APOA4_PIG
ID APOA4_PIG Reviewed; 382 AA.
AC O46409; A9LM22;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Apolipoprotein A-IV;
DE Short=Apo-AIV;
DE Short=ApoA-IV;
DE AltName: Full=Apolipoprotein A4;
DE Flags: Precursor;
GN Name=APOA4;
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 [MRNA].
RX PubMed=14697520; DOI=10.1016/j.gene.2003.10.007;
RA Navarro M.A., Acin S., Iturralde M., Calleja L., Carnicer R.,
RA Guzman-Garcia M.A., Gonzalex-Ramon N., Mata P., Isabel B., Lopez-Bote C.J.,
RA Lampreave F., Pineiro A., Osada J.;
RT "Cloning, characterization and comparative analysis of pig plasma
RT apolipoprotein A-IV.";
RL Gene 325:157-164(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 203-382.
RA Chung H.Y.;
RT "Analysis of differentially expressed proteins at different growth stages
RT in pig.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May have a role in chylomicrons and VLDL secretion and
CC catabolism. Required for efficient activation of lipoprotein lipase by
CC ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL
CC and chylomicrons.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06727}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Secreted in plasma.
CC -!- DOMAIN: Nine of the thirteen 22-amino acid tandem repeats (each 22-mer
CC is actually a tandem array of two, A and B, related 11-mers) occurring
CC in this sequence are predicted to be highly alpha-helical, and many of
CC these helices are amphipathic. They may therefore serve as lipid-
CC binding domains with lecithin:cholesterol acyltransferase (LCAT)
CC activating abilities.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; AJ222966; CAA11020.1; -; mRNA.
DR EMBL; EU244462; ABX11183.1; -; mRNA.
DR EMBL; EU263979; ABY64542.1; -; mRNA.
DR RefSeq; NP_999553.1; NM_214388.1.
DR AlphaFoldDB; O46409; -.
DR SMR; O46409; -.
DR STRING; 9823.ENSSSCP00000015992; -.
DR PaxDb; O46409; -.
DR PeptideAtlas; O46409; -.
DR PRIDE; O46409; -.
DR GeneID; 397681; -.
DR KEGG; ssc:397681; -.
DR CTD; 337; -.
DR eggNOG; ENOG502QSC5; Eukaryota.
DR InParanoid; O46409; -.
DR OrthoDB; 1299087at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0034364; C:high-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IBA:GO_Central.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
DR GO; GO:0043691; P:reverse cholesterol transport; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 2.
PE 2: Evidence at transcript level;
KW Chylomicron; HDL; Lipid transport; Reference proteome; Repeat; Secreted;
KW Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..382
FT /note="Apolipoprotein A-IV"
FT /id="PRO_0000001979"
FT REPEAT 33..54
FT /note="1"
FT REPEAT 60..81
FT /note="2"
FT REPEAT 82..103
FT /note="3"
FT REPEAT 115..136
FT /note="4"
FT REPEAT 137..158
FT /note="5"
FT REPEAT 159..180
FT /note="6"
FT REPEAT 181..202
FT /note="7"
FT REPEAT 203..224
FT /note="8"
FT REPEAT 225..246
FT /note="9"
FT REPEAT 247..268
FT /note="10"
FT REPEAT 269..286
FT /note="11"
FT REPEAT 287..308
FT /note="12"
FT REPEAT 309..330
FT /note="13"
FT REGION 33..330
FT /note="13 X 22 AA approximate tandem repeats"
FT REGION 361..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 43294 MW; 2ACA88A02D4379EF CRC64;
MFLKAVVLSL ALVAVTGARA EVNADQVATV MWDYFSQLGS NAKKAVEHLQ KSELTQQLNT
LFQDKLGEVN TYTEDLQKKL VPFATELHER LTKDSEKLKE EIRRELEELR ARLLPHATEV
SQKIGDNVRE LQQRLGPFTG GLRTQVNTQV QQLQRQLKPY AERMESVLRQ NIRNLEASVA
PYADEFKAKI DQNVEELKGS LTPYAEELKA KIDQNVEELR RSLAPYAQDV QEKLNHQLEG
LAFQMKKQAE ELKAKISANA DELRQKLVPV AENVHGHLKG NTEGLQKSLL ELRSHLDQQV
EEFRLKVEPY GETFNKALVQ QVEDLRQKLG PLAGDVEGHL SFLEKDLRDK VNTFFSTLKE
EASQGQSQAL PAQEKAQAPL EG
