ID H2NFD7_PONAB Unreviewed; 396 AA.
AC H2NFD7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Apolipoprotein A-IV {ECO:0000256|ARBA:ARBA00041197};
DE AltName: Full=Apolipoprotein A4 {ECO:0000256|ARBA:ARBA00042591};
GN Name=APOA4 {ECO:0000313|Ensembl:ENSPPYP00000004470.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000004470.1, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000004470.1, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000004470.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037735}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000256|ARBA:ARBA00008788}.
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DR AlphaFoldDB; H2NFD7; -.
DR Ensembl; ENSPPYT00000004646.2; ENSPPYP00000004470.1; ENSPPYG00000003902.3.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_0_0_1; -.
DR OMA; VIWKYFT; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0042627; C:chylomicron; IEA:Ensembl.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0016209; F:antioxidant activity; IEA:Ensembl.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR GO; GO:0031210; F:phosphatidylcholine binding; IEA:Ensembl.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl.
DR GO; GO:0002227; P:innate immune response in mucosa; IEA:Ensembl.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0034445; P:negative regulation of plasma lipoprotein oxidation; IEA:Ensembl.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IEA:Ensembl.
DR GO; GO:0065005; P:protein-lipid complex assembly; IEA:Ensembl.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:Ensembl.
DR GO; GO:0006982; P:response to lipid hydroperoxide; IEA:Ensembl.
DR GO; GO:0035634; P:response to stilbenoid; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR Gene3D; 1.20.120.20; Apolipoprotein; 2.
DR InterPro; IPR000074; ApoA_E.
DR PANTHER; PTHR18976; APOLIPOPROTEIN; 1.
DR PANTHER; PTHR18976:SF1; APOLIPOPROTEIN A-IV; 1.
DR Pfam; PF01442; Apolipoprotein; 1.
DR SUPFAM; SSF58113; Apolipoprotein A-I; 2.
PE 3: Inferred from homology;
KW HDL {ECO:0000256|ARBA:ARBA00022850};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..396
FT /note="Apolipoprotein A-IV"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003566519"
FT REGION 362..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 45436 MW; F4AAD94E5F0C23EF CRC64;
MFLKAVVLAL ALVAVTGARA EVSADQVATV MWDYFSQLSN NAKEAVEHLQ KSELTQQLNA
LFQDKLGEVN TYAGDLQKKL VPFATELHER LAKDSEKLKE EIRKELEEVR ARLLPHANEV
SQKIGDNVRE LQQRLEPYAD QLRTQVNTQA EQLRRQLTPY AQRMERVLRE NADSLHASLR
PHADELKAKI DQNVEELKGR LTPYADEFKV KIDQTVEELR RSLAPYAQDA QEKLNHQLEG
LAFQMKKNAE ELKTRISASA EELRQRLAPL VEDVRGNLRG NTEGLQKSLA ELGGHLDRQV
EEFRSRVEPY GENFNKALVQ QMEQLRQKLG PHAGDVEGHL SFLEKDLRDK VNSFFSTFKE
KESQDKTLSL PELEQQQEQQ QEQQQEQVQM LAPLES
//
