Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P02648 (APOA1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length266 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. Synthesized in the liver and small intestine.

Post-translational modification

Palmitoylated. Ref.2

Glycosylated. Ref.2

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 27468.3±0.071 Da from positions 25 - 266. Determined by ESI. Ref.2

Molecular mass is 28354 Da from positions 19 - 266. Determined by ESI. Ref.2

Molecular mass is 27470 Da from positions 25 - 266. Determined by ESI. Glycosylated ApoA-I. Ref.2

Molecular mass is 27733±0.071 Da from positions 25 - 266. Determined by ESI. Stearoylated ApoA-I. Ref.2

Molecular mass is 27707 Da from positions 25 - 266. Determined by ESI. Palmitoylated ApoA-I. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.2
Chain19 – 266248Proapolipoprotein A-I
PRO_0000425320
Chain25 – 266242Apolipoprotein A-I
PRO_0000001937
Chain25 – 265241Truncated apolipoprotein A-I By similarity
PRO_0000416572

Regions

Repeat67 – 88221
Repeat89 – 110222
Repeat111 – 121113; half-length
Repeat122 – 143224
Repeat144 – 165225
Repeat166 – 187226
Repeat188 – 209227
Repeat210 – 231228
Repeat232 – 242119; half-length
Repeat243 – 2662410
Region67 – 26620010 X approximate tandem repeats

Amino acid modifications

Modified residue1091Methionine sulfoxide

Experimental info

Sequence conflict1681A → G AA sequence Ref.2
Sequence conflict1681A → G AA sequence Ref.3
Sequence conflict2021E → Q AA sequence Ref.2
Sequence conflict2021E → Q AA sequence Ref.3
Sequence conflict2351E → Q AA sequence Ref.3
Sequence conflict264 – 2663NAQ → A AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
P02648 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: A3202620C28A869D

FASTA26630,196
        10         20         30         40         50         60 
MKAALLTLAV LFLTGSQARH FWQQDEPQSP WDRVKDLATV YVDAVKDSGR DYVAQFEASA 

        70         80         90        100        110        120 
LGKQLNLKLL DNWDSLSSTV TKLREQIGPV TQEFWDNLEK ETEVLRQEMS KDLEEVKQKV 

       130        140        150        160        170        180 
QPYLDDFQKK WQEEVELYRQ KVAPLGSELR EGARQKLQEL QEKLSPLAEE LRDRARTHVD 

       190        200        210        220        230        240 
ALRAQLAPYS DDLRERLAAR LEALKEGGGA SLAEYHARAS EQLSALGEKA RPALEDLRQG 

       250        260 
LLPVLESFKV SLLAAIDEAT KKLNAQ 

« Hide

References

[1]"Structure and expression of dog apolipoprotein A-I, E, and C-I mRNAs: implications for the evolution and functional constraints of apolipoprotein structure."
Luo C.-C., Li W.-H., Chan L.
J. Lipid Res. 30:1735-1746(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Mass spectral analysis of the apolipoproteins on dog (Canis lupus familiaris) high density lipoproteins. Detection of apolipoprotein A-II."
Puppione D.L., Bassilian S., Souda P., MacDonald M.H., Halgand F., Hagland F., Whitelegge J.P.
Comp. Biochem. Physiol. 3:290-296(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-139; 142-150; 155-172; 184-196 AND 201-266, MASS SPECTROMETRY, OXIDATION, GLYCOSYLATION, PALMITOYLATION.
Tissue: Plasma.
[3]"The covalent structure of apolipoprotein A-I from canine high density lipoproteins."
Chung H., Randolph A., Reardon I., Heinrikson R.L.
J. Biol. Chem. 257:2961-2967(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-266.
[4]"The amino- and carboxyl-terminal sequences of canine apolipoprotein A-i."
Nakai T., Whayne T.F., Tang J.
FEBS Lett. 64:409-411(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-57 AND 262-265.
[5]"HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog heart proteins."
Dunn M.J., Corbett J.M., Wheeler C.H.
Electrophoresis 18:2795-2802(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-37.
Tissue: Heart.

Cross-references

Sequence databases

PIRLPDGA1. A60940.

3D structure databases

ProteinModelPortalP02648.
SMRP02648. Positions 25-266.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000019630.

2D gel databases

UCD-2DPAGEP02648.

Proteomic databases

PaxDbP02648.
PRIDEP02648.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG39720.
HOGENOMHOG000033998.
HOVERGENHBG105708.
InParanoidP02648.

Family and domain databases

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

Entry information

Entry nameAPOA1_CANFA
AccessionPrimary (citable) accession number: P02648
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 15, 1998
Last modified: March 19, 2014
This is version 101 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