APOA1_PIG
ID APOA1_PIG Reviewed; 265 AA.
AC P18648;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 4.
DT 25-MAY-2022, entry version 141.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8468059; DOI=10.1006/geno.1993.1119;
RA Birchbauer A., Knipping G., Juritsch B., Aschauer H., Zechner R.;
RT "Characterization of the apolipoprotein AI and CIII genes in the domestic
RT pig.";
RL Genomics 15:643-652(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain, and Liver;
RX PubMed=8294940; DOI=10.1046/j.1471-4159.1994.62020788.x;
RA Moeckel B., Zinke H., Flach R., Weiss B., Weiler-Guettler H., Gassen H.;
RT "Expression of apolipoprotein A-I in porcine brain endothelium in vitro.";
RL J. Neurochem. 62:788-798(1994).
RN [3]
RP PROTEIN SEQUENCE OF 25-265.
RA Hasler-Rapacz J.O., Chaudhary R., Chowdhary B.P., Trieu V.N., Jackson K.,
RA Gustavsson I., Rapacz J.;
RL Submitted (OCT-1995) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 25-34.
RX PubMed=178359; DOI=10.1021/bi00654a021;
RA Mahley R.W., Weisgraber K.H., Innerarity T., Brewer H.B. Jr.;
RT "Characterization of the plasma lipoproteins and apoproteins of the
RT Erythrocebus patas monkey.";
RL Biochemistry 15:1928-1933(1976).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-265.
RC TISSUE=Brain;
RX PubMed=2105375; DOI=10.1111/j.1471-4159.1990.tb01892.x;
RA Weiler-Guettler H., Sommerfeldt M., Papandrikopoulou A., Mischek U.,
RA Bonitz D., Frey A., Grupe M., Scheerer J., Gassen H.G.;
RT "Synthesis of apolipoprotein A-1 in pig brain microvascular endothelial
RT cells.";
RL J. Neurochem. 54:444-450(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-265, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8428656; DOI=10.1016/0378-1119(93)90121-i;
RA Trieu V.N., Hasler-Rapacz J., Rapacz J., Black D.D.;
RT "Sequences and expression of the porcine apolipoprotein A-I and C-III
RT mRNAs.";
RL Gene 123:173-179(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-265.
RX PubMed=7916724; DOI=10.1016/0378-1119(93)90105-c;
RA Trieu V.N., Patel B., Zhan R., Black D.D.;
RT "Sequence of the porcine apoA-I gene.";
RL Gene 134:267-270(1993).
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 predominantly in the intestine and the liver.
CC {ECO:0000269|PubMed:8428656}.
CC -!- DEVELOPMENTAL STAGE: Liver apoa-I expressed in fetal, newborn and
CC suckling animals. Intestinal apoA-I only expressed in postpartum
CC animals.
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; L00626; AAA30992.1; -; Genomic_DNA.
DR EMBL; X69477; CAA49234.1; -; mRNA.
DR EMBL; X17057; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X59414; CAA42050.1; -; mRNA.
DR PIR; A46018; A46018.
DR PIR; JT0672; JT0672.
DR PIR; S21830; S21830.
DR PIR; S31394; S31394.
DR RefSeq; NP_999563.1; NM_214398.1.
DR AlphaFoldDB; P18648; -.
DR SMR; P18648; -.
DR STRING; 9823.ENSSSCP00000015994; -.
DR PaxDb; P18648; -.
DR PeptideAtlas; P18648; -.
DR PRIDE; P18648; -.
DR GeneID; 397691; -.
DR KEGG; ssc:397691; -.
DR CTD; 335; -.
DR eggNOG; ENOG502S1XQ; Eukaryota.
DR HOGENOM; CLU_058447_1_0_1; -.
DR InParanoid; P18648; -.
DR OrthoDB; 1553412at2759; -.
DR TreeFam; TF334458; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P18648; SS.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
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:0000250"
FT CHAIN 19..265
FT /note="Proapolipoprotein A-I"
FT /id="PRO_0000425336"
FT CHAIN 25..265
FT /note="Apolipoprotein A-I"
FT /id="PRO_0000001950"
FT CHAIN 25..264
FT /note="Truncated apolipoprotein A-I"
FT /evidence="ECO:0000250"
FT /id="PRO_0000416578"
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..142
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..230
FT /note="8"
FT REPEAT 231..241
FT /note="9; half-length"
FT REPEAT 242..265
FT /note="10"
FT REGION 67..265
FT /note="10 X approximate tandem repeats"
FT MOD_RES 109
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 135
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT CONFLICT 108
FT /note="E -> K (in Ref. 5; X17057)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="Missing (in Ref. 2; CAA49234 and 5; X17057)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="D -> S (in Ref. 6; CAA42050)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="E -> A (in Ref. 2; CAA49234 and 5; X17057)"
FT /evidence="ECO:0000305"
FT CONFLICT 185..186
FT /note="HV -> QL (in Ref. 1; AAA30992 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="G -> D (in Ref. 2; CAA49234 and 5; X17057)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> G (in Ref. 6; CAA42050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 30325 MW; 2C6E578318ECF69C CRC64;
MKAVVLTLAV LFLTGSQARH FWQQDDPQSP WDRVKDFATV YVDAIKDSGR DYVAQFEASA
LGKHLNLKLL DNWDSLGSTF TKVREQLGPV TQEFWDNLEK ETEALRQEMS KDLEEVKKKV
QPYLDDFQNK WQEEMETYRQ KMAPLGAEFR EGARQKVQEL QEKLSPLAEE LRDRLRAHVE
ALRQHVAPYS DDLRQRMAAR FEALKEGGGS LAEYQAKAQE QLKALGEKAK PALEDLRQGL
LPVLENLKVS ILAAIDEASK KLNAQ
