APOA4_BOVIN
ID APOA4_BOVIN Reviewed; 380 AA.
AC Q32PJ2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06727}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; BC108096; AAI08097.1; -; mRNA.
DR RefSeq; NP_001032557.1; NM_001037480.1.
DR AlphaFoldDB; Q32PJ2; -.
DR SMR; Q32PJ2; -.
DR STRING; 9913.ENSBTAP00000026345; -.
DR PaxDb; Q32PJ2; -.
DR PeptideAtlas; Q32PJ2; -.
DR PRIDE; Q32PJ2; -.
DR GeneID; 537301; -.
DR KEGG; bta:537301; -.
DR CTD; 337; -.
DR eggNOG; ENOG502QSC5; Eukaryota.
DR InParanoid; Q32PJ2; -.
DR OrthoDB; 1299087at2759; -.
DR Proteomes; UP000009136; 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:0000255"
FT CHAIN 21..380
FT /note="Apolipoprotein A-IV"
FT /id="PRO_0000259419"
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..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 380 AA; 43018 MW; D080922ACEEB1F1D CRC64;
MFLKAVVLSL ALVAVTGAEA EVNADQVATV IWDYFSQLGN NAKKAVEHIQ KSELTQQLNT
LFQDKLGEVS TYTDDLQKKL VPFATELHER LTKDSEKLKE EIRKELEDLR ARLLPHATEV
SQKIGDNVRE LQQRLGPYAE ELRTQVDTQA QQLRRQLTPY VERMEKVMRQ NLDQLQASLA
PYAEELQATV NQRVEELKGR LTPYADQLQT KIEENVEELR RSLAPYAQDV QGKLNHQLEG
LAFQMKKHAE ELKAKISAKA EELRQGLVPL VNSVHGSQLG NAEDLQKSLA ELSSRLDQQV
EDFRRTVGPY GETFNKAMVQ QLDTLRQKLG PLAGDVEDHL SFLEKDLRDK VSSFFNTLKE
KESQAPALPA QEEMPVPLGG
