APOA4_RAT
ID APOA4_RAT Reviewed; 391 AA.
AC P02651; Q5BK92;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 131.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3009456; DOI=10.1016/s0021-9258(19)84575-1;
RA Boguski M.S., Birkenmeier E.H., Elshourbagy N.A., Taylor J.M., Gordon J.I.;
RT "Evolution of the apolipoproteins. Structure of the rat apo-A-IV gene and
RT its relationship to the human genes for apo-A-I, C-III, and E.";
RL J. Biol. Chem. 261:6398-6407(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6591177; DOI=10.1073/pnas.81.16.5021;
RA Boguski M.S., Elshourbagy N.A., Taylor J.M., Gordon J.I.;
RT "Rat apolipoprotein A-IV contains 13 tandem repetitions of a 22-amino acid
RT segment with amphipathic helical potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5021-5025(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3020028; DOI=10.1016/s0021-9258(18)69300-7;
RA Haddad I.A., Ordovas J.M., Fitzpatrick T., Karathanasis S.K.;
RT "Linkage, evolution, and expression of the rat apolipoprotein A-I, C-III,
RT and A-IV genes.";
RL J. Biol. Chem. 261:13268-13277(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; M00002; AAA85909.1; -; mRNA.
DR EMBL; J02588; AAA40747.1; -; Genomic_DNA.
DR EMBL; M13508; AAA40748.1; -; Genomic_DNA.
DR EMBL; BC091159; AAH91159.1; -; mRNA.
DR PIR; A03095; LPRTA4.
DR RefSeq; NP_036869.1; NM_012737.1.
DR AlphaFoldDB; P02651; -.
DR SMR; P02651; -.
DR IntAct; P02651; 2.
DR iPTMnet; P02651; -.
DR PhosphoSitePlus; P02651; -.
DR PRIDE; P02651; -.
DR Ensembl; ENSRNOT00000080658; ENSRNOP00000069659; ENSRNOG00000055909.
DR GeneID; 25080; -.
DR KEGG; rno:25080; -.
DR UCSC; RGD:2132; rat.
DR CTD; 337; -.
DR RGD; 2132; Apoa4.
DR GeneTree; ENSGT00950000182929; -.
DR InParanoid; P02651; -.
DR OrthoDB; 1299087at2759; -.
DR PhylomeDB; P02651; -.
DR PRO; PR:P02651; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0042627; C:chylomicron; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0016209; F:antioxidant activity; ISO:RGD.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0120020; F:cholesterol transfer activity; ISO:RGD.
DR GO; GO:0005507; F:copper ion binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:RGD.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:RGD.
DR GO; GO:0002227; P:innate immune response in mucosa; ISO:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; ISO:RGD.
DR GO; GO:0055088; P:lipid homeostasis; ISO:RGD.
DR GO; GO:0006869; P:lipid transport; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0034445; P:negative regulation of plasma lipoprotein oxidation; ISO:RGD.
DR GO; GO:0014012; P:peripheral nervous system axon regeneration; IEP:RGD.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:RGD.
DR GO; GO:0033700; P:phospholipid efflux; ISO:RGD.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; ISO:RGD.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISO:RGD.
DR GO; GO:0065005; P:protein-lipid complex assembly; ISO:RGD.
DR GO; GO:0032374; P:regulation of cholesterol transport; ISO:RGD.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; ISO:RGD.
DR GO; GO:0019430; P:removal of superoxide radicals; ISO:RGD.
DR GO; GO:0032094; P:response to food; TAS:RGD.
DR GO; GO:0006982; P:response to lipid hydroperoxide; ISO:RGD.
DR GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
DR GO; GO:0034014; P:response to triglyceride; IEP:RGD.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; IBA:GO_Central.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; ISO:RGD.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 3.
PE 1: Evidence at protein level;
KW Chylomicron; HDL; Lipid transport; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..20
FT CHAIN 21..391
FT /note="Apolipoprotein A-IV"
FT /id="PRO_0000001980"
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 354..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VARIANT 253
FT /note="Q -> H"
SQ SEQUENCE 391 AA; 44456 MW; 24095004A809201D CRC64;
MFLKAVVLTV ALVAITGTQA EVTSDQVANV MWDYFTQLSN NAKEAVEQLQ KTDVTQQLNT
LFQDKLGNIN TYADDLQNKL VPFAVQLSGH LTKETERVRE EIQKELEDLR ANMMPHANKV
SQMFGDNVQK LQEHLRPYAT DLQAQINAQT QDMKRQLTPY IQRMQTTIQD NVENLQSSMV
PFANELKEKF NQNMEGLKGQ LTPRANELKA TIDQNLEDLR SRLAPLAEGV QEKLNHQMEG
LAFQMKKNAE ELQTKVSTNI DQLQKNLAPL VEDVQSKLKG NTEGLQKSLE DLNKQLDQQV
EVFRRAVEPL GDKFNMALVQ QMEKFRQQLG SDSGDVESHL SFLEKNLREK VSSFMSTLQK
KGSPDQPLAL PLPEQVQEQV QEQVQPKPLE S
