APOA2_NASLA
ID APOA2_NASLA Reviewed; 100 AA.
AC P0DP86;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 25-MAY-2022, entry version 10.
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 Nasalis larvatus (Proboscis monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Nasalis.
OX NCBI_TaxID=43780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Abdullah M.T., Mat Daud M.H.R., Nur Aida M.T., Idris A., Croft L.,
RA Saidin A., Alias H., Zaidan Z., Buang Z., Zainuddin R., Esa Y., Hercus R.;
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (JUN-2017).
CC -!- FUNCTION: May stabilize HDL (high density lipoprotein) structure by its
CC association with lipids, and affect the HDL metabolism.
CC {ECO:0000250|UniProtKB:P18656}.
CC -!- SUBUNIT: Monomer. Interacts with NAXE and NDRG1.
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; JMHX01319529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DP86; -.
DR SMR; P0DP86; -.
DR GO; GO:0034364; C:high-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 GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
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; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..100
FT /note="Proapolipoprotein A-II"
FT /evidence="ECO:0000250|UniProtKB:P18656"
FT /id="PRO_0000441388"
FT CHAIN 24..100
FT /note="Apolipoprotein A-II"
FT /evidence="ECO:0000250|UniProtKB:P02652"
FT /id="PRO_0000441389"
FT CHAIN 24..99
FT /note="Truncated apolipoprotein A-II"
FT /evidence="ECO:0000250|UniProtKB:P02652"
FT /id="PRO_0000441390"
FT MOD_RES 49
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02652"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02652"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02652"
SQ SEQUENCE 100 AA; 11214 MW; 52B734AAB3F87AB1 CRC64;
MKLLAATVLL LTICSLEGAL VRRQAEEPSV ESLVSQYFQT VTDYGKDLME KVKSPELQAQ
AKAYFEKSKE QLTPLVKKAG TDLVNFLSYF VELRTQPATQ