APOA5_RAT
ID APOA5_RAT Reviewed; 367 AA.
AC Q9QUH3; Q5FVT8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Apolipoprotein A-V;
DE Short=Apo-AV;
DE Short=ApoA-V;
DE AltName: Full=Apolipoprotein A5;
DE AltName: Full=Regeneration-associated protein 3;
DE Flags: Precursor;
GN Name=Apoa5; Synonyms=Rap3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=11577099; DOI=10.1074/jbc.m106888200;
RA van Der Vliet H.N., Sammels M.G., Leegwater A.C.J., Levels J.H.M.,
RA Reitsma P.H., Boers W., Chamuleau R.A.F.M.;
RT "Apolipoprotein A-V. A novel apolipoprotein associated with an early phase
RT of liver regeneration.";
RL J. Biol. Chem. 276:44512-44520(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:11577099}.
CC -!- INDUCTION: Induced in early phase of liver regeneration. Expression is
CC maximally increased 6 hours after partial hepatectomy, both at the
CC liver RNA level and at the plasma protein level.
CC {ECO:0000269|PubMed:11577099}.
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; AF202887; AAF25659.1; -; mRNA.
DR EMBL; AF202888; AAF25660.1; -; mRNA.
DR EMBL; BC089780; AAH89780.1; -; mRNA.
DR RefSeq; NP_001264193.1; NM_001277264.1.
DR RefSeq; NP_542143.1; NM_080576.2.
DR AlphaFoldDB; Q9QUH3; -.
DR SMR; Q9QUH3; -.
DR IntAct; Q9QUH3; 1.
DR STRING; 10116.ENSRNOP00000024918; -.
DR iPTMnet; Q9QUH3; -.
DR PhosphoSitePlus; Q9QUH3; -.
DR PaxDb; Q9QUH3; -.
DR GeneID; 140638; -.
DR KEGG; rno:140638; -.
DR UCSC; RGD:70903; rat.
DR CTD; 116519; -.
DR RGD; 70903; Apoa5.
DR eggNOG; ENOG502S33P; Eukaryota.
DR HOGENOM; CLU_747959_0_0_1; -.
DR InParanoid; Q9QUH3; -.
DR PhylomeDB; Q9QUH3; -.
DR TreeFam; TF334458; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-8963901; Chylomicron remodeling.
DR PRO; PR:Q9QUH3; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q9QUH3; RN.
DR GO; GO:0042627; C:chylomicron; ISO:RGD.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0060229; F:lipase activator activity; ISO:RGD.
DR GO; GO:0035473; F:lipase binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; ISO:RGD.
DR GO; GO:0070325; F:lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:RGD.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0055090; P:acylglycerol homeostasis; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IBA:GO_Central.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IMP:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; IBA:GO_Central.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; IBA:GO_Central.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; ISO:RGD.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; ISO:RGD.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISO:RGD.
DR GO; GO:0010902; P:positive regulation of very-low-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0042246; P:tissue regeneration; ISO:RGD.
DR GO; GO:0019433; P:triglyceride catabolic process; ISO:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IBA:GO_Central.
DR InterPro; IPR000074; ApoA_E.
DR Pfam; PF01442; Apolipoprotein; 1.
PE 1: Evidence at protein level;
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_0000001983"
FT REGION 305..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 231..255
FT /evidence="ECO:0000255"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 367 AA; 41427 MW; D5B1A4F4CB016478 CRC64;
MAAVITWALA LLSVFATVQA RKSFWEYFGQ NSQGKGMMGQ QQKLAQESLK GSLEQDLYNM
NNFLEKLGPL REPGKEPPRL AQDPEGIRKQ LQQELEEVST RLEPYMAAKH QQVGWNLEGL
RQQLKPYTVE LMEQVGLSVQ DLQEQLRMVG KGTKAQLLGG VDEAMSLLQD MQSRVLHHTD
RVKELFHPYA ERLVTGIGHH VQELHRSVAP HAVASPARLS RCVQTLSHKL TRKAKDLHTS
IQRNLDQLRD ELSTFIRVST DGADNRDSLD PQALSDEVRQ RLQAFRHDTY LQIAAFTQAI
DQETEEIQHQ LAPPPPSHSA FAPELGHSDS NKALSRLQSR LDDLWEDIAY GLHDQGHSQN
NPEGHSG
