Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P33622

- APOC3_MOUSE

UniProt

P33622 - APOC3_MOUSE

Protein

Apolipoprotein C-III

Gene

Apoc3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Inhibits lipoprotein lipase and hepatic lipase and decreases the uptake of lymph chylomicrons by hepatic cells. This suggests that it delays the catabolism of triglyceride-rich particles.

    GO - Molecular functioni

    1. lipase inhibitor activity Source: Ensembl
    2. phospholipid binding Source: Ensembl

    GO - Biological processi

    1. cellular response to glucose stimulus Source: Ensembl
    2. cholesterol efflux Source: Ensembl
    3. cholesterol homeostasis Source: Ensembl
    4. cholesterol metabolic process Source: MGI
    5. chylomicron remnant clearance Source: Ensembl
    6. G-protein coupled receptor signaling pathway Source: Ensembl
    7. high-density lipoprotein particle remodeling Source: Ensembl
    8. inflammatory response Source: Ensembl
    9. lipoprotein metabolic process Source: InterPro
    10. lipoprotein transport Source: Ensembl
    11. negative regulation of cholesterol import Source: Ensembl
    12. negative regulation of fatty acid biosynthetic process Source: Ensembl
    13. negative regulation of high-density lipoprotein particle clearance Source: Ensembl
    14. negative regulation of lipoprotein lipase activity Source: Ensembl
    15. negative regulation of low-density lipoprotein particle clearance Source: Ensembl
    16. negative regulation of receptor-mediated endocytosis Source: Ensembl
    17. negative regulation of triglyceride catabolic process Source: Ensembl
    18. negative regulation of very-low-density lipoprotein particle clearance Source: Ensembl
    19. phospholipid efflux Source: Ensembl
    20. regulation of Cdc42 protein signal transduction Source: Ensembl
    21. response to drug Source: Ensembl
    22. response to nutrient Source: Ensembl
    23. response to peptide hormone Source: Ensembl
    24. triglyceride catabolic process Source: MGI
    25. triglyceride homeostasis Source: Ensembl
    26. triglyceride metabolic process Source: MGI
    27. triglyceride mobilization Source: MGI

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism, Lipid transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_198569. Retinoid metabolism and transport.
    REACT_213857. HDL-mediated lipid transport.
    REACT_216017. Chylomicron-mediated lipid transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apolipoprotein C-III
    Short name:
    Apo-CIII
    Short name:
    ApoC-III
    Alternative name(s):
    Apolipoprotein C3
    Gene namesi
    Name:Apoc3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:88055. Apoc3.

    Subcellular locationi

    GO - Cellular componenti

    1. chylomicron Source: UniProtKB-KW
    2. cytosol Source: Reactome
    3. extracellular region Source: Reactome
    4. intermediate-density lipoprotein particle Source: Ensembl
    5. spherical high-density lipoprotein particle Source: Ensembl
    6. very-low-density lipoprotein particle Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chylomicron, Secreted, VLDL

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 9979Apolipoprotein C-IIIPRO_0000002033Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631Methionine sulfoxide1 Publication
    Glycosylationi94 – 941O-linked (GalNAc...)By similarity

    Keywords - PTMi

    Glycoprotein, Oxidation

    Proteomic databases

    MaxQBiP33622.
    PaxDbiP33622.
    PRIDEiP33622.

    PTM databases

    PhosphoSiteiP33622.

    Expressioni

    Tissue specificityi

    Mainly VLDL and also in HDL. Synthesized predominantly in liver and to a lesser degree in intestine.

    Gene expression databases

    BgeeiP33622.
    CleanExiMM_APOC3.
    GenevestigatoriP33622.

    Interactioni

    Protein-protein interaction databases

    IntActiP33622. 1 interaction.
    MINTiMINT-1858244.

    Structurei

    3D structure databases

    ProteinModelPortaliP33622.
    SMRiP33622. Positions 22-99.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni68 – 9932Lipid-bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the apolipoprotein C3 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG39866.
    GeneTreeiENSGT00390000015395.
    HOGENOMiHOG000247042.
    HOVERGENiHBG050549.
    InParanoidiP33622.
    KOiK08759.
    PhylomeDBiP33622.
    TreeFamiTF338209.

    Family and domain databases

    InterProiIPR008403. Apo-CIII.
    [Graphical view]
    PANTHERiPTHR14225. PTHR14225. 1 hit.
    PfamiPF05778. Apo-CIII. 1 hit.
    [Graphical view]
    ProDomiPD010414. Apo-CIII. 1 hit.
    [Graphical view] [Entries sharing at least one domain]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P33622-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPRTLLTVA LLALLASARA EEVEGSLLLG SVQGYMEQAS KTVQDALSSV   50
    QESDIAVVAR GWMDNHFRFL KGYWSKFTDK FTGFWDSNPE DQPTPAIES 99
    Length:99
    Mass (Da):10,982
    Last modified:November 7, 2003 - v2
    Checksum:iBBC1690C055ADEC7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 571V → A in L04150. (PubMed:1478650)Curated
    Sequence conflicti69 – 691F → S in BAB22448. (PubMed:16141072)Curated
    Sequence conflicti69 – 691F → S in BAB25563. (PubMed:16141072)Curated

    Mass spectrometryi

    Molecular mass is 8830.5±0.354 Da from positions 21 - 99. Determined by ESI. Strain C57BL/6. Without methionine sulfoxide.1 Publication
    Molecular mass is 8891.4 Da from positions 21 - 99. Determined by ESI. Strain BALB/c. Without methionine sulfoxide.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04149 Genomic DNA. No translation available.
    L04150 mRNA. No translation available.
    AK002908 mRNA. Translation: BAB22448.1.
    AK008260 mRNA. Translation: BAB25563.1.
    BC021776 mRNA. Translation: AAH21776.1.
    CCDSiCCDS23141.1.
    PIRiB44364.
    RefSeqiNP_001276685.1. NM_001289756.1.
    NP_075603.1. NM_023114.4.
    UniGeneiMm.390161.

    Genome annotation databases

    EnsembliENSMUST00000034586; ENSMUSP00000034586; ENSMUSG00000032081.
    ENSMUST00000118649; ENSMUSP00000113058; ENSMUSG00000032081.
    GeneIDi11814.
    KEGGimmu:11814.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04149 Genomic DNA. No translation available.
    L04150 mRNA. No translation available.
    AK002908 mRNA. Translation: BAB22448.1 .
    AK008260 mRNA. Translation: BAB25563.1 .
    BC021776 mRNA. Translation: AAH21776.1 .
    CCDSi CCDS23141.1.
    PIRi B44364.
    RefSeqi NP_001276685.1. NM_001289756.1.
    NP_075603.1. NM_023114.4.
    UniGenei Mm.390161.

    3D structure databases

    ProteinModelPortali P33622.
    SMRi P33622. Positions 22-99.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P33622. 1 interaction.
    MINTi MINT-1858244.

    PTM databases

    PhosphoSitei P33622.

    Proteomic databases

    MaxQBi P33622.
    PaxDbi P33622.
    PRIDEi P33622.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034586 ; ENSMUSP00000034586 ; ENSMUSG00000032081 .
    ENSMUST00000118649 ; ENSMUSP00000113058 ; ENSMUSG00000032081 .
    GeneIDi 11814.
    KEGGi mmu:11814.

    Organism-specific databases

    CTDi 345.
    MGIi MGI:88055. Apoc3.

    Phylogenomic databases

    eggNOGi NOG39866.
    GeneTreei ENSGT00390000015395.
    HOGENOMi HOG000247042.
    HOVERGENi HBG050549.
    InParanoidi P33622.
    KOi K08759.
    PhylomeDBi P33622.
    TreeFami TF338209.

    Enzyme and pathway databases

    Reactomei REACT_198569. Retinoid metabolism and transport.
    REACT_213857. HDL-mediated lipid transport.
    REACT_216017. Chylomicron-mediated lipid transport.

    Miscellaneous databases

    ChiTaRSi APOC3. mouse.
    NextBioi 279695.
    PROi P33622.
    SOURCEi Search...

    Gene expression databases

    Bgeei P33622.
    CleanExi MM_APOC3.
    Genevestigatori P33622.

    Family and domain databases

    InterProi IPR008403. Apo-CIII.
    [Graphical view ]
    PANTHERi PTHR14225. PTHR14225. 1 hit.
    Pfami PF05778. Apo-CIII. 1 hit.
    [Graphical view ]
    ProDomi PD010414. Apo-CIII. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the mouse apolipoprotein Apoa-1/Apoc-3 gene locus: genomic, mRNA, and protein sequences with comparisons to other species."
      Januzzi J.L., Azrolan N., O'Connell A., Aalto-Setala K., Breslow J.L.
      Genomics 14:1081-1088(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Kidney and Small intestine.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    4. "Mass spectral analysis of the apolipoproteins on mouse high density lipoproteins. Detection of post-translational modifications."
      Puppione D.L., Yam L.M., Bassilian S., Souda P., Castellani L.W., Schumaker V.N., Whitelegge J.P.
      Biochim. Biophys. Acta 1764:1363-1371(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 42-68, MASS SPECTROMETRY, OXIDATION AT MET-63.

    Entry informationi

    Entry nameiAPOC3_MOUSE
    AccessioniPrimary (citable) accession number: P33622
    Secondary accession number(s): Q8VC58, Q9CPP9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: November 7, 2003
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3