APOA4_MACFA
ID APOA4_MACFA Reviewed; 429 AA.
AC P33621;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 85.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leukocyte;
RX PubMed=8448212; DOI=10.1016/0167-4781(93)90226-4;
RA Osada J., Pocovi M., Nicolosi R.J., Schaefer E.J., Ordovas J.M.;
RT "Nucleotide sequences of the Macaca fascicularis apolipoprotein C-III and
RT A-IV genes.";
RL Biochim. Biophys. Acta 1172:335-339(1993).
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 -!- 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; X68361; CAA48421.1; -; Genomic_DNA.
DR PIR; S30195; S29565.
DR AlphaFoldDB; P33621; -.
DR SMR; P33621; -.
DR STRING; 9541.XP_005579784.1; -.
DR eggNOG; ENOG502QSC5; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 2.
PE 2: Evidence at transcript level;
KW Chylomicron; HDL; Lipid transport; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..429
FT /note="Apolipoprotein A-IV"
FT /id="PRO_0000001976"
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 359..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 49877 MW; 3D458F551D0DB60C CRC64;
MFLKAVVLTL ALVAVTGARA EVSADQVATV MWDYFSQLSS NAKEAVEHLQ KSELTQQLNA
LFQDKLGEVN TYAGDLQKKL VPFATELHER LAKDSEKLKE EIRKELEEVR ARLLPHANEV
SQKIGENVRE LQQRLEPYTD QLRTQVNTQT EQLRRQLTPY AQRMERVLRE NADSLQTSLR
PHADQLKAKI DQNVEELKER LTPYADEFKV KIDQTVEELR RSLAPYAQDA QEKLNHQLEG
LAFQMKKNAE ELKARISASA EELRQRLAPL AEDMRGNLRG NTEGLQKSLA ELGGHLDRHV
EEFRLRVEPY GENFNKALVQ QMEQLRQKLG PHAGDVEGHL SFLEKDLRDK VNSFFSTFKE
KESQDNTLSL PEPEQQREQQ QEQQQEQEQE QQQQQEQQQQ QEQQREQQQQ EQQQEQQQEQ
VQMLAPLES