ID   APOA1_CANLF             Reviewed;         266 AA.
AC   P02648;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Apolipoprotein A-I;
DE            Short=Apo-AI;
DE            Short=ApoA-I;
DE   AltName: Full=Apolipoprotein A1;
DE   Contains:
DE     RecName: Full=Proapolipoprotein A-I;
DE              Short=ProapoA-I;
DE   Contains:
DE     RecName: Full=Truncated apolipoprotein A-I;
DE   Flags: Precursor;
GN   Name=APOA1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2515239;
RA   Luo C.-C., Li W.-H., Chan L.;
RT   "Structure and expression of dog apolipoprotein A-I, E, and C-I mRNAs:
RT   implications for the evolution and functional constraints of apolipoprotein
RT   structure.";
RL   J. Lipid Res. 30:1735-1746(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-139; 142-150; 155-172; 184-196 AND 201-266, MASS
RP   SPECTROMETRY, OXIDATION AT MET-109, GLYCOSYLATION, AND PALMITOYLATION.
RC   TISSUE=Plasma;
RX   PubMed=20483223; DOI=10.1016/j.cbd.2008.08.002;
RA   Puppione D.L., Bassilian S., Souda P., MacDonald M.H., Halgand F.,
RA   Hagland F., Whitelegge J.P.;
RT   "Mass spectral analysis of the apolipoproteins on dog (Canis lupus
RT   familiaris) high density lipoproteins. Detection of apolipoprotein A-II.";
RL   Comp. Biochem. Physiol. 3:290-296(2008).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-266.
RX   PubMed=6801039; DOI=10.1016/s0021-9258(19)81058-x;
RA   Chung H., Randolph A., Reardon I., Heinrikson R.L.;
RT   "The covalent structure of apolipoprotein A-I from canine high density
RT   lipoproteins.";
RL   J. Biol. Chem. 257:2961-2967(1982).
RN   [4]
RP   PROTEIN SEQUENCE OF 25-57 AND 262-265.
RX   PubMed=179887; DOI=10.1016/0014-5793(76)80338-9;
RA   Nakai T., Whayne T.F., Tang J.;
RT   "The amino- and carboxyl-terminal sequences of canine apolipoprotein A-i.";
RL   FEBS Lett. 64:409-411(1976).
RN   [5]
RP   PROTEIN SEQUENCE OF 25-37.
RC   TISSUE=Heart;
RX   PubMed=9504812; DOI=10.1002/elps.1150181514;
RA   Dunn M.J., Corbett J.M., Wheeler C.H.;
RT   "HSC-2DPAGE and the two-dimensional gel electrophoresis database of dog
RT   heart proteins.";
RL   Electrophoresis 18:2795-2802(1997).
CC   -!- FUNCTION: Participates in the reverse transport of cholesterol from
CC       tissues to the liver for excretion by promoting cholesterol efflux from
CC       tissues and by acting as a cofactor for the lecithin cholesterol
CC       acyltransferase (LCAT). As part of the SPAP complex, activates
CC       spermatozoa motility.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with APOA1BP and CLU.
CC       Component of a sperm activating protein complex (SPAP), consisting of
CC       APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and
CC       albumin. Interacts with NDRG1. Interacts with SCGB3A2 (By similarity).
CC       Interacts with NAXE and YJEFN3 (By similarity).
CC       {ECO:0000250|UniProtKB:G5BQH5, ECO:0000250|UniProtKB:P02647,
CC       ECO:0000250|UniProtKB:P04639}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Major protein of plasma HDL, also found in
CC       chylomicrons. Synthesized in the liver and small intestine.
CC   -!- PTM: Palmitoylated. {ECO:0000269|PubMed:20483223}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:20483223}.
CC   -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC       {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=27468.3;
CC       Mass_error=0.071; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:20483223};
CC   -!- MASS SPECTROMETRY: [Proapolipoprotein A-I]: Mass=28354;
CC       Method=Electrospray; Evidence={ECO:0000269|PubMed:20483223};
CC   -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=27470;
CC       Method=Electrospray; Note=Glycosylated ApoA-I.;
CC       Evidence={ECO:0000269|PubMed:20483223};
CC   -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=27733; Mass_error=0.071;
CC       Method=Electrospray; Note=Stearoylated ApoA-I.;
CC       Evidence={ECO:0000269|PubMed:20483223};
CC   -!- MASS SPECTROMETRY: [Apolipoprotein A-I]: Mass=27707;
CC       Method=Electrospray; Note=Palmitoylated ApoA-I.;
CC       Evidence={ECO:0000269|PubMed:20483223};
CC   -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC       {ECO:0000305}.
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DR   PIR; A60940; LPDGA1.
DR   AlphaFoldDB; P02648; -.
DR   SMR; P02648; -.
DR   STRING; 9615.ENSCAFP00000019630; -.
DR   PaxDb; 9612-ENSCAFP00000019630; -.
DR   eggNOG; ENOG502S1XQ; Eukaryota.
DR   InParanoid; P02648; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IBA:GO_Central.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR   GO; GO:0018206; P:peptidyl-methionine modification; ISS:UniProtKB.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR   GO; GO:1902995; P:positive regulation of phospholipid efflux; ISS:UniProtKB.
DR   GO; GO:0018158; P:protein oxidation; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
DR   Gene3D; 1.20.5.20; -; 1.
DR   Gene3D; 6.10.140.380; -; 1.
DR   Gene3D; 1.20.120.20; Apolipoprotein; 1.
DR   InterPro; IPR000074; ApoA_E.
DR   PANTHER; PTHR18976; APOLIPOPROTEIN; 1.
DR   PANTHER; PTHR18976:SF11; APOLIPOPROTEIN A-I; 1.
DR   Pfam; PF01442; Apolipoprotein; 1.
DR   SUPFAM; SSF58113; Apolipoprotein A-I; 1.
DR   UCD-2DPAGE; P02648; -.
PE   1: Evidence at protein level;
KW   Cholesterol metabolism; Direct protein sequencing; Glycoprotein; HDL;
KW   Lipid metabolism; Lipid transport; Lipoprotein; Oxidation; Palmitate;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW   Steroid metabolism; Sterol metabolism; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:20483223"
FT   CHAIN           19..266
FT                   /note="Proapolipoprotein A-I"
FT                   /id="PRO_0000425320"
FT   CHAIN           25..266
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000001937"
FT   CHAIN           25..265
FT                   /note="Truncated apolipoprotein A-I"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000416572"
FT   REPEAT          67..88
FT                   /note="1"
FT   REPEAT          89..110
FT                   /note="2"
FT   REPEAT          111..121
FT                   /note="3; half-length"
FT   REPEAT          122..143
FT                   /note="4"
FT   REPEAT          144..165
FT                   /note="5"
FT   REPEAT          166..187
FT                   /note="6"
FT   REPEAT          188..209
FT                   /note="7"
FT   REPEAT          210..231
FT                   /note="8"
FT   REPEAT          232..242
FT                   /note="9; half-length"
FT   REPEAT          243..266
FT                   /note="10"
FT   REGION          67..266
FT                   /note="10 X approximate tandem repeats"
FT   MOD_RES         109
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:20483223"
FT   CONFLICT        168
FT                   /note="A -> G (in Ref. 2; AA sequence and 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202
FT                   /note="E -> Q (in Ref. 2; AA sequence and 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="E -> Q (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264..266
FT                   /note="NAQ -> A (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   266 AA;  30196 MW;  A3202620C28A869D CRC64;
     MKAALLTLAV LFLTGSQARH FWQQDEPQSP WDRVKDLATV YVDAVKDSGR DYVAQFEASA
     LGKQLNLKLL DNWDSLSSTV TKLREQIGPV TQEFWDNLEK ETEVLRQEMS KDLEEVKQKV
     QPYLDDFQKK WQEEVELYRQ KVAPLGSELR EGARQKLQEL QEKLSPLAEE LRDRARTHVD
     ALRAQLAPYS DDLRERLAAR LEALKEGGGA SLAEYHARAS EQLSALGEKA RPALEDLRQG
     LLPVLESFKV SLLAAIDEAT KKLNAQ
//