APOA4_MIRAN
ID APOA4_MIRAN Reviewed; 382 AA.
AC P0DTS0;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 1.
DT 25-MAY-2022, entry version 5.
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 Mirounga angustirostris (Northern elephant seal).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Mirounga.
OX NCBI_TaxID=9716;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Johnson J., Muren E., Swofford R., Turner-Maier J., Marinescu V.D.,
RA Genereux D.P., Alfoldi J., Birren B., Karlsson E.K., Lindblad-Toh K.;
RT "The 200 mammals project: sequencing genomes by a novel cost-effective
RT method, yielding a high resolution annotation of the human genome.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (OCT-2019).
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:0000250|UniProtKB:P33621}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06727}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P33621}.
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. {ECO:0000250|UniProtKB:P33621}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PITE01000000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DTS0; -.
DR SMR; P0DTS0; -.
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 3: Inferred from homology;
KW Chylomicron; HDL; Lipid transport; Phosphoprotein; Repeat; Secreted;
KW Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..382
FT /note="Apolipoprotein A-IV"
FT /id="PRO_0000448767"
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"
SQ SEQUENCE 382 AA; 43620 MW; 24D07EDF080CA306 CRC64;
MFLKAVVLTL SLVAVTGAQA EVSANQVATV VWDYFSQLSN NAKEAVEHLQ KSELTQQLNA
LFQDKIGQVN TYTDNLQKKL VSFAMELHER LRKDSEKLKE EIRKELEELR AGLLPHADEV
SRKIGDNMHE LQQRLGPYAE ELRTQVNTHA EHLRNQLTAH AQRMETTLRQ NVGNLQASLT
PYADELKAKI DQNVEELKGH LTPYADELKV KIDQNVEDLR RSLAPYAQDV QEKLNHQLEG
LAFQMKKNAE ELKAKISANA DELRQKLVPV AEVVRGKLRD NTEELQKSLA ELSSHLDRQV
EEFRRNMGPY GETFNKALLQ QVEELRQKLG PYAGDVEDHL SFLEKDLRDK VNSFFSTLEE
KENQDMLVAV PELQLTPVPL ES