APOA1_CANLF
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 03-AUG-2022, entry version 123.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A60940; LPDGA1.
DR AlphaFoldDB; P02648; -.
DR SMR; P02648; -.
DR STRING; 9612.ENSCAFP00000019630; -.
DR UCD-2DPAGE; P02648; -.
DR PaxDb; P02648; -.
DR PRIDE; P02648; -.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR InParanoid; P02648; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
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: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 InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
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
