ID   APOA5_MIRAN             Reviewed;         367 AA.
AC   P0DTS2;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2019, sequence version 1.
DT   25-MAY-2022, entry version 6.
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   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RL   Unpublished observations (OCT-2019).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: Minor apolipoprotein mainly associated with HDL and to a
CC       lesser extent with VLDL. May also be associated with chylomicrons (By
CC       similarity). Important determinant of plasma triglyceride (TG) levels
CC       by both being a potent stimulator of apo-CII lipoprotein lipase (LPL)
CC       TG hydrolysis and an inhibitor of the hepatic VLDL-TG production rate
CC       (without affecting the VLDL-apoB production rate) (By similarity).
CC       Activates poorly lecithin:cholesterol acyltransferase (LCAT) and does
CC       not enhance efflux of cholesterol from macrophages (By similarity).
CC       Binds heparin (By similarity). {ECO:0000250|UniProtKB:Q6Q788,
CC       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   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:Q6Q788}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC       {ECO:0000305}.
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DR   EMBL; PITE01000000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DTS2; -.
DR   SMR; P0DTS2; -.
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; 1.
PE   3: Inferred from homology;
KW   Chylomicron; Coiled coil; Endosome; Golgi apparatus; HDL; Lipid transport;
KW   Phosphoprotein; Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..367
FT                   /note="Apolipoprotein A-V"
FT                   /id="PRO_0000448769"
FT   REGION          71..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6Q788"
SQ   SEQUENCE   367 AA;  41226 MW;  EEF7FB5941659FED CRC64;
     MVAVLTWALA LLSAFATVQT QKGFWDYFSQ SSGDKSKVAR VQQQKLIWEP TSLKDSLEQD
     LSNMDKFLEK LGPLSGQGRE PPGLPHDPEG MRQQLQEELA EVRARLEPYM AEAHQQVGWN
     LEGLRRQLKP YTVELMEQVA RRVQELQEQL RVVGEGTKAQ LLGGVDEARG LLQELQTRVV
     QHTGRVGELF HPYAQRLVTG IGRHVQELHR SVAPHAAASS ARLSRCVQTL SRKLTLKAEA
     LHARIQQNLD RLREELSAFA RAGAGGAEEG ANPDPQMLPQ EVRQRLQAFR HDTFLQIADF
     TRAIDQETEE VQLQLAPPPP GHSAFAPELL QADSSEARSK LQARLEDLWE DINDSLHDRG
     LSHLEEP