ID   APOA5_ACIJB             Reviewed;         370 AA.
AC   P0DSO9;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Apolipoprotein A-V;
DE            Short=Apo-AV;
DE            Short=ApoA-V;
DE   AltName: Full=Apolipoprotein A5;
DE   Flags: Precursor;
GN   Name=APOA5;
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RL   Unpublished observations (JUN-2019).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: Minor apolipoprotein mainly associated with HDL and to a
CC       lesser extent with VLDL (By similarity). May also be associated with
CC       chylomicrons (By similarity). Important determinant of plasma
CC       triglyceride (TG) levels by both being a potent stimulator of apo-CII
CC       lipoprotein lipase (LPL) TG hydrolysis and an inhibitor of the hepatic
CC       VLDL-TG production rate (without affecting the VLDL-apoB production
CC       rate) (By similarity). Activates poorly lecithin:cholesterol
CC       acyltransferase (LCAT) and does not enhance efflux of cholesterol from
CC       macrophages (By similarity). Binds heparin (By similarity).
CC       {ECO:0000250|UniProtKB:Q6Q788, ECO:0000250|UniProtKB:Q8C7G5}.
CC   -!- SUBUNIT: Interacts with GPIHBP1 (By similarity). Interacts with SORL1;
CC       this interaction leads to APOA5 internalization and sorting either to
CC       lysosomes and degradation, or to the trans-Golgi network (By
CC       similarity). {ECO:0000250|UniProtKB:Q6Q788}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q6Q788}. Early
CC       endosome {ECO:0000250|UniProtKB:Q6Q788}. Late endosome
CC       {ECO:0000250|UniProtKB:Q6Q788}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000250|UniProtKB:Q6Q788}. Note=In the presence of SORL1,
CC       internalized to early endosomes, sorted in a retrograde fashion to late
CC       endosomes, from which a portion is sent to lysosomes and degradation,
CC       another portion is sorted to the trans-Golgi network.
CC       {ECO:0000250|UniProtKB:Q6Q788}.
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; P0DSO9; -.
DR   SMR; P0DSO9; -.
DR   Proteomes; UP000504626; Unplaced.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0034361; C:very-low-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; Endosome; Golgi apparatus; HDL; Lipid transport;
KW   Phosphoprotein; Reference proteome; Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..370
FT                   /note="Apolipoprotein A-V"
FT                   /id="PRO_0000447662"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6Q788"
SQ   SEQUENCE   370 AA;  41443 MW;  F166F28A7F2AC1AD CRC64;
     MASMIALLTW ALALLPALAS AQTQKGFWDY FSQSSGDKGK AEQVQRQKLA WEPTSLKDSL
     EQDLSNIDKF LEKLGPLSGQ AREPPALPQD PADMRRQLQE ELVEVRARLE PYMAEAHEQV
     GWNLESLRRQ LKPYTAELME QVALRVQELQ EQLRVVGEGT KAQLLGGVDE ARGLLRELQN
     LVAHHTGRVQ ALFHPYAQRL VSGIGRHVQE LHRSVAPHAV ASPARLSRCV QTLSRKLTLK
     AKALHARIQQ NLDQLREELS AFAGARADGA VEGTSQDPQV LSQEVRQRLQ AFRQDTFLQI
     ADFTRAMDQE TEEVQLQLAP PPPGHSAFAP EFLQADSGKA LSKLQARLED LWEDINYSLH
     DHGLGHQEEP