APOA4_ACIJB
ID APOA4_ACIJB Reviewed; 382 AA.
AC P0DSO8;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 1.
DT 25-MAY-2022, entry version 8.
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 Acinonyx jubatus (Cheetah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Acinonychinae;
OC Acinonyx.
OX NCBI_TaxID=32536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scott A., Pukazhenthi B., Koepfli K.-P., Mohr D., Crosier A., O'Brien S.J.,
RA Tamazian G., Dobrynin P., Komissarov A., Kliver S., Krasheninnikova K.;
RT "Linked reads assembly of the African cheetah.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (JUN-2019).
CC -!- FUNCTION: May have a role in chylomicrons and VLDL secretion and
CC catabolism (By similarity). Required for efficient activation of
CC lipoprotein lipase by ApoC-II; potent activator of LCAT (By
CC similarity). Apoa-IV is a major component of HDL and chylomicrons (By
CC similarity). {ECO:0000250|UniProtKB:P06727}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06727}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P06727}.
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 (By similarity). They may therefore serve
CC as lipid-binding domains with lecithin:cholesterol acyltransferase
CC (LCAT) activating abilities (By similarity).
CC {ECO:0000250|UniProtKB:P06727}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000305}.
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DR EMBL; QURD01003265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DSO8; -.
DR SMR; P0DSO8; -.
DR Proteomes; UP000504626; 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 3: Inferred from homology;
KW Chylomicron; HDL; Lipid transport; Reference proteome; 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_0000447661"
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 362..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 43722 MW; 1B948A1B44C522BA CRC64;
MFLRAVVLTL ALVAVTGARA EVSPDQVATV VWDYFSQLSN NAKEAVEHLQ QSELTQQLNA
LFQDKLGQVN TYADNLQKKL VPFATELHER LTKDSEKLKE EIRKELEELR ARLLPHANEV
SQKIGDNVRE LQQRLGPYAD ELRTQVNTHA EHLRRHLTSH AQRMEAVLRE NVDNLQSSLT
PYADEFKAKI DRNIEELKGH LTPYADELKV KIDQNVEELR RSLAPYAQDV QEKLNHQLEG
LAFQMKKNAE ELKAKITANA DELRQRLAPV VEDVRGKLRD NAKGLQESLA QLNSHLDRQV
EEFRHNMGPY GDTFNRALVQ QVEELRQKLG SYAGGMEDHL SFLEKDLRDK VNSFFSTLKE
KENQDMPLAL PEQEQAPGPL ES