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APOC2_CAVPO
ID   APOC2_CAVPO             Reviewed;         100 AA.
AC   P27916;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Apolipoprotein C-II;
DE            Short=Apo-CII;
DE            Short=ApoC-II;
DE   AltName: Full=Apolipoprotein C2;
DE   Contains:
DE     RecName: Full=Proapolipoprotein C-II;
DE              Short=ProapoC-II;
DE   Flags: Precursor;
GN   Name=APOC2;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=1999402; DOI=10.1016/s0021-9258(20)64287-9;
RA   Andersson Y., Thelander L., Bengtsson-Olivecrona G.;
RT   "Demonstration of apolipoprotein CII in guinea pigs. Functional
RT   characteristics, cDNA sequence, and tissue expression.";
RL   J. Biol. Chem. 266:4074-4080(1991).
CC   -!- FUNCTION: Component of chylomicrons, very low-density lipoproteins
CC       (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins
CC       (HDL) in plasma. Plays an important role in lipoprotein metabolism as
CC       an activator of lipoprotein lipase. Both proapolipoprotein C-II and
CC       apolipoprotein C-II can activate lipoprotein lipase.
CC       {ECO:0000250|UniProtKB:P02655}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02655}.
CC   -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:1999402}.
CC   -!- PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing
CC       glycoprotein which is subsequently desialylated prior to its
CC       proteolytic processing. {ECO:0000250|UniProtKB:P02655}.
CC   -!- PTM: Proapolipoprotein C-II, the major form found in plasma undergoes
CC       proteolytic cleavage of its N-terminal hexapeptide to generate
CC       apolipoprotein C-II, which occurs as the minor form in plasma.
CC       {ECO:0000250|UniProtKB:P02655}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C2 family. {ECO:0000305}.
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DR   EMBL; M59913; AAA37031.1; -; mRNA.
DR   PIR; A38685; A38685.
DR   RefSeq; NP_001166385.1; NM_001172914.2.
DR   RefSeq; XP_013002235.1; XM_013146781.1.
DR   AlphaFoldDB; P27916; -.
DR   SMR; P27916; -.
DR   STRING; 10141.ENSCPOP00000019331; -.
DR   PRIDE; P27916; -.
DR   Ensembl; ENSCPOT00000022988; ENSCPOP00000019331; ENSCPOG00000009302.
DR   GeneID; 100135480; -.
DR   KEGG; cpoc:100135480; -.
DR   CTD; 344; -.
DR   eggNOG; ENOG502SEJB; Eukaryota.
DR   GeneTree; ENSGT00390000007913; -.
DR   HOGENOM; CLU_180154_0_0_1; -.
DR   InParanoid; P27916; -.
DR   OMA; EVQGAHL; -.
DR   OrthoDB; 1548460at2759; -.
DR   TreeFam; TF338218; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000009302; Expressed in liver and 5 other tissues.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0055102; F:lipase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0008289; F:lipid binding; IEA:Ensembl.
DR   GO; GO:0060230; F:lipoprotein lipase activator activity; IEA:Ensembl.
DR   GO; GO:0016004; F:phospholipase activator activity; IEA:Ensembl.
DR   GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR   GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR   GO; GO:0034382; P:chylomicron remnant clearance; IEA:Ensembl.
DR   GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0032375; P:negative regulation of cholesterol transport; IEA:Ensembl.
DR   GO; GO:0045833; P:negative regulation of lipid metabolic process; IEA:Ensembl.
DR   GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; 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:0051006; P:positive regulation of lipoprotein lipase activity; IEA:Ensembl.
DR   GO; GO:0010518; P:positive regulation of phospholipase activity; IEA:Ensembl.
DR   GO; GO:0060697; P:positive regulation of phospholipid catabolic process; IEA:Ensembl.
DR   GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IEA:Ensembl.
DR   GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR   Gene3D; 1.10.1440.10; -; 1.
DR   InterPro; IPR008019; Apo-CII.
DR   InterPro; IPR023121; ApoC-II_dom_sf.
DR   PANTHER; PTHR16566; PTHR16566; 1.
DR   Pfam; PF05355; Apo-CII; 1.
PE   2: Evidence at transcript level;
KW   Chylomicron; Glycoprotein; HDL; LDL; Lipid degradation; Lipid metabolism;
KW   Lipid transport; Reference proteome; Secreted; Sialic acid; Signal;
KW   Transport; VLDL.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..100
FT                   /note="Proapolipoprotein C-II"
FT                   /id="PRO_0000002023"
FT   CHAIN           32..100
FT                   /note="Apolipoprotein C-II"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
FT                   /id="PRO_0000430837"
FT   REGION          65..73
FT                   /note="Lipid binding"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
FT   REGION          77..100
FT                   /note="Lipoprotein lipase cofactor"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
SQ   SEQUENCE   100 AA;  10985 MW;  BBCF8DB52FC9E9BD CRC64;
     MDARSLLLLW LLLPLLLLLG CEVQGAHLTQ QDEPTSPDLL ETLSTYWDSA KAAAQGLYNN
     TYLPAVDETI RDIYSKGSAA ISTYTGILTD QILTMLQGKQ
 
 
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