APOC2_RAT
ID APOC2_RAT Reviewed; 97 AA.
AC G3V8D4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:P02655}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02655}.
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 the
CC mature form apolipoprotein C-II, which occurs as the minor form in
CC plasma. {ECO:0000250|UniProtKB:P02655}.
CC -!- SIMILARITY: Belongs to the apolipoprotein C2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR07002678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473979; EDM08174.1; -; Genomic_DNA.
DR RefSeq; NP_001078821.1; NM_001085352.1.
DR AlphaFoldDB; G3V8D4; -.
DR SMR; G3V8D4; -.
DR IntAct; G3V8D4; 1.
DR STRING; 10116.ENSRNOP00000024800; -.
DR PaxDb; G3V8D4; -.
DR PRIDE; G3V8D4; -.
DR Ensembl; ENSRNOT00000024800; ENSRNOP00000024800; ENSRNOG00000018402.
DR GeneID; 292697; -.
DR KEGG; rno:292697; -.
DR CTD; 344; -.
DR RGD; 2135; Apoc2.
DR eggNOG; ENOG502SEJB; Eukaryota.
DR GeneTree; ENSGT00390000007913; -.
DR HOGENOM; CLU_180154_0_0_1; -.
DR InParanoid; G3V8D4; -.
DR OMA; EVQGAHL; -.
DR OrthoDB; 1548460at2759; -.
DR TreeFam; TF338218; -.
DR Reactome; R-RNO-8963888; Chylomicron assembly.
DR Reactome; R-RNO-8963901; Chylomicron remodeling.
DR Reactome; R-RNO-8964058; HDL remodeling.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:G3V8D4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000018402; Expressed in liver and 14 other tissues.
DR GO; GO:0042627; C:chylomicron; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; ISO:RGD.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0055102; F:lipase inhibitor activity; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; ISO:RGD.
DR GO; GO:0016004; F:phospholipase activator activity; ISO:RGD.
DR GO; GO:0043274; F:phospholipase binding; ISO:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR GO; GO:0034382; P:chylomicron remnant clearance; ISO:RGD.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042953; P:lipoprotein transport; IDA:RGD.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; ISO:RGD.
DR GO; GO:0045833; P:negative regulation of lipid metabolic process; ISO:RGD.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0033700; P:phospholipid efflux; ISO:RGD.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; ISO:RGD.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; ISO:RGD.
DR GO; GO:0060697; P:positive regulation of phospholipid catabolic process; ISO:RGD.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:RGD.
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 3: Inferred from homology;
KW Chylomicron; HDL; LDL; Lipid degradation; Lipid metabolism;
KW Lipid transport; Reference proteome; Secreted; Signal; Transport; VLDL.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..97
FT /note="Proapolipoprotein C-II"
FT /id="PRO_0000454005"
FT CHAIN 26..97
FT /note="Apolipoprotein C-II"
FT /evidence="ECO:0000250|UniProtKB:P02655"
FT /id="PRO_5015091722"
FT REGION 63..71
FT /note="Lipid binding"
FT /evidence="ECO:0000250|UniProtKB:P02655"
FT REGION 75..97
FT /note="Lipoprotein lipase cofactor"
FT /evidence="ECO:0000250|UniProtKB:P02655"
SQ SEQUENCE 97 AA; 10695 MW; D33BDBE66C5278B9 CRC64;
MGSRFFLALF LALLVLGNEV QGTEEDDPGS SALLDTVQEH LFSYWNSAKA AAGELYQKTY
LTSVDEKLRD MYSKSSAAMT TYAGIFTDQL LTLLKGE
