MTP_RAT
ID MTP_RAT Reviewed; 896 AA.
AC D4A1W8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Microsomal triglyceride transfer protein large subunit;
DE Flags: Precursor;
GN Name=Mttp; Synonyms=Mtp;
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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).
CC -!- FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester,
CC and phospholipid between phospholipid surfaces (PubMed:15897609,
CC PubMed:16478722). Required for the assembly and secretion of plasma
CC lipoproteins that contain apolipoprotein B (By similarity). May be
CC involved in regulating cholesteryl ester biosynthesis in cells that
CC produce lipoproteins (By similarity). {ECO:0000250|UniProtKB:O08601,
CC ECO:0000269|PubMed:15897609, ECO:0000269|PubMed:16478722}.
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:0000269|PubMed:16478722};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000305|PubMed:16478722};
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};
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39012;
CC Evidence={ECO:0000305|PubMed:15897609};
CC -!- SUBUNIT: Heterodimer; heterodimerizes with the protein disulfide
CC isomerase (P4HB/PDI) (By similarity). Interacts with APOB (By
CC similarity). Interacts with PRAP1 (By similarity).
CC {ECO:0000250|UniProtKB:O08601, ECO:0000250|UniProtKB:P55157}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P55157}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P55157}. Note=Colocalizes with P4HB/PDI in the
CC endoplasmic reticulum. {ECO:0000250|UniProtKB:P55157}.
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DR EMBL; AABR07013550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07013551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473952; EDL82305.1; -; Genomic_DNA.
DR RefSeq; NP_001101197.1; NM_001107727.1.
DR AlphaFoldDB; D4A1W8; -.
DR SMR; D4A1W8; -.
DR STRING; 10116.ENSRNOP00000014630; -.
DR SwissLipids; SLP:000000410; -.
DR PhosphoSitePlus; D4A1W8; -.
DR PaxDb; D4A1W8; -.
DR PeptideAtlas; D4A1W8; -.
DR PRIDE; D4A1W8; -.
DR Ensembl; ENSRNOT00000014631; ENSRNOP00000014630; ENSRNOG00000010655.
DR GeneID; 310900; -.
DR KEGG; rno:310900; -.
DR CTD; 4547; -.
DR RGD; 1308388; Mttp.
DR eggNOG; KOG4337; Eukaryota.
DR GeneTree; ENSGT00390000011412; -.
DR HOGENOM; CLU_014703_0_0_1; -.
DR InParanoid; D4A1W8; -.
DR OMA; HVWGGSA; -.
DR OrthoDB; 673565at2759; -.
DR PhylomeDB; D4A1W8; -.
DR TreeFam; TF328754; -.
DR Reactome; R-RNO-8866423; VLDL assembly.
DR Reactome; R-RNO-8963888; Chylomicron assembly.
DR Reactome; R-RNO-8964041; LDL remodeling.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000234681; Chromosome 2.
DR Bgee; ENSRNOG00000010655; Expressed in jejunum and 13 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0031528; C:microvillus membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0034185; F:apolipoprotein binding; IPI:RGD.
DR GO; GO:1902388; F:ceramide 1-phosphate transfer activity; ISO:RGD.
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:RGD.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IMP:UniProtKB.
DR GO; GO:1904121; F:phosphatidylethanolamine transfer activity; IDA:UniProtKB.
DR GO; GO:0120014; F:phospholipid transfer activity; ISO:RGD.
DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0140344; F:triglyceride transfer activity; IDA:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IEP:RGD.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR GO; GO:0006869; P:lipid transport; IDA:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; IDA:RGD.
DR GO; GO:0042953; P:lipoprotein transport; ISO:RGD.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0015914; P:phospholipid transport; ISO:RGD.
DR GO; GO:0034377; P:plasma lipoprotein particle assembly; ISS:UniProtKB.
DR GO; GO:0006497; P:protein lipidation; ISO:RGD.
DR GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0034197; P:triglyceride transport; ISO:RGD.
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 Disulfide bond; Endoplasmic reticulum; Golgi apparatus; Lipid transport;
KW Lipid-binding; Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..896
FT /note="Microsomal triglyceride transfer protein large
FT subunit"
FT /id="PRO_5014087804"
FT DOMAIN 28..659
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 174..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
SQ SEQUENCE 896 AA; 99187 MW; B815F841AA9C3588 CRC64;
MILLAVLFLC FFSSYSASVK GHTTGLSLNN ERLYKLTYST EVFLDGGKGK LQDSVGYRIS
SDVDVVLLWR NPDGDDDQLI QVTITAVNVE NAGQQRGEKS IFKGKSTPKI VGKDNLEALR
RPMLLHLVRG KVKEFYSYEN EPVGIENLKR GLASLFQMQL TSGTTNEVDI SGDCKVTYQA
QQDKVVKIKA LDTCKIERSG FTTANQVLGV TSKATSVTTY KIEDSFVTAV VAEETRAFAL
NFLQTVAGKI VSKQKLELKT TEAGPRMVPG KQVAGVIKAI DSKYKAIPIV GQVLQSVCKG
CPSLAEHWQS IRKHLEPENL SNAEAVQSFL AFIQHLRTSR REEILQILKA EKKEVLPQLV
DAVTSAQTPA SLEAILDFLD FKSDSSIILQ ERFLYACGFA SHPDEELLQA LLSKFKGSFA
SNDIRESVMI IIGALVRKLC QNEGCKLKAV VEAKKLILGG LEKPEKKEDT TMYLLALKNA
LLPEGIPLLL KYAEAGEGPV SHLATTVLQR YDASFITDEV KKTLNRIYHQ NRKVHEKTVR
TTAAAVILKN NPSYMDVKNI LLSIGELPKE MNKYMLTIVQ DILHFEMPAS KMIRRVLKEM
IVHNYDRFSK SGSSSAYTGY VERSPHAAST YSLDILYSGS GILRRSNLNI FQYIGKAELH
GSQVVIEAQG LEGLIAATPD EGEENLDSYA GMSAILFDVQ LRPVTFFNGY SDLMSKMLSA
SGDPVSVVKG LILLIDHSQD IQLQSGLKAN MDIQGGLAID ISGSMEFSLW YRESKTRVKN
RVAVVITSDI TVDSSFVKAG LESRAETEAG LEFISTVQFS QYPFLVCMQM DKAEAPLRQF
ETKYERLSTG RGYVSRRRKE SLVPGCELPL HQENSEMCNV VFPPQPESGN SGGGWF
