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)

O08601

- MTP_MOUSE

UniProt

O08601 - MTP_MOUSE

Protein

Microsomal triglyceride transfer protein large subunit

Gene

Mttp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (19 Jan 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces. Required for the secretion of plasma lipoproteins that contain apolipoprotein B. May be involved in regulating cholesteryl ester biosynthesis in cells that produce lipoproteins. Loads phospholipid into the C1D1 antigen-binding groove. Isoform 2 is critical for the development of natural killer T (NKT) cells. May have a role in the biogenesis of lipid droplets.3 Publications

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW
    2. lipid transporter activity Source: MGI
    3. protein binding Source: MGI

    GO - Biological processi

    1. cholesterol homeostasis Source: MGI
    2. cholesterol metabolic process Source: UniProtKB-KW
    3. lipid metabolic process Source: MGI
    4. lipoprotein metabolic process Source: MGI
    5. lipoprotein transport Source: MGI
    6. protein lipidation Source: MGI
    7. response to calcium ion Source: Ensembl
    8. triglyceride metabolic process Source: MGI

    Keywords - Biological processi

    Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism, Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_216017. Chylomicron-mediated lipid transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microsomal triglyceride transfer protein large subunit
    Gene namesi
    Name:Mttp
    Synonyms:Mtp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:106926. Mttp.

    Subcellular locationi

    Isoform 1 : Endoplasmic reticulum
    Note: Localized to the endoplasmic reticulum according to PubMed:17312007.
    Isoform 2 : Endoplasmic reticulum. Golgi apparatus
    Note: Localized to the endoplasmic reticulum according to PubMed:17312007. Localized to the Golgi apparatus according to PubMed:17635917.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. brush border membrane Source: Ensembl
    3. endoplasmic reticulum Source: MGI
    4. Golgi apparatus Source: MGI
    5. membrane-bounded vesicle Source: Ensembl
    6. microvillus membrane Source: Ensembl
    7. receptor complex Source: MGI
    8. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus

    Pathology & Biotechi

    Disruption phenotypei

    Lowers plasma and tissue triglyceride levels, and increases cellular free cholesterol.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 894873Microsomal triglyceride transfer protein large subunitPRO_0000041595Add
    BLAST

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO08601.
    PaxDbiO08601.
    PRIDEiO08601.

    PTM databases

    PhosphoSiteiO08601.

    Expressioni

    Tissue specificityi

    Expressed in heart. Isoform 1 is mainly expressed in the intestine and the liver, and at lower levels in white and brown fat cells. Isoform 2 is ubiquitous, and is the major isoform in hematopoietic cells and adipocytes.3 Publications

    Developmental stagei

    Expression in the yolk sac tissues followed by expression in the primordial liver cell nests as early as day 9 post-coitum (E9.5). Intestinal expression is detected around E12.5 and attains full adult expression patterns by E14.5.1 Publication

    Inductioni

    Up-regulated by FOXO1.1 Publication

    Gene expression databases

    ArrayExpressiO08601.
    BgeeiO08601.
    CleanExiMM_MTTP.
    GenevestigatoriO08601.

    Interactioni

    Subunit structurei

    Heterodimer composed of MTTP and of protein disulfide isomerase (P4HB/PDI).

    Protein-protein interaction databases

    BioGridi201601. 1 interaction.
    IntActiO08601. 6 interactions.
    MINTiMINT-1864006.
    STRINGi10090.ENSMUSP00000029805.

    Structurei

    3D structure databases

    ProteinModelPortaliO08601.
    SMRiO08601. Positions 470-508.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 658631VitellogeninPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 vitellogenin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG272516.
    GeneTreeiENSGT00390000011412.
    HOGENOMiHOG000113688.
    HOVERGENiHBG006416.
    InParanoidiQ91X33.
    KOiK14463.
    OMAiRPVTFFN.
    OrthoDBiEOG747PH9.
    PhylomeDBiO08601.
    TreeFamiTF328754.

    Family and domain databases

    Gene3Di1.25.10.20. 1 hit.
    2.30.230.10. 1 hit.
    InterProiIPR015819. Lipid_transp_b-sht_shell.
    IPR001747. Lipid_transpt_N.
    IPR015816. Vitellinogen_b-sht_N.
    IPR011030. Vitellinogen_superhlx.
    [Graphical view]
    PfamiPF01347. Vitellogenin_N. 1 hit.
    [Graphical view]
    SMARTiSM00638. LPD_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48431. SSF48431. 1 hit.
    SSF56968. SSF56968. 1 hit.
    PROSITEiPS51211. VITELLOGENIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform 1 (identifier: O08601-1) [UniParc]FASTAAdd to Basket

    Also known as: MTP-A

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MILLAVLFLC FFSSYSASVK GHTTGLSLNN ERLYKLTYST EVFLDGGKGK    50
    PQDSVGYKIS SDVDVVLLWR NPDGDDDQVI QVTITAVNVE NAGQQRGEKS 100
    IFQGKSTPKI IGKDNLEALQ RPMLLHLVRG KVKEFYSYEN EPVGIENLKR 150
    GLASLFQMQL SSGTTNEVDI SGDCKVTYQA QQDKVVKIKA LDTCKIERSG 200
    FTTANQVLGV SSKATSVTTY KIEDSFVTAV LAEETRAFAL NFQQTIAGKI 250
    VSKQKLELKT TEAGPRMIPG KQVAGVIKAV DSKYKAIPIV GQVLERVCKG 300
    CPSLAEHWKS IRKNLEPENL SKAEAVQSFL AFIQHLRTSR REEILQILKA 350
    EKKEVLPQLV DAVTSAQTPD SLEAILDFLD FKSDSSIILQ ERFLYACGFA 400
    THPDEELLRA LLSKFKGSFA SNDIRESVMI IIGALVRKLC QNEGCKLKAV 450
    VEAKKLILGG LEKPEKKEDT TMYLLALKNA LLPEGIPLLL KYAEAGEGPV 500
    SHLATTVLQR YDVSFITDEV KKTLNRIYHQ NRKVHEKTVR TTAAAVILKN 550
    PSYMDVKNIL LSIGELPKEM NKYMLTVVQD ILHFEMPASK MIRRVLKEMA 600
    VHNYDRFSKS GSSSAYTGYV ERSPRAASTY SLDILYSGSG ILRRSNLNIF 650
    QYIGKAELHG SQVVIEAQGL EGLIAATPDE GEENLDSYAG MSAILFDVQL 700
    RPVTFFNGYS DLMSKMLSAS GDPVSVVKGL ILLIDHSQDI QLQSGLKANM 750
    EIQGGLAIDI SGSMEFSLWY RESKTRVKNR VAVVITSDVT VDASFVKAGV 800
    ESRAETEAGL EFISTVQFSQ YPFLVCMQMD KAEAPLRQFE TKYERLSTGR 850
    GYVSRRRKES LVAGCELPLH QENSEMCNVV FPPQPESDNS GGWF 894
    Length:894
    Mass (Da):99,099
    Last modified:January 19, 2010 - v2
    Checksum:i3D8E5EB470CAA6FC
    GO
    Isoform 2 (identifier: O08601-2) [UniParc]FASTAAdd to Basket

    Also known as: MTPv1, MTP-B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: MILLAVLFLCFFSSYSASVK → MTVVMGKCQVSDGRQLLLFYAVLLLFPTLCAMQNS

    Note: Cleaved by signal peptidase between residues Gln-33 and Asn-34 (PubMed:17312007 and PubMed:17635917).

    Show »
    Length:909
    Mass (Da):100,751
    Checksum:i522AD2682867FA4A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti654 – 6563GKA → KGT in AAB51431. (PubMed:8660984)Curated
    Sequence conflicti654 – 6563GKA → KGT in ACB41497. (PubMed:17312007)Curated
    Sequence conflicti800 – 8001V → L in AAB51431. (PubMed:8660984)Curated
    Sequence conflicti800 – 8001V → L in ACB41497. (PubMed:17312007)Curated
    Sequence conflicti800 – 8001V → L in AAH12686. 1 PublicationCurated
    Sequence conflicti800 – 8001V → L in EDL12110. (PubMed:15489334)Curated
    Sequence conflicti872 – 8721E → Q in AAB51431. (PubMed:8660984)Curated
    Sequence conflicti872 – 8721E → Q in ACB41497. (PubMed:17312007)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2020MILLA…SASVK → MTVVMGKCQVSDGRQLLLFY AVLLLFPTLCAMQNS in isoform 2. 1 PublicationVSP_038546Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L47970 mRNA. Translation: AAB51431.1.
    EU553486 mRNA. Translation: ACB41497.1.
    AK146553 mRNA. Translation: BAE27255.1.
    CH466532 Genomic DNA. Translation: EDL12110.1.
    BC012686 mRNA. Translation: AAH12686.1.
    CCDSiCCDS38650.1. [O08601-1]
    CCDS51080.1. [O08601-2]
    RefSeqiNP_001156929.1. NM_001163457.1. [O08601-2]
    NP_032668.2. NM_008642.2. [O08601-1]
    XP_006501165.1. XM_006501102.1. [O08601-2]
    XP_006501166.1. XM_006501103.1. [O08601-1]
    UniGeneiMm.2941.

    Genome annotation databases

    EnsembliENSMUST00000029805; ENSMUSP00000029805; ENSMUSG00000028158. [O08601-1]
    ENSMUST00000098580; ENSMUSP00000096179; ENSMUSG00000028158. [O08601-2]
    GeneIDi17777.
    KEGGimmu:17777.
    UCSCiuc008rmw.2. mouse. [O08601-1]
    uc008rmx.2. mouse. [O08601-2]

    Keywords - Coding sequence diversityi

    Alternative promoter usage

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L47970 mRNA. Translation: AAB51431.1 .
    EU553486 mRNA. Translation: ACB41497.1 .
    AK146553 mRNA. Translation: BAE27255.1 .
    CH466532 Genomic DNA. Translation: EDL12110.1 .
    BC012686 mRNA. Translation: AAH12686.1 .
    CCDSi CCDS38650.1. [O08601-1 ]
    CCDS51080.1. [O08601-2 ]
    RefSeqi NP_001156929.1. NM_001163457.1. [O08601-2 ]
    NP_032668.2. NM_008642.2. [O08601-1 ]
    XP_006501165.1. XM_006501102.1. [O08601-2 ]
    XP_006501166.1. XM_006501103.1. [O08601-1 ]
    UniGenei Mm.2941.

    3D structure databases

    ProteinModelPortali O08601.
    SMRi O08601. Positions 470-508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201601. 1 interaction.
    IntActi O08601. 6 interactions.
    MINTi MINT-1864006.
    STRINGi 10090.ENSMUSP00000029805.

    PTM databases

    PhosphoSitei O08601.

    Proteomic databases

    MaxQBi O08601.
    PaxDbi O08601.
    PRIDEi O08601.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029805 ; ENSMUSP00000029805 ; ENSMUSG00000028158 . [O08601-1 ]
    ENSMUST00000098580 ; ENSMUSP00000096179 ; ENSMUSG00000028158 . [O08601-2 ]
    GeneIDi 17777.
    KEGGi mmu:17777.
    UCSCi uc008rmw.2. mouse. [O08601-1 ]
    uc008rmx.2. mouse. [O08601-2 ]

    Organism-specific databases

    CTDi 4547.
    MGIi MGI:106926. Mttp.

    Phylogenomic databases

    eggNOGi NOG272516.
    GeneTreei ENSGT00390000011412.
    HOGENOMi HOG000113688.
    HOVERGENi HBG006416.
    InParanoidi Q91X33.
    KOi K14463.
    OMAi RPVTFFN.
    OrthoDBi EOG747PH9.
    PhylomeDBi O08601.
    TreeFami TF328754.

    Enzyme and pathway databases

    Reactomei REACT_216017. Chylomicron-mediated lipid transport.

    Miscellaneous databases

    ChiTaRSi MTTP. mouse.
    NextBioi 292509.
    PROi O08601.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08601.
    Bgeei O08601.
    CleanExi MM_MTTP.
    Genevestigatori O08601.

    Family and domain databases

    Gene3Di 1.25.10.20. 1 hit.
    2.30.230.10. 1 hit.
    InterProi IPR015819. Lipid_transp_b-sht_shell.
    IPR001747. Lipid_transpt_N.
    IPR015816. Vitellinogen_b-sht_N.
    IPR011030. Vitellinogen_superhlx.
    [Graphical view ]
    Pfami PF01347. Vitellogenin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00638. LPD_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48431. SSF48431. 1 hit.
    SSF56968. SSF56968. 1 hit.
    PROSITEi PS51211. VITELLOGENIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse microsomal triglyceride transfer protein large subunit: cDNA cloning, tissue-specific expression and chromosomal localization."
      Nakamuta M., Chang B.H., Hoogeveen R., Li W.H., Chan L.
      Genomics 33:313-316(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver and Small intestine.
    2. "MTP regulated by an alternate promoter is essential for NKT cell development."
      Dougan S.K., Rava P., Hussain M.M., Blumberg R.S.
      J. Exp. Med. 204:533-545(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE, FUNCTION, SUBCELLULAR LOCATION, PROCESSING, TISSUE SPECIFICITY.
      Strain: C57BL/6J.
      Tissue: Thymus.
    3. "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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Amnion.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Liver.
    6. "Apo B100-containing lipoproteins are secreted by the heart."
      Boren J., Veniant M.M., Young S.G.
      J. Clin. Invest. 101:1197-1202(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "A deficiency of microsomal triglyceride transfer protein reduces apolipoprotein B secretion."
      Leung G.K., Veniant M.M., Kim S.K., Zlot C.H., Raabe M., Bjorkegren J., Neese R.A., Hellerstein M.K., Young S.G.
      J. Biol. Chem. 275:7515-7520(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    8. "Microsomal triglyceride transfer protein expression during mouse development."
      Shelton J.M., Lee M.H., Richardson J.A., Patel S.B.
      J. Lipid Res. 41:532-537(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    9. "Identification of a novel isoform of microsomal triglyceride transfer protein."
      Mohler P.J., Zhu M.Y., Blade A.M., Ham A.J., Shelness G.S., Swift L.L.
      J. Biol. Chem. 282:26981-26988(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. "Microsomal triglyceride transfer protein enhances cellular cholesteryl esterification by relieving product inhibition."
      Iqbal J., Rudel L.L., Hussain M.M.
      J. Biol. Chem. 283:19967-19980(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    11. "FoxO1 mediates insulin-dependent regulation of hepatic VLDL production in mice."
      Kamagate A., Qu S., Perdomo G., Su D., Kim D.H., Slusher S., Meseck M., Dong H.H.
      J. Clin. Invest. 118:2347-2364(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY FOXO1.

    Entry informationi

    Entry nameiMTP_MOUSE
    AccessioniPrimary (citable) accession number: O08601
    Secondary accession number(s): B2CXA7, Q3UJA0, Q91X33
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 19, 2010
    Last modified: October 1, 2014
    This is version 108 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, 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