MTP_MESAU
ID MTP_MESAU Reviewed; 895 AA.
AC P55158;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Microsomal triglyceride transfer protein large subunit;
DE Flags: Precursor;
GN Name=MTTP; Synonyms=MTP;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Intestine;
RX PubMed=7961879; DOI=10.1016/s0021-9258(19)62022-3;
RA Lin M.C., Arbeeny C., Bergquist K., Kienzle B., Gordon D.A., Wetterau J.R.;
RT "Cloning and regulation of hamster microsomal triglyceride transfer
RT protein. The regulation is independent from that of other hepatic and
RT intestinal proteins which participate in the transport of fatty acids and
RT triglycerides.";
RL J. Biol. Chem. 269:29138-29145(1994).
CC -!- FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester,
CC and phospholipid between phospholipid surfaces (By similarity).
CC Required for the assembly and secretion of plasma lipoproteins that
CC contain apolipoprotein B (By similarity). May be involved in regulating
CC cholesteryl ester biosynthesis in cells that produce lipoproteins (By
CC similarity). {ECO:0000250|UniProtKB:O08601,
CC ECO:0000250|UniProtKB:P55157}.
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:0000250|UniProtKB:P55157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896;
CC Evidence={ECO:0000250|UniProtKB:P55157};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cholesterol ester(in) = a cholesterol ester(out);
CC Xref=Rhea:RHEA:39007, ChEBI:CHEBI:17002;
CC Evidence={ECO:0000250|UniProtKB:P55157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39008;
CC Evidence={ECO:0000250|UniProtKB:P55157};
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:0000250|UniProtKB:P55157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39012;
CC Evidence={ECO:0000250|UniProtKB:P55157};
CC -!- SUBUNIT: Heterodimer; heterodimerizes with the protein disulfide
CC isomerase (P4HB/PDI). Interacts with APOB (By similarity). Interacts
CC with PRAP1 (By similarity). {ECO:0000250|UniProtKB:O08601,
CC 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; U14995; AAA53143.1; -; mRNA.
DR PIR; A55413; A55413.
DR RefSeq; NP_001268537.1; NM_001281608.1.
DR AlphaFoldDB; P55158; -.
DR SMR; P55158; -.
DR STRING; 10036.XP_005082019.1; -.
DR GeneID; 101836921; -.
DR CTD; 4547; -.
DR eggNOG; KOG4337; Eukaryota.
DR OrthoDB; 673565at2759; -.
DR Proteomes; UP000189706; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS:UniProtKB.
DR GO; GO:1904121; F:phosphatidylethanolamine transfer activity; ISS:UniProtKB.
DR GO; GO:0120014; F:phospholipid transfer activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0140344; F:triglyceride transfer activity; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Golgi apparatus; Lipid transport;
KW Lipid-binding; Reference proteome; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..895
FT /note="Microsomal triglyceride transfer protein large
FT subunit"
FT /id="PRO_0000041594"
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 895 AA; 99388 MW; 841062179548059D CRC64;
MILLAVLFLC FFSSYSASVK GHTTGLSLNN ERLYKLTYST EVFLDGGKGK LKDSVGYRIS
SDVDVVLLWR NPDGDDDQLI QVTITAVNVE NVNQQRGEKS IFKGKTTPKI IGKDNLEALQ
RPVLLHLVRG KVKEFYSYEN EPVGIENLKR GLASLFQMQL SSGTTNEVDI SGDCKVTYQA
QQDKVVKTKA LDTCKIERSG FTTVNQVLGV SSKATSVTTY KIEDSFVTAV HAEETRDFSL
NFLQAIAGKI VSKQKLELKT TEAGPRMVPG KQVAGVIKAL DSKYTAIPIV GQVLQSACQG
CPSLAEHWQS IRKHLEPENL SNAKAVSSFL AFIQHLRTAR REEILQILKA EKKEVLPQLV
DAVTSAQTPD SLEAILDFLD FKSDSSIVLQ ERFLYACGFA SHPDEELLRA LLSKFKGSFA
SNDIRETVMI IIGALVRKLC QNEGCKLKAV VEAKKLILGG LEKPEKKEDT TMYLLALKNA
LLPEGIPLLL KYAEAGEGPV SHLATTVLQR YDVSFITDEV KKTLNRIYHQ NRKIHEKTVR
TTAAAVILKS NPSYMDVKNI LLSIGELPKE MNKYMLTFVR DILNFEMPSS KMIRRVLKEM
VAHNYDRFSK SGSSSAYTGY IERSPHAAST YSLDMLYSGS GILRRSNLNV FQYLGKAGLH
GSQVVIEAQG LESLIAATPD EGEENLDSYA GMSAILFDVQ LRPVTFFNGY SDLMSKMLSA
SGDPVSVVKG LILLIDHSQD IQLQSGLKAN MEIQGGLAID ISGSMEFSLW YRESKTRVKN
RVAVVIDSAV TVDSSFVKAG LESRAETEAG LEFISTVQFS QYPFLVCMQM DRAEAPFRQF
ETKYERLSTG RGYVSRRRKE SLVSGYELPL HQENSEMCNM VFPPQPESDN SGGWF
