MTP_MOUSE
ID MTP_MOUSE Reviewed; 894 AA.
AC O08601; B2CXA7; Q3UJA0; Q91X33;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Microsomal triglyceride transfer protein large subunit;
DE Flags: Precursor;
GN Name=Mttp; Synonyms=Mtp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver, and Small intestine;
RX PubMed=8660984; DOI=10.1006/geno.1996.0200;
RA Nakamuta M., Chang B.H., Hoogeveen R., Li W.H., Chan L.;
RT "Mouse microsomal triglyceride transfer protein large subunit: cDNA
RT cloning, tissue-specific expression and chromosomal localization.";
RL Genomics 33:313-316(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE PROMOTER USAGE,
RP FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), PROTEOLYTIC
RP PROCESSING (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=17312007; DOI=10.1084/jem.20062006;
RA Dougan S.K., Rava P., Hussain M.M., Blumberg R.S.;
RT "MTP regulated by an alternate promoter is essential for NKT cell
RT development.";
RL J. Exp. Med. 204:533-545(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Amnion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9502759; DOI=10.1172/jci1785;
RA Boren J., Veniant M.M., Young S.G.;
RT "Apo B100-containing lipoproteins are secreted by the heart.";
RL J. Clin. Invest. 101:1197-1202(1998).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=10713055; DOI=10.1074/jbc.275.11.7515;
RA Leung G.K., Veniant M.M., Kim S.K., Zlot C.H., Raabe M., Bjorkegren J.,
RA Neese R.A., Hellerstein M.K., Young S.G.;
RT "A deficiency of microsomal triglyceride transfer protein reduces
RT apolipoprotein B secretion.";
RL J. Biol. Chem. 275:7515-7520(2000).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=10744773;
RA Shelton J.M., Lee M.H., Richardson J.A., Patel S.B.;
RT "Microsomal triglyceride transfer protein expression during mouse
RT development.";
RL J. Lipid Res. 41:532-537(2000).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15897609; DOI=10.1194/jlr.d400043-jlr200;
RA Rava P., Athar H., Johnson C., Hussain M.M.;
RT "Transfer of cholesteryl esters and phospholipids as well as net deposition
RT by microsomal triglyceride transfer protein.";
RL J. Lipid Res. 46:1779-1785(2005).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16478722; DOI=10.1074/jbc.m512823200;
RA Rava P., Ojakian G.K., Shelness G.S., Hussain M.M.;
RT "Phospholipid transfer activity of microsomal triacylglycerol transfer
RT protein is sufficient for the assembly and secretion of apolipoprotein B
RT lipoproteins.";
RL J. Biol. Chem. 281:11019-11027(2006).
RN [11]
RP ALTERNATIVE PROMOTER USAGE, FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR
RP LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY (ISOFORMS 1 AND 2), AND
RP INTERACTION WITH P4HB (ISOFORMS 1 AND 2).
RX PubMed=17635917; DOI=10.1074/jbc.m700500200;
RA Mohler P.J., Zhu M.Y., Blade A.M., Ham A.J., Shelness G.S., Swift L.L.;
RT "Identification of a novel isoform of microsomal triglyceride transfer
RT protein.";
RL J. Biol. Chem. 282:26981-26988(2007).
RN [12]
RP DISRUPTION PHENOTYPE, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18502767; DOI=10.1074/jbc.m800398200;
RA Iqbal J., Rudel L.L., Hussain M.M.;
RT "Microsomal triglyceride transfer protein enhances cellular cholesteryl
RT esterification by relieving product inhibition.";
RL J. Biol. Chem. 283:19967-19980(2008).
RN [13]
RP INDUCTION BY FOXO1.
RX PubMed=18497885; DOI=10.1172/jci32914;
RA Kamagate A., Qu S., Perdomo G., Su D., Kim D.H., Slusher S., Meseck M.,
RA Dong H.H.;
RT "FoxO1 mediates insulin-dependent regulation of hepatic VLDL production in
RT mice.";
RL J. Clin. Invest. 118:2347-2364(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP INDUCTION.
RX PubMed=24353284; DOI=10.1530/jme-13-0042;
RA Wang F., Zhang X., Wang J., Chen M., Fan N., Ma Q., Liu R., Wang R., Li X.,
RA Liu M., Ning G.;
RT "LGR4 acts as a link between the peripheral circadian clock and lipid
RT metabolism in liver.";
RL J. Mol. Endocrinol. 52:133-143(2014).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP PRAP1.
RX PubMed=33168624; DOI=10.1074/jbc.ra120.015002;
RA Peng H., Chiu T.Y., Liang Y.J., Lee C.J., Liu C.S., Suen C.S., Yen J.J.,
RA Chen H.T., Hwang M.J., Hussain M.M., Yang H.C., Yang-Yen H.F.;
RT "PRAP1 is a novel lipid-binding protein that promotes lipid absorption by
RT facilitating MTTP-mediated lipid transport.";
RL J. Biol. Chem. 296:100052-100052(2020).
CC -!- FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester,
CC and phospholipid between phospholipid surfaces (PubMed:15897609,
CC PubMed:16478722, PubMed:18502767, PubMed:33168624). Required for the
CC assembly and secretion of plasma lipoproteins that contain
CC apolipoprotein B (PubMed:17635917, PubMed:10713055, PubMed:9502759,
CC PubMed:18502767, PubMed:33168624). May be involved in regulating
CC cholesteryl ester biosynthesis in cells that produce lipoproteins
CC (PubMed:18502767). {ECO:0000269|PubMed:10713055,
CC ECO:0000269|PubMed:15897609, ECO:0000269|PubMed:16478722,
CC ECO:0000269|PubMed:17635917, ECO:0000269|PubMed:18502767,
CC ECO:0000269|PubMed:33168624, ECO:0000269|PubMed:9502759}.
CC -!- FUNCTION: [Isoform 2]: Critical for the development of natural killer T
CC (NKT) cells (PubMed:17312007). Required for the assembly and secretion
CC of plasma lipoproteins that contain apolipoprotein B (PubMed:17635917).
CC {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:P55157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000250|UniProtKB:P55157};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:15897609};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896;
CC Evidence={ECO:0000305|PubMed:15897609};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cholesterol ester(in) = a cholesterol ester(out);
CC Xref=Rhea:RHEA:39007, ChEBI:CHEBI:17002;
CC Evidence={ECO:0000269|PubMed:15897609, ECO:0000269|PubMed:18502767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39008;
CC Evidence={ECO:0000305|PubMed:15897609};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out);
CC Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615;
CC Evidence={ECO:0000269|PubMed:15897609, ECO:0000269|PubMed:16478722,
CC ECO:0000269|PubMed:18502767, ECO:0000269|PubMed:33168624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39012;
CC Evidence={ECO:0000305|PubMed:16478722};
CC -!- SUBUNIT: Interacts with PRAP1. {ECO:0000269|PubMed:33168624}.
CC -!- SUBUNIT: [Isoform 1]: Heterodimer; heterodimerizes with the protein
CC disulfide isomerase (P4HB/PDI) (PubMed:17635917). Interacts with APOB
CC (By similarity). {ECO:0000250|UniProtKB:P55157,
CC ECO:0000269|PubMed:17635917}.
CC -!- SUBUNIT: [Isoform 2]: Heterodimer; heterodimerizes with the protein
CC disulfide isomerase (P4HB/PDI) (PubMed:17635917).
CC {ECO:0000269|PubMed:17635917}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:33168624}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917}. Golgi
CC apparatus {ECO:0000250|UniProtKB:P55157}. Note=Colocalizes with
CC P4HB/PDI in the endoplasmic reticulum (By similarity).
CC {ECO:0000250|UniProtKB:P55157}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum
CC {ECO:0000269|PubMed:17312007}. Golgi apparatus
CC {ECO:0000269|PubMed:17635917}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1; Synonyms=MTP-A;
CC IsoId=O08601-1; Sequence=Displayed;
CC Name=2; Synonyms=MTPv1, MTP-B;
CC IsoId=O08601-2; Sequence=VSP_038546;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Mainly expressed in the intestine and
CC the liver, and at lower levels in white and brown fat cells
CC (PubMed:17635917, PubMed:8660984). Expressed in heart (PubMed:9502759).
CC {ECO:0000269|PubMed:17635917, ECO:0000269|PubMed:8660984,
CC ECO:0000269|PubMed:9502759}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Ubiquitous, and is the major isoform
CC in hematopoietic cells and adipocytes. {ECO:0000269|PubMed:17312007,
CC ECO:0000269|PubMed:17635917}.
CC -!- DEVELOPMENTAL STAGE: Expression in the yolk sac tissues followed by
CC expression in the primordial liver cell nests as early as day 9 post-
CC coitum (9.5 dpc). Intestinal expression is detected around 12.5 dpc and
CC attains full adult expression patterns by 14.5 dpc.
CC {ECO:0000269|PubMed:10744773}.
CC -!- INDUCTION: Up-regulated by FOXO1. Expressed in a circadian manner in
CC the liver. {ECO:0000269|PubMed:18497885, ECO:0000269|PubMed:24353284}.
CC -!- PTM: [Isoform 2]: Cleaved by signal peptidase between residues Gln-33
CC and Asn-34. {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917}.
CC -!- DISRUPTION PHENOTYPE: Lowers plasma and tissue triglyceride levels, and
CC increases cellular free cholesterol. {ECO:0000269|PubMed:10713055,
CC ECO:0000269|PubMed:18502767}.
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DR EMBL; L47970; AAB51431.1; -; mRNA.
DR EMBL; EU553486; ACB41497.1; -; mRNA.
DR EMBL; AK146553; BAE27255.1; -; mRNA.
DR EMBL; CH466532; EDL12110.1; -; Genomic_DNA.
DR EMBL; BC012686; AAH12686.1; -; mRNA.
DR CCDS; CCDS38650.1; -. [O08601-1]
DR CCDS; CCDS51080.1; -. [O08601-2]
DR RefSeq; NP_001156929.1; NM_001163457.1. [O08601-2]
DR RefSeq; NP_032668.2; NM_008642.2. [O08601-1]
DR RefSeq; XP_006501165.1; XM_006501102.3. [O08601-2]
DR RefSeq; XP_006501166.1; XM_006501103.3. [O08601-1]
DR RefSeq; XP_017174963.1; XM_017319474.1.
DR RefSeq; XP_017174964.1; XM_017319475.1.
DR AlphaFoldDB; O08601; -.
DR SMR; O08601; -.
DR BioGRID; 201601; 7.
DR IntAct; O08601; 5.
DR MINT; O08601; -.
DR STRING; 10090.ENSMUSP00000096179; -.
DR CarbonylDB; O08601; -.
DR iPTMnet; O08601; -.
DR PhosphoSitePlus; O08601; -.
DR SwissPalm; O08601; -.
DR EPD; O08601; -.
DR jPOST; O08601; -.
DR MaxQB; O08601; -.
DR PaxDb; O08601; -.
DR PeptideAtlas; O08601; -.
DR PRIDE; O08601; -.
DR ProteomicsDB; 287517; -. [O08601-1]
DR ProteomicsDB; 287518; -. [O08601-2]
DR Antibodypedia; 25923; 247 antibodies from 29 providers.
DR DNASU; 17777; -.
DR Ensembl; ENSMUST00000029805; ENSMUSP00000029805; ENSMUSG00000028158. [O08601-1]
DR Ensembl; ENSMUST00000098580; ENSMUSP00000096179; ENSMUSG00000028158. [O08601-2]
DR GeneID; 17777; -.
DR KEGG; mmu:17777; -.
DR UCSC; uc008rmw.2; mouse. [O08601-1]
DR UCSC; uc008rmx.2; mouse. [O08601-2]
DR CTD; 4547; -.
DR MGI; MGI:106926; Mttp.
DR VEuPathDB; HostDB:ENSMUSG00000028158; -.
DR eggNOG; KOG4337; Eukaryota.
DR GeneTree; ENSGT00390000011412; -.
DR HOGENOM; CLU_014703_0_0_1; -.
DR InParanoid; O08601; -.
DR OMA; HVWGGSA; -.
DR OrthoDB; 673565at2759; -.
DR PhylomeDB; O08601; -.
DR TreeFam; TF328754; -.
DR Reactome; R-MMU-8866423; VLDL assembly.
DR Reactome; R-MMU-8963888; Chylomicron assembly.
DR Reactome; R-MMU-8964041; LDL remodeling.
DR BioGRID-ORCS; 17777; 3 hits in 74 CRISPR screens.
DR PRO; PR:O08601; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O08601; protein.
DR Bgee; ENSMUSG00000028158; Expressed in small intestine Peyer's patch and 209 other tissues.
DR Genevisible; O08601; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR GO; GO:1902388; F:ceramide 1-phosphate transfer activity; ISS:UniProtKB.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005319; F:lipid transporter activity; IDA:MGI.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISO:MGI.
DR GO; GO:1904121; F:phosphatidylethanolamine transfer activity; IDA:UniProtKB.
DR GO; GO:0120014; F:phospholipid transfer activity; IDA:UniProtKB.
DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0140344; F:triglyceride transfer activity; IDA:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IDA:MGI.
DR GO; GO:0006869; P:lipid transport; ISO:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IMP:MGI.
DR GO; GO:0042953; P:lipoprotein transport; IMP:MGI.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:MGI.
DR GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
DR GO; GO:0034377; P:plasma lipoprotein particle assembly; ISS:UniProtKB.
DR GO; GO:0006497; P:protein lipidation; IDA:MGI.
DR GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0006641; P:triglyceride metabolic process; IDA:MGI.
DR GO; GO:0034197; P:triglyceride transport; ISS:UniProtKB.
DR Gene3D; 1.25.10.20; -; 1.
DR Gene3D; 2.30.230.10; -; 1.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR045811; MTP_lip-bd.
DR InterPro; IPR039988; MTTP.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR001747; Vitellogenin_N.
DR PANTHER; PTHR13024; PTHR13024; 1.
DR Pfam; PF19444; MTP_lip_bd; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR SMART; SM00638; LPD_N; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 1.
DR PROSITE; PS51211; VITELLOGENIN; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Cholesterol metabolism; Disulfide bond;
KW Endoplasmic reticulum; Golgi apparatus; Lipid metabolism; Lipid transport;
KW Lipid-binding; Reference proteome; Signal; Steroid metabolism;
KW Sterol metabolism; Transport.
FT SIGNAL 1..21
FT CHAIN 22..894
FT /note="Microsomal triglyceride transfer protein large
FT subunit"
FT /id="PRO_0000041595"
FT DOMAIN 28..658
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 174..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT VAR_SEQ 1..20
FT /note="MILLAVLFLCFFSSYSASVK -> MTVVMGKCQVSDGRQLLLFYAVLLLFPT
FT LCAMQNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17312007"
FT /id="VSP_038546"
FT CONFLICT 654..656
FT /note="GKA -> KGT (in Ref. 1; AAB51431 and 2; ACB41497)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="V -> L (in Ref. 1; AAB51431, 2; ACB41497, 4;
FT AAH12686 and 5; EDL12110)"
FT /evidence="ECO:0000305"
FT CONFLICT 872
FT /note="E -> Q (in Ref. 1; AAB51431 and 2; ACB41497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 894 AA; 99099 MW; 3D8E5EB470CAA6FC CRC64;
MILLAVLFLC FFSSYSASVK GHTTGLSLNN ERLYKLTYST EVFLDGGKGK PQDSVGYKIS
SDVDVVLLWR NPDGDDDQVI QVTITAVNVE NAGQQRGEKS IFQGKSTPKI IGKDNLEALQ
RPMLLHLVRG KVKEFYSYEN EPVGIENLKR GLASLFQMQL SSGTTNEVDI SGDCKVTYQA
QQDKVVKIKA LDTCKIERSG FTTANQVLGV SSKATSVTTY KIEDSFVTAV LAEETRAFAL
NFQQTIAGKI VSKQKLELKT TEAGPRMIPG KQVAGVIKAV DSKYKAIPIV GQVLERVCKG
CPSLAEHWKS IRKNLEPENL SKAEAVQSFL AFIQHLRTSR REEILQILKA EKKEVLPQLV
DAVTSAQTPD SLEAILDFLD FKSDSSIILQ ERFLYACGFA THPDEELLRA LLSKFKGSFA
SNDIRESVMI IIGALVRKLC QNEGCKLKAV VEAKKLILGG LEKPEKKEDT TMYLLALKNA
LLPEGIPLLL KYAEAGEGPV SHLATTVLQR YDVSFITDEV KKTLNRIYHQ NRKVHEKTVR
TTAAAVILKN PSYMDVKNIL LSIGELPKEM NKYMLTVVQD ILHFEMPASK MIRRVLKEMA
VHNYDRFSKS GSSSAYTGYV ERSPRAASTY SLDILYSGSG ILRRSNLNIF QYIGKAELHG
SQVVIEAQGL EGLIAATPDE GEENLDSYAG MSAILFDVQL RPVTFFNGYS DLMSKMLSAS
GDPVSVVKGL ILLIDHSQDI QLQSGLKANM EIQGGLAIDI SGSMEFSLWY RESKTRVKNR
VAVVITSDVT VDASFVKAGV ESRAETEAGL EFISTVQFSQ YPFLVCMQMD KAEAPLRQFE
TKYERLSTGR GYVSRRRKES LVAGCELPLH QENSEMCNVV FPPQPESDNS GGWF
