MTP_BOVIN
ID MTP_BOVIN Reviewed; 887 AA.
AC P55156;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Microsomal triglyceride transfer protein large subunit;
DE Flags: Precursor; Fragment;
GN Name=MTTP; Synonyms=MTP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Small intestine;
RX PubMed=8361539; DOI=10.1038/365065a0;
RA Sharp D., Blinderman L., Combs K.A., Kienzle B., Ricci B., Wager-Smith K.,
RA Gil C.M., Turck C.W., Bouma M.-E., Rader D.J., Aggerbeck L.P., Gregg R.E.,
RA Gordon D.A., Wetterau J.R.;
RT "Cloning and gene defects in microsomal triglyceride transfer protein
RT associated with abetalipoproteinaemia.";
RL Nature 365:65-69(1993).
RN [2]
RP INTERACTION WITH P4HB.
RX PubMed=2351674; DOI=10.1016/s0021-9258(19)38742-3;
RA Wetterau J.R., Combs K.A., Spinner S.N., Joiner B.J.;
RT "Protein disulfide isomerase is a component of the microsomal triglyceride
RT transfer protein complex.";
RL J. Biol. Chem. 265:9800-9807(1990).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8876250; DOI=10.1073/pnas.93.21.11991;
RA Jamil H., Gordon D.A., Eustice D.C., Brooks C.M., Dickson J.K. Jr.,
RA Chen Y., Ricci B., Chu C.H., Harrity T.W., Ciosek C.P. Jr., Biller S.A.,
RA Gregg R.E., Wetterau J.R.;
RT "An inhibitor of the microsomal triglyceride transfer protein inhibits apoB
RT secretion from HepG2 cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11991-11995(1996).
RN [4]
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).
CC -!- FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester,
CC and phospholipid between phospholipid surfaces (PubMed:15897609,
CC PubMed:8876250). 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:0000250|UniProtKB:P55157, ECO:0000269|PubMed:15897609,
CC ECO:0000269|PubMed:8876250}.
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};
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:8876250};
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) (PubMed:2351674). Interacts with APOB (By
CC similarity). Interacts with PRAP1 (By similarity).
CC {ECO:0000250|UniProtKB:O08601, ECO:0000250|UniProtKB:P55157,
CC ECO:0000269|PubMed:2351674}.
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; X78567; CAA55310.1; -; mRNA.
DR PIR; A46764; A46764.
DR AlphaFoldDB; P55156; -.
DR SMR; P55156; -.
DR STRING; 9913.ENSBTAP00000015850; -.
DR BindingDB; P55156; -.
DR ChEMBL; CHEMBL2934; -.
DR SwissLipids; SLP:000000409; -.
DR PaxDb; P55156; -.
DR PeptideAtlas; P55156; -.
DR PRIDE; P55156; -.
DR eggNOG; KOG4337; Eukaryota.
DR HOGENOM; CLU_014703_0_0_1; -.
DR InParanoid; P55156; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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:1904121; F:phosphatidylethanolamine 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:0140344; F:triglyceride transfer activity; IDA:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
DR GO; GO:0034377; P:plasma lipoprotein particle assembly; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
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 Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Golgi apparatus; Lipid transport; Lipid-binding; Reference proteome;
KW Signal; Transport.
FT SIGNAL <1..11
FT /evidence="ECO:0000255"
FT CHAIN 12..887
FT /note="Microsomal triglyceride transfer protein large
FT subunit"
FT /id="PRO_0000041592"
FT DOMAIN 21..655
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 167..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT NON_TER 1
SQ SEQUENCE 887 AA; 99032 MW; 45CD454541054BBF CRC64;
FLCFISSYSA SVKGHTTGLS LNNDRLYKLT YSTEVFLDRG KGNLQDSVGY RISSNVDVAL
LWRSPDGDDN QLIQITMKDV NLENVNQQRG EKSIFKGKKS SQIIRKENLE AMQRPVLLHL
IHGKIKEFYS YQNEPAAIEN LKRGLASLFQ MQLSSGTTNE VDISGDCKVT YQAHQDKVTK
IKALDSCKIE RAGFTTPHQV LGVTSKATSV TTYKIEDSFV VAVLSEEIRA LRLNFLQSIA
GKIVSRQKLE LKTTEASVRL KPGKQVAAII KAVDSKYTAI PIVGQVFQSK CKGCPSLSEH
WQSIRKHLQP DNLSKAEAVR SFLAFIKHLR TAKKEEILQI LKAENKEVLP QLVDAVTSAQ
TPDSLDAILD FLDFKSTESV ILQERFLYAC AFASHPDEEL LRALISKFKG SFGSNDIRES
VMIIIGALVR KLCQNQGCKL KGVIEAKKLI LGGLEKAEKK EDIVMYLLAL KNARLPEGIP
LLLKYTETGE GPISHLAATT LQRYDVPFIT DEVKKTMNRI YHQNRKIHEK TVRTTAAAII
LKNNPSYMEV KNILLSIGEL PKEMNKYMLS IVQDILRFET PASKMVRQVL KEMVAHNYDR
FSKSGSSSAY TGYVERTSHS ASTYSLDILY SGSGILRRSN LNIFQYIEKT PLHGIQVVIE
AQGLEALIAA TPDEGEENLD SYAGLSALLF DVQLRPVTFF NGYSDLMSKM LSASSDPMSV
VKGLLLLIDH SQELQLQSGL KANMDVQGGL AIDITGAMEF SLWYRESKTR VKNRVSVLIT
GGITVDSSFV KAGLEIGAET EAGLEFISTV QFSQYPFLVC LQMDKEDVPY RQFETKYERL
STGRGYISRK RKESLIGGCE FPLHQENSDM CKVVFAPQPE SSSSGWF
