MTP_PIG
ID MTP_PIG Reviewed; 894 AA.
AC Q865F1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, 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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Small intestine;
RX PubMed=12177174;
RA Lu S., Huffman M., Yao Y., Mansbach C.M., Cheng X., Meng S., Black D.D.;
RT "Regulation of MTP expression in developing swine.";
RL J. Lipid Res. 43:1303-1311(2002).
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; AY217034; AAO61497.1; -; mRNA.
DR RefSeq; NP_999350.1; NM_214185.1.
DR AlphaFoldDB; Q865F1; -.
DR SMR; Q865F1; -.
DR STRING; 9823.ENSSSCP00000009789; -.
DR PaxDb; Q865F1; -.
DR PeptideAtlas; Q865F1; -.
DR PRIDE; Q865F1; -.
DR Ensembl; ENSSSCT00045051910; ENSSSCP00045036128; ENSSSCG00045030426.
DR GeneID; 397381; -.
DR KEGG; ssc:397381; -.
DR CTD; 4547; -.
DR eggNOG; KOG4337; Eukaryota.
DR InParanoid; Q865F1; -.
DR OrthoDB; 673565at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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..894
FT /note="Microsomal triglyceride transfer protein large
FT subunit"
FT /id="PRO_0000041596"
FT DOMAIN 28..662
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 174..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
SQ SEQUENCE 894 AA; 99771 MW; FBC410C925FA8F70 CRC64;
MILLAVLFLC FISSYSASVK GHTTGLSLNN DRLYKLKYST EVFLDRGKGN LQDSVGYQIS
SNVDVVLLWR SPDGDDDQLI QITIKDVKVE NVNQQRGEKS IFKGKKPPQI IRKENLEALQ
RPVLLHLIHG KVKEFYSYQN EPPAIQNLKR GLASLFQMQL SSGTTNEVDI SGDCKVTYQA
HQDKVTKIKA LDSCTIERSG FTTRNQVLGV TSKATSVTTY KIEDSFVVAV LAEEIHALRL
NFLQTIAGKI VSKQKLELKT TEAGPRLKSG KQVAAIIKAV DSKYTAIPIV GQVFQSECKG
CSSLSQHWQS VRKHLQPDNL SKTEAVRSFL TFIQHLRTAK KEEILQILKA ENKDILPQLV
DAVTSAQTPD SLDAILDFLD FKSDSNIILQ ERFLYACGFA SHPDEELLRA LISKFKGSFG
SNDIRESVMI IIGALVRKLC QNEGCKLKAV VDAKKLILGG LERAEKKEDT MMYLLALKNA
RLPEGIPLLL KYAEAAEGPI SHLAVTTLQR YDAPFITDEV KKTMNRIYHQ TRKVHEKTVR
TTAAAVILNN NPSYMEVKNI LLSIGELPKE MNKYMLSIVQ DILRFEMPAS KMVRRVLKEM
VAHNYDRFSK SGSSSAYTGY IERGPHSAST YSLDILYSGS GILRRSNLNI FQYVGKTPLH
AIQVVIEAQG LEALIAATPD EGEENLDSYA GLSPLLFDVQ LRPVTFFNGY SDLMSKMLSA
SSDPISVVKG LILLIDHSQE LQLQSGLKAN MEVQGGLAID ISGSMEFSLW YRESKTRVKN
RVTVVITGDI TVDSSFVKAG LEISAETEAG LEFISTVQFS QYPFLVCLQM DRDGIPYRQF
ETKYERLSTG RGYVSRKRKE ILVAGSEFPL HQENSEMCKV VFAPEPESSS SGWF
