ID U3JSQ8_FICAL Unreviewed; 468 AA.
AC U3JSQ8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Apolipoprotein A-IV {ECO:0000256|ARBA:ARBA00041197};
DE AltName: Full=Apolipoprotein A4 {ECO:0000256|ARBA:ARBA00042591};
GN Name=APOA4 {ECO:0000313|Ensembl:ENSFALP00000005812.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000005812.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000005812.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000005812.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC {ECO:0000256|ARBA:ARBA00008788}.
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DR AlphaFoldDB; U3JSQ8; -.
DR STRING; 59894.ENSFALP00000005812; -.
DR Ensembl; ENSFALT00000005839.2; ENSFALP00000005812.2; ENSFALG00000005578.2.
DR eggNOG; ENOG502QSC5; Eukaryota.
DR GeneTree; ENSGT00950000182929; -.
DR HOGENOM; CLU_058447_0_0_1; -.
DR Proteomes; UP000016665; Chromosome 24.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0042627; C:chylomicron; IEA:Ensembl.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0016209; F:antioxidant activity; IEA:Ensembl.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR GO; GO:0031210; F:phosphatidylcholine binding; IEA:Ensembl.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl.
DR GO; GO:0002227; P:innate immune response in mucosa; IEA:Ensembl.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:Ensembl.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0034445; P:negative regulation of plasma lipoprotein oxidation; IEA:Ensembl.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IEA:Ensembl.
DR GO; GO:0065005; P:protein-lipid complex assembly; IEA:Ensembl.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:Ensembl.
DR GO; GO:0006982; P:response to lipid hydroperoxide; IEA:Ensembl.
DR GO; GO:0035634; P:response to stilbenoid; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR Gene3D; 1.20.5.20; -; 3.
DR Gene3D; 1.20.120.20; Apolipoprotein; 2.
DR InterPro; IPR000074; ApoA_E.
DR PANTHER; PTHR18976; APOLIPOPROTEIN; 1.
DR PANTHER; PTHR18976:SF1; APOLIPOPROTEIN A-IV; 1.
DR Pfam; PF01442; Apolipoprotein; 1.
DR SUPFAM; SSF58113; Apolipoprotein A-I; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT REGION 48..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..220
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 468 AA; 51782 MW; A37CB785E533AE6F CRC64;
MSGLRARQAL PRRDCAKVQA LAVSQPAWKL QEGSGCINSA GSCRLRRYRS SDSTGEQLQG
LEGARREPGS PSPLARGWGA AGPWGFLHLC SVLPQELPAL RMAPKAAALV LVLLAISGSR
ADVNPDDVAN VIWKYFTELG SNAKDTVGQL QQTEISKQLN TLLKSNLQTV SAYAEDLQER
LVPFATELQA RLAQDSQRMK EQIQRELREL QAKLAPYADE VHQQIGTNIR ELQAKLSPYA
EELRSQVDRS AGELQRALEP YAAELRERLQ DNTDSIKASL SPYADRLQQQ IDGGVESLKE
RLSPMADELK AQVEQSVAEL RRGLSPYAQE VQDGLNRQLE SLTLQMERAA EELRGRLATS
SEELRAQLSP LARELREAAS GDAESLRQRL APLAQQLEQR VGQTLESFRQ QAAPFGETFG
KQLVQRLEEM RGKLETGAAG VEDHLELLEK EVREKVAAFL STVPPPQN
//
