da from positions 19 - 264. Determined by ESI. Strain C57BL/6. Without methionine sulfoxide. Ref.7

Molecular mass is 28790.7 Da from positions 19 - 264. Determined by ESI. Strain BALB/c. Without methionine sulfoxide. Ref.7

Ontologies

Keywords
   Biological processCholesterol metabolism
Lipid metabolism
Lipid transport
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentHDL
Secreted
   DomainRepeat
Signal
   PTMGlycoprotein
Lipoprotein
Oxidation
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

cholesterol import

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from mutant phenotype PubMed 10357841PubMed 15466405PubMed 17071966PubMed 7751823PubMed 9327769PubMed 9795222. Source: MGI

cholesterol transport

Inferred from direct assay PubMed 9300780. Source: MGI

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: Ensembl

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: Ensembl

negative regulation of cytokine secretion involved in immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of heterotypic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of hydrolase activity

Inferred from genetic interaction PubMed 15995171. Source: MGI

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-1 beta secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of tumor necrosis factor-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of very-low-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

peptidyl-methionine modification

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylcholine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

phospholipid efflux

Inferred from electronic annotation. Source: Ensembl

phospholipid homeostasis

Inferred from electronic annotation. Source: Ensembl

phospholipid metabolic process

Inferred from mutant phenotype PubMed 9795222. Source: MGI

positive regulation of cholesterol esterification

Inferred from electronic annotation. Source: Ensembl

positive regulation of hydrolase activity

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

regulation of Cdc42 protein signal transduction

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

reverse cholesterol transport

Inferred from electronic annotation. Source: Ensembl

triglyceride homeostasis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from direct assay PubMed 15793583. Source: MGI

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: Ensembl

spherical high-density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionbeta-amyloid binding

Inferred from electronic annotation. Source: Ensembl

cholesterol binding

Inferred from electronic annotation. Source: Ensembl

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

identical protein binding

Inferred from physical interaction PubMed 11744719PubMed 8049247. Source: MGI

lipase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

lipid binding

Inferred from direct assay PubMed 8049247. Source: MGI

lipid transporter activity

Inferred from direct assay PubMed 11744719. Source: MGI

lipoprotein particle binding

Inferred from direct assay PubMed 8049247. Source: MGI

phosphatidylcholine-sterol O-acyltransferase activator activity

Inferred from electronic annotation. Source: Ensembl

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

phospholipid transporter activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kcnma1Q084604EBI-1634106,EBI-1633915

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 264246Proapolipoprotein A-I
PRO_0000425326
Chain25 – 264240Apolipoprotein A-I
PRO_0000001946
Chain25 – 263239Truncated apolipoprotein A-I By similarity
PRO_0000416576

Regions

Repeat67 – 88221
Repeat89 – 110222
Repeat111 – 121113; half-length
Repeat122 – 143224
Repeat144 – 165225
Repeat166 – 187226
Repeat188 – 207207; truncated
Repeat208 – 229228
Repeat230 – 240119; half-length
Repeat241 – 2642410
Region67 – 26419810 X approximate tandem repeats

Amino acid modifications

Modified residue1091Methionine sulfoxide By similarity
Modified residue1931Methionine sulfoxide
Modified residue2401Methionine sulfoxide
Modified residue2421Methionine sulfoxide

Natural variations

Natural variant249 – 2502QV → KA in strain: BALB/c, C3H and ICR.

Experimental info

Sequence conflict1431A → G in AAB58424. Ref.3
Sequence conflict1431A → G in AAB58425. Ref.3
Sequence conflict1431A → G in AAB58426. Ref.3
Sequence conflict1431A → G in AAB58427. Ref.3
Sequence conflict1461Missing in AAB58424. Ref.3
Sequence conflict1461Missing in AAB58425. Ref.3
Sequence conflict1461Missing in AAB58426. Ref.3
Sequence conflict1461Missing in AAB58427. Ref.3

Secondary structure

.................. 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00623 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 5E33FF201963583B

FASTA26430,616
        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 

« Hide

References

« Hide '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]Chiang A.-N., Fan K.-C., Shaw G.-C., Yang U.-C.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT 249-LYS-ALA--250.
Strain: BALB/c, C3H, C57BL/6 and ICR.
Tissue: Spleen.
[4]"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. expand/collapse author list , 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], VARIANT 249-GLN-VAL-250.
Strain: C57BL/6J.
Tissue: Liver, Ovary, Placenta and Uterus.
[5]"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. expand/collapse author list , 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], VARIANT 249-GLN-VAL-250.
Strain: C57BL/6J.
[6]"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].
Strain: FVB/N.
Tissue: Liver.
[7]"Mass spectral analysis of the apolipoproteins on mouse high density lipoproteins. Detection of post-translational modifications."
Puppione D.L., Yam L.M., Bassilian S., Souda P., Castellani L.W., Schumaker V.N., Whitelegge J.P.
Biochim. Biophys. Acta 1764:1363-1371(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-46; 93-106; 120-129; 131-139; 142-154; 157-172; 177-194; 201-216 AND 223-256, MASS SPECTROMETRY, OXIDATION AT MET-193; MET-240 AND MET-242 TO METHIONINE SULFOXIDES.
+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.
U79572 Genomic DNA. Translation: AAB58424.1.
U79574 Genomic DNA. Translation: AAB58426.1.
U79573 Genomic DNA. Translation: AAB58425.1.
U79575 Genomic DNA. Translation: AAB58427.1.
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.
PIRS22420.
RefSeqNP_033822.2. NM_009692.4.
UniGeneMm.26743.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LEMNMR-A25-240[»]
ProteinModelPortalQ00623.
SMRQ00623. Positions 25-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ00623. 5 interactions.
MINTMINT-1855786.
STRING10090.ENSMUSP00000034588.

PTM databases

PhosphoSiteQ00623.

2D gel databases

REPRODUCTION-2DPAGEIPI00121209.
Q00623.
SWISS-2DPAGEQ00623.

Proteomic databases

PaxDbQ00623.
PRIDEQ00623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034588; ENSMUSP00000034588; ENSMUSG00000032083.
GeneID11806.
KEGGmmu:11806.
UCSCuc009phb.2. mouse.

Organism-specific databases

CTD335.
MGIMGI:88049. Apoa1.

Phylogenomic databases

eggNOGNOG39720.
GeneTreeENSGT00530000063081.
HOGENOMHOG000033998.
HOVERGENHBG105708.
InParanoidQ00623.
KOK08757.
OMAYRQKVAP.
OrthoDBEOG7TBC3N.
TreeFamTF334458.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_189085. Disease.
REACT_196573. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

CleanExMM_APOA1.
GenevestigatorQ00623.

Family and domain databases

InterProIPR000074. ApoA1_A4_E.
[Graphical view]
PfamPF01442. Apolipoprotein. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPOA1. mouse.
NextBio279667.
PROQ00623.
SOURCESearch...

Entry information

Entry nameAPOA1_MOUSE
AccessionPrimary (citable) accession number: Q00623
Secondary accession number(s): O08855, O09042, Q8BPD5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot