APOA2_HETGA
ID APOA2_HETGA Reviewed; 101 AA.
AC G5BWH8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Apolipoprotein A-II;
DE Short=Apo-AII;
DE Short=ApoA-II;
DE AltName: Full=Apolipoprotein A2;
DE Contains:
DE RecName: Full=Proapolipoprotein A-II;
DE Short=ProapoA-II;
DE Contains:
DE RecName: Full=Truncated apolipoprotein A-II;
DE Flags: Precursor;
GN Name=Apoa2;
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- FUNCTION: May stabilize HDL (high density lipoprotein) structure by its
CC association with lipids, and affect the HDL metabolism.
CC -!- SUBUNIT: Monomer. Interacts with NAXE and NDRG1 (By similarity).
CC {ECO:0000250|UniProtKB:P02652}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}.
CC -!- SIMILARITY: Belongs to the apolipoprotein A2 family. {ECO:0000305}.
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DR EMBL; GEBF01000010; JAO03623.1; -; Transcribed_RNA.
DR EMBL; JH172217; EHB13639.1; -; Genomic_DNA.
DR RefSeq; XP_004858718.1; XM_004858661.1.
DR AlphaFoldDB; G5BWH8; -.
DR SMR; G5BWH8; -.
DR STRING; 10181.XP_004858718.1; -.
DR Ensembl; ENSHGLT00000026848; ENSHGLP00000026611; ENSHGLG00000018928.
DR GeneID; 101701317; -.
DR KEGG; hgl:101701317; -.
DR CTD; 336; -.
DR eggNOG; ENOG502SVYZ; Eukaryota.
DR InParanoid; G5BWH8; -.
DR OMA; LTICSFE; -.
DR OrthoDB; 1612564at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR Bgee; ENSHGLG00000018928; Expressed in liver and 3 other tissues.
DR GO; GO:0042627; C:chylomicron; IEA:Ensembl.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034190; F:apolipoprotein receptor binding; IEA:Ensembl.
DR GO; GO:0015485; F:cholesterol binding; IEA:Ensembl.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:0055102; F:lipase inhibitor activity; 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:0046982; F:protein heterodimerization 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:0046340; P:diacylglycerol catabolic process; IEA:Ensembl.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IEA:Ensembl.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:Ensembl.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0060621; P:negative regulation of cholesterol import; IEA:Ensembl.
DR GO; GO:0060695; P:negative regulation of cholesterol transporter activity; IEA:Ensembl.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IEA:Ensembl.
DR GO; GO:0060192; P:negative regulation of lipase activity; IEA:Ensembl.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0018206; P:peptidyl-methionine modification; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:0018158; P:protein oxidation; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
DR GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; IEA:Ensembl.
DR InterPro; IPR006801; ApoA-II.
DR InterPro; IPR036172; ApoA-II_sf.
DR PANTHER; PTHR11027; PTHR11027; 1.
DR Pfam; PF04711; ApoA-II; 1.
DR SUPFAM; SSF82936; SSF82936; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues; HDL; Lipid transport; Oxidation;
KW Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..101
FT /note="Proapolipoprotein A-II"
FT /id="PRO_5007661161"
FT CHAIN 24..101
FT /note="Apolipoprotein A-II"
FT /id="PRO_0000450127"
FT CHAIN 24..100
FT /note="Truncated apolipoprotein A-II"
FT /evidence="ECO:0000250|UniProtKB:P02652"
FT /id="PRO_0000450128"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P02652"
SQ SEQUENCE 101 AA; 11381 MW; 633F10E7A926C1C9 CRC64;
MKLLAMTVLL VTICSLDGAL VRRQAEEPDL QGLFSQYFQT VTSYGKDLLQ KTKPQDLQAQ
VQSYFEKTQE QLVPLVKKAG TELFNMLSNM IELKKTQPAT A