APOA1_RABIT
ID APOA1_RABIT Reviewed; 266 AA.
AC P09809;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 25-MAY-2022, entry version 121.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Intestine;
RX PubMed=3121329; DOI=10.1111/j.1432-1033.1987.tb13672.x;
RA Pan T.C., Hao Q.L., Yamin T.T., Dai P.H., Chen B.S., Chen S.L., Kroon P.A.,
RA Chao Y.S.;
RT "Rabbit apolipoprotein A-I mRNA and gene. Evidence that rabbit
RT apolipoprotein A-I is synthesized in the intestine but not in the liver.";
RL Eur. J. Biochem. 170:99-104(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=2ZAP AI; TISSUE=Small intestine;
RA Paraskevopoulou T.B., Kritis A., Zannis V.I.;
RL Submitted (JUL-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 25-266.
RX PubMed=3095115; DOI=10.1111/j.1432-1033.1986.tb09990.x;
RA Yang C., Yang T., Pownall H.J., Gotto A.M. Jr.;
RT "The primary structure of apolipoprotein A-I from rabbit high-density
RT lipoprotein.";
RL Eur. J. Biochem. 160:427-431(1986).
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.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: Palmitoylated. {ECO:0000250}.
CC -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; X06658; CAA29857.1; -; mRNA.
DR EMBL; X06659; CAA29858.1; -; Genomic_DNA.
DR EMBL; X15908; CAA34024.1; -; mRNA.
DR PIR; A24998; A24998.
DR PIR; S00230; LPRB1B.
DR PIR; S06064; LPRB1Z.
DR RefSeq; NP_001095157.1; NM_001101687.1.
DR AlphaFoldDB; P09809; -.
DR SMR; P09809; -.
DR STRING; 9986.ENSOCUP00000009241; -.
DR GeneID; 100009253; -.
DR KEGG; ocu:100009253; -.
DR CTD; 335; -.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR InParanoid; P09809; -.
DR OrthoDB; 1553412at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0042277; F:peptide binding; IPI:ARUK-UCL.
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 CHAIN 19..266
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425328"
FT CHAIN 25..266
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000001952"
FT CHAIN 25..265
FT /note="Truncated apolipoprotein A-I"
FT /evidence="ECO:0000250"
FT /id="PRO_0000416579"
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:0000250"
FT CONFLICT 18
FT /note="A -> R (in Ref. 1; CAA29858)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="V -> I (in Ref. 1; CAA29858)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="Y -> F (in Ref. 1; CAA29857)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="A -> V (in Ref. 1; CAA29858 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="R -> G (in Ref. 1; CAA29858/CAA29857)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="N -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="Missing (in Ref. 1; CAA29858/CAA29857)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="S -> K (in Ref. 1; CAA29858/CAA29857)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..256
FT /note="VL -> LV (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="L -> V (in Ref. 1; CAA29858/CAA29857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 266 AA; 30591 MW; 0FF6DB386497C7D2 CRC64;
MKAVVLTLAV LFLTGSQARH FWQRDEPRSS WDKIKDFATV YVDTVKDSGR EYVAQFEASA
FGKQLNLKLL DNWDSLSSTV SKLQEQLGPV TQEFWDNLEK ETEGLREEMN KDLQEVRQKV
QPYLDEFQKK WQEEVERYRQ KVEPLGAELR ESARQKLTEL QEKLSPLAEE LRDSARTHVD
TLRTKLAPYS NELQQRLAAR LESIKEGGGA SLAEYQAKAR EHLSVLSEKA RPALEDLRQG
LLPVLESFKA SVQNVLDEAT KKLNTQ
