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Database: UniProt
Entry: A0A2K6R6B7_RHIRO
LinkDB: A0A2K6R6B7_RHIRO
Original site: A0A2K6R6B7_RHIRO 
ID   A0A2K6R6B7_RHIRO        Unreviewed;       408 AA.
AC   A0A2K6R6B7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 35.
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:ENSRROP00000036567.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000036567.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000036567.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: May have a role in chylomicrons and VLDL secretion and
CC       catabolism. Required for efficient activation of lipoprotein lipase by
CC       ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL
CC       and chylomicrons. {ECO:0000256|ARBA:ARBA00037735}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC       {ECO:0000256|ARBA:ARBA00008788}.
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DR   RefSeq; XP_010370007.1; XM_010371705.1.
DR   AlphaFoldDB; A0A2K6R6B7; -.
DR   STRING; 61622.ENSRROP00000036567; -.
DR   Ensembl; ENSRROT00000061030.1; ENSRROP00000036567.1; ENSRROG00000041743.1.
DR   GeneTree; ENSGT00950000182929; -.
DR   OMA; VIWKYFT; -.
DR   Proteomes; UP000233200; Unplaced.
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:UniProtKB-KW.
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; 1.20.120.20; Apolipoprotein; 2.
DR   InterPro; IPR000074; ApoA_E.
DR   PANTHER; PTHR18976; APOLIPOPROTEIN; 1.
DR   PANTHER; PTHR18976:SF1; APOLIPOPROTEIN A-IV; 1.
DR   Pfam; PF01442; Apolipoprotein; 2.
DR   SUPFAM; SSF58113; Apolipoprotein A-I; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; HDL {ECO:0000256|ARBA:ARBA00022850};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..408
FT                   /note="Apolipoprotein A-IV"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014467886"
FT   REGION          360..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          235..266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        373..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   408 AA;  47168 MW;  C3611B628D230765 CRC64;
     MFLKAVVLTL ALVAVTGARA EVSADQVATV MWDYFSQLSN NAKEAVEHLQ KSELTQQLNA
     LFQDKLGEVN TYADDLQKKL VPFATELHER LAKDSEKLKE EIRKELEEVR ARLLPHANEV
     SQKIGENVRE LQQRLEPYTD QLRTQVNTQT EQLRRQLTPY AQRMERVLRE NAHSLQASLR
     PHADQLKAKI DQNVEELKER LTPYADEFKV KIDQTVEELR RSLAPYAQDA QEKLNHQLEG
     LAFQMKKNAE ELRARISASA EELRQRLAPL AEDMRGNLRG NTEGLQKSLA ELGGHLDQHV
     EEFRLRVEPY GENFNKALVQ QLEQLRQKLG PHAGDVEGHL SFLEKDLRDK VNSFFSTFKE
     KESQDKTLSL PKPKQQEEQV QEQQQEQQQE QQQEQQQEQV QMLAPLES
//
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