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APOA1_OCTDE
ID   APOA1_OCTDE             Reviewed;         263 AA.
AC   P0DMS5;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-MAR-2015, sequence version 1.
DT   03-AUG-2022, entry version 29.
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   Octodon degus (Degu) (Sciurus degus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Octodontidae;
OC   Octodon.
OX   NCBI_TaxID=10160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (DEC-2014).
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. {ECO:0000250|UniProtKB:P02647}.
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 {ECO:0000250|UniProtKB:P02647}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P02648}.
CC   -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:P02648}.
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; AJSA01122103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004636538.1; XM_004636481.1.
DR   AlphaFoldDB; P0DMS5; -.
DR   SMR; P0DMS5; -.
DR   OMA; KEVREMW; -.
DR   Proteomes; UP000515203; Unplaced.
DR   GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR   GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR   GO; GO:0034191; F:apolipoprotein A-I receptor binding; IEA:Ensembl.
DR   GO; GO:0045499; F:chemorepellent activity; IEA:Ensembl.
DR   GO; GO:0015485; F:cholesterol binding; IEA:Ensembl.
DR   GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR   GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR   GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IEA:Ensembl.
DR   GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IEA:Ensembl.
DR   GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR   GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR   GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR   GO; GO:0070508; P:cholesterol import; IEA:Ensembl.
DR   GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
DR   GO; GO:0034380; P:high-density lipoprotein particle assembly; IEA:Ensembl.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0019915; P:lipid storage; IEA:Ensembl.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR   GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IEA:Ensembl.
DR   GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IEA:Ensembl.
DR   GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0051346; P:negative regulation of hydrolase activity; IEA:Ensembl.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl.
DR   GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR   GO; GO:0018206; P:peptidyl-methionine modification; IEA:Ensembl.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR   GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR   GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR   GO; GO:0090205; P:positive regulation of cholesterol metabolic process; IEA:Ensembl.
DR   GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR   GO; GO:0051345; P:positive regulation of hydrolase activity; IEA:Ensembl.
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:0035025; P:positive regulation of Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0018158; P:protein oxidation; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR   GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
DR   GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR   GO; GO:0051180; P:vitamin transport; IEA:Ensembl.
DR   InterPro; IPR000074; ApoA_E.
DR   Pfam; PF01442; Apolipoprotein; 1.
PE   3: Inferred from homology;
KW   Cholesterol metabolism; Glycoprotein; HDL; Lipid metabolism;
KW   Lipid transport; Lipoprotein; Oxidation; Palmitate; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal; Steroid metabolism;
KW   Sterol metabolism; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..263
FT                   /note="Proapolipoprotein A-I"
FT                   /id="PRO_0000432013"
FT   CHAIN           25..263
FT                   /note="Apolipoprotein A-I"
FT                   /id="PRO_0000432014"
FT   CHAIN           25..262
FT                   /note="Truncated apolipoprotein A-I"
FT                   /evidence="ECO:0000250|UniProtKB:P02647"
FT                   /id="PRO_0000432015"
FT   REPEAT          66..87
FT                   /note="1"
FT   REPEAT          88..109
FT                   /note="2"
FT   REPEAT          110..120
FT                   /note="3; half-length"
FT   REPEAT          121..142
FT                   /note="4"
FT   REPEAT          143..164
FT                   /note="5"
FT   REPEAT          165..186
FT                   /note="6"
FT   REPEAT          187..206
FT                   /note="7"
FT   REPEAT          207..228
FT                   /note="8"
FT   REPEAT          229..239
FT                   /note="9; half-length"
FT   REPEAT          240..263
FT                   /note="10"
FT   REGION          66..263
FT                   /note="10 X approximate tandem repeats"
FT   MOD_RES         108
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P02647"
SQ   SEQUENCE   263 AA;  30421 MW;  CB09016B95E3D9C2 CRC64;
     MKAVVLAVAV LFLTGSQARH FWQRDDPQTS WDRVRDFATV YVDAVKESGR DYVAQLEASL
     GKHLNLKLLD NWDTLSTTFS KLRSELGPVT QEFWDNLEKD TEWLRQEMNK DLVEVKEKVQ
     PYLKNFQEKV QLELEHYRKK VEPLGTDLRD GARQKLQELQ EKLTPLGEDL RDRARQHVDE
     LRAQLGPYSD QMRQRLTQRL EALKDSASLA EYQAKAQEHL KTFSEKAKPA LEDLRLGLLP
     VLESLKASFL SSIDEVSKKL SAQ
 
 
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