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Protein

Microsomal triglyceride transfer protein large subunit

Gene

Mttp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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

  • lipid binding Source: UniProtKB-KW
  • lipid transporter activity Source: MGI

GO - Biological processi

  • cholesterol homeostasis Source: MGI
  • cholesterol metabolic process Source: UniProtKB-KW
  • circadian rhythm Source: UniProtKB
  • lipid metabolic process Source: MGI
  • lipoprotein metabolic process Source: MGI
  • lipoprotein transport Source: MGI
  • protein lipidation Source: MGI
  • response to calcium ion Source: Ensembl
  • triglyceride metabolic process Source: MGI
Complete GO annotation...

Keywords - Biological processi

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

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_314625. 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 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:106926. Mttp.

Subcellular locationi

Isoform 1 :
Isoform 2 :

GO - Cellular componenti

Complete GO annotation...

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. Expressed in a circadian manner in the liver.2 Publications

Gene expression databases

BgeeiO08601.
CleanExiMM_MTTP.
ExpressionAtlasiO08601. baseline and differential.
GenevisibleiO08601. MM.

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.ENSMUSP00000096179.

Structurei

3D structure databases

ProteinModelPortaliO08601.
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.
InParanoidiO08601.
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. AlignAdd to basket

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

        10         20         30         40         50
MILLAVLFLC FFSSYSASVK GHTTGLSLNN ERLYKLTYST EVFLDGGKGK
60 70 80 90 100
PQDSVGYKIS SDVDVVLLWR NPDGDDDQVI QVTITAVNVE NAGQQRGEKS
110 120 130 140 150
IFQGKSTPKI IGKDNLEALQ RPMLLHLVRG KVKEFYSYEN EPVGIENLKR
160 170 180 190 200
GLASLFQMQL SSGTTNEVDI SGDCKVTYQA QQDKVVKIKA LDTCKIERSG
210 220 230 240 250
FTTANQVLGV SSKATSVTTY KIEDSFVTAV LAEETRAFAL NFQQTIAGKI
260 270 280 290 300
VSKQKLELKT TEAGPRMIPG KQVAGVIKAV DSKYKAIPIV GQVLERVCKG
310 320 330 340 350
CPSLAEHWKS IRKNLEPENL SKAEAVQSFL AFIQHLRTSR REEILQILKA
360 370 380 390 400
EKKEVLPQLV DAVTSAQTPD SLEAILDFLD FKSDSSIILQ ERFLYACGFA
410 420 430 440 450
THPDEELLRA LLSKFKGSFA SNDIRESVMI IIGALVRKLC QNEGCKLKAV
460 470 480 490 500
VEAKKLILGG LEKPEKKEDT TMYLLALKNA LLPEGIPLLL KYAEAGEGPV
510 520 530 540 550
SHLATTVLQR YDVSFITDEV KKTLNRIYHQ NRKVHEKTVR TTAAAVILKN
560 570 580 590 600
PSYMDVKNIL LSIGELPKEM NKYMLTVVQD ILHFEMPASK MIRRVLKEMA
610 620 630 640 650
VHNYDRFSKS GSSSAYTGYV ERSPRAASTY SLDILYSGSG ILRRSNLNIF
660 670 680 690 700
QYIGKAELHG SQVVIEAQGL EGLIAATPDE GEENLDSYAG MSAILFDVQL
710 720 730 740 750
RPVTFFNGYS DLMSKMLSAS GDPVSVVKGL ILLIDHSQDI QLQSGLKANM
760 770 780 790 800
EIQGGLAIDI SGSMEFSLWY RESKTRVKNR VAVVITSDVT VDASFVKAGV
810 820 830 840 850
ESRAETEAGL EFISTVQFSQ YPFLVCMQMD KAEAPLRQFE TKYERLSTGR
860 870 880 890
GYVSRRRKES LVAGCELPLH QENSEMCNVV FPPQPESDNS GGWF
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 (Ref. 4) Curated
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:
EMBLi
GenBanki
DDBJi
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_006501102.2. [O08601-2]
XP_006501166.1. XM_006501103.2. [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:
EMBLi
GenBanki
DDBJi
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_006501102.2. [O08601-2]
XP_006501166.1. XM_006501103.2. [O08601-1]
UniGeneiMm.2941.

3D structure databases

ProteinModelPortaliO08601.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201601. 1 interaction.
IntActiO08601. 6 interactions.
MINTiMINT-1864006.
STRINGi10090.ENSMUSP00000096179.

PTM databases

PhosphoSiteiO08601.

Proteomic databases

MaxQBiO08601.
PaxDbiO08601.
PRIDEiO08601.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi4547.
MGIiMGI:106926. Mttp.

Phylogenomic databases

eggNOGiNOG272516.
GeneTreeiENSGT00390000011412.
HOGENOMiHOG000113688.
HOVERGENiHBG006416.
InParanoidiO08601.
KOiK14463.
OMAiRPVTFFN.
OrthoDBiEOG747PH9.
PhylomeDBiO08601.
TreeFamiTF328754.

Enzyme and pathway databases

ReactomeiREACT_314625. Chylomicron-mediated lipid transport.

Miscellaneous databases

ChiTaRSiMttp. mouse.
NextBioi292509.
PROiO08601.
SOURCEiSearch...

Gene expression databases

BgeeiO08601.
CleanExiMM_MTTP.
ExpressionAtlasiO08601. baseline and differential.
GenevisibleiO08601. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  12. "LGR4 acts as a link between the peripheral circadian clock and lipid metabolism in liver."
    Wang F., Zhang X., Wang J., Chen M., Fan N., Ma Q., Liu R., Wang R., Li X., Liu M., Ning G.
    J. Mol. Endocrinol. 52:133-143(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

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: June 24, 2015
This is version 114 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.