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APOA2_BOVIN
ID   APOA2_BOVIN             Reviewed;         100 AA.
AC   P81644; Q2NKV9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Apolipoprotein A-II;
DE            Short=Apo-AII;
DE            Short=ApoA-II;
DE   AltName: Full=Antimicrobial peptide BAMP-1;
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     AltName: Full=Apolipoprotein A-II(1-76);
DE   Flags: Precursor;
GN   Name=APOA2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 24-99, MASS SPECTROMETRY, AND PYROGLUTAMATE FORMATION
RP   AT GLN-24.
RC   TISSUE=Fetal serum;
RX   PubMed=9538260; DOI=10.1093/oxfordjournals.jbchem.a021990;
RA   Motizuki M., Itoh T., Yamada M., Shimamura S., Tsurugi K.;
RT   "Purification, primary structure, and antimicrobial activities of bovine
RT   apolipoprotein A-II.";
RL   J. Biochem. 123:675-679(1998).
CC   -!- FUNCTION: May stabilize HDL (high density lipoprotein) structure by its
CC       association with lipids, and affect the HDL metabolism. Has
CC       antimicrobial activity.
CC   -!- SUBUNIT: Monomer. Interacts with NAXE and NDRG1 (By similarity).
CC       {ECO:0000250|UniProtKB:P02652}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- MASS SPECTROMETRY: [Truncated apolipoprotein A-II]: Mass=8545;
CC       Method=MALDI; Evidence={ECO:0000269|PubMed:9538260};
CC   -!- SIMILARITY: Belongs to the apolipoprotein A2 family. {ECO:0000305}.
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DR   EMBL; BC111607; AAI11608.1; -; mRNA.
DR   PIR; JC5734; JC5734.
DR   RefSeq; NP_001039381.1; NM_001045916.2.
DR   AlphaFoldDB; P81644; -.
DR   SMR; P81644; -.
DR   STRING; 9913.ENSBTAP00000012138; -.
DR   PaxDb; P81644; -.
DR   PeptideAtlas; P81644; -.
DR   PRIDE; P81644; -.
DR   Ensembl; ENSBTAT00000012138; ENSBTAP00000012138; ENSBTAG00000009212.
DR   GeneID; 505394; -.
DR   KEGG; bta:505394; -.
DR   CTD; 336; -.
DR   VEuPathDB; HostDB:ENSBTAG00000009212; -.
DR   VGNC; VGNC:26023; APOA2.
DR   eggNOG; ENOG502SVYZ; Eukaryota.
DR   GeneTree; ENSGT00390000003306; -.
DR   HOGENOM; CLU_157351_0_0_1; -.
DR   InParanoid; P81644; -.
DR   OMA; LTICSFE; -.
DR   OrthoDB; 1612564at2759; -.
DR   TreeFam; TF338165; -.
DR   Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000009212; Expressed in liver and 57 other tissues.
DR   GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR   GO; GO:0034366; C:spherical high-density lipoprotein particle; IBA:GO_Central.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IBA:GO_Central.
DR   GO; GO:0034190; F:apolipoprotein receptor binding; IBA:GO_Central.
DR   GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IBA:GO_Central.
DR   GO; GO:0055102; F:lipase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR   GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0017129; F:triglyceride binding; NAS:UniProtKB.
DR   GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR   GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR   GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR   GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0046340; P:diacylglycerol catabolic process; IEA:Ensembl.
DR   GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR   GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IBA:GO_Central.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR   GO; GO:0034374; P:low-density lipoprotein particle remodeling; IBA:GO_Central.
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; IBA:GO_Central.
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; ISS:UniProtKB.
DR   GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR   GO; GO:0018158; P:protein oxidation; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
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; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Direct protein sequencing; HDL; Lipid transport;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW   Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..100
FT                   /note="Proapolipoprotein A-II"
FT                   /id="PRO_0000425349"
FT   CHAIN           24..100
FT                   /note="Apolipoprotein A-II"
FT                   /id="PRO_0000181373"
FT   CHAIN           24..99
FT                   /note="Truncated apolipoprotein A-II"
FT                   /evidence="ECO:0000269|PubMed:9538260"
FT                   /id="PRO_0000244388"
FT   MOD_RES         24
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:9538260"
SQ   SEQUENCE   100 AA;  11202 MW;  399C4EB3F0D15FB3 CRC64;
     MKLLALTVLL LTICGLEGAL VRRQAEESNL QSLVSQYFQT VADYGKDLVE KAKGSELQTQ
     AKAYFEKTQE ELTPFFKKAG TDLLNFLSSF IDPKKQPATR
 
 
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