ID   APOA5_NEOSC             Reviewed;         367 AA.
AC   A0A2Y9HKE5;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   25-MAY-2022, entry version 14.
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   Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Neomonachus.
OX   NCBI_TaxID=29088;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood;
RA   Mohr D.W., Scott A.F.;
RT   "Improved de novo genome assembly: linked-read sequencing combined with
RT   optical mapping produce a high quality mammalian genome at relatively low
RT   cost.";
RL   Submitted (MAY-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RL   Unpublished observations (OCT-2019).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}.
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; NINY01000000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2Y9HKE5; -.
DR   SMR; A0A2Y9HKE5; -.
DR   Proteomes; UP000248481; Genome assembly.
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; Reference proteome; Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..367
FT                   /note="Apolipoprotein A-V"
FT                   /id="PRO_5015986864"
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;  41156 MW;  A879A1AB5D067EAF CRC64;
     MVAVLTWALA LLSAFATVQT QKGFWDYFSQ SSGDKSKVAR VQQQKLTWEP TSLKDSLEQD
     LSNMDKFLEK LGPLSGQGRE PPGLPHDPEG MRQQLQEELA EVRARLEPYM AEAHQQVGWN
     LEGLRRQLKP YTVELMEQVA RRVQELQEQL RVVGEGTKAQ LLGGVDEARG LLQELQTRVV
     QHTGRVRELF HPYAQRLVTG IGRHVQELHR SVAPHAAASS ARLSRCVQTL SRKLTLKAEA
     LHARIQQNLG QLREELSAFA SAGAGGAEEG ANPDAQMLSQ EVRQRLQAFR HDTFLQIADF
     TRAIDQETEE VQLQLAPPPP GHSAFAPEFL QADSSEARSK LQARLEDLWE DINDSLHDRG
     LSHLEEP