ID   MTP_MEGAM               Reviewed;         886 AA.
AC   A0A0N6WHT4;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Microsomal triglyceride transfer protein {ECO:0000303|PubMed:26210738, ECO:0000312|EMBL:AKN79614.1};
DE   Flags: Precursor;
GN   Name=MTTP {ECO:0000303|PubMed:26210738};
OS   Megalobrama amblycephala (Chinese blunt snout bream) (Brema carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Xenocyprididae; Xenocypridinae; Megalobrama.
OX   NCBI_TaxID=75352 {ECO:0000312|EMBL:AKN79614.1};
RN   [1] {ECO:0000312|EMBL:AKN79614.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, INDUCTION, AND
RP   PHYLOGENETIC ANALYSIS.
RC   TISSUE=Liver {ECO:0000303|PubMed:26210738, ECO:0000312|EMBL:AKN79614.1};
RX   PubMed=26210738; DOI=10.1016/j.cbpb.2015.07.004;
RA   Li J.Y., Zhang D.D., Jiang G.Z., Li X.F., Zhang C.N., Zhou M., Liu W.B.,
RA   Xu W.N.;
RT   "Cloning and characterization of microsomal triglyceride transfer protein
RT   gene and its potential connection with peroxisome proliferator-activated
RT   receptor (PPAR) in blunt snout bream (Megalobrama amblycephala).";
RL   Comp. Biochem. Physiol. 189:23-33(2015).
CC   -!- FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester,
CC       and phospholipid between phospholipid surfaces. Required for the
CC       secretion of plasma lipoproteins that contain apolipoprotein B.
CC       {ECO:0000250|UniProtKB:P55157}.
CC   -!- SUBUNIT: Heterodimer; heterodimerizes with the protein disulfide
CC       isomerase. Interacts with apolipoprotein B.
CC       {ECO:0000250|UniProtKB:P55157}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P55157}.
CC   -!- DEVELOPMENTAL STAGE: In juvenile fish, high level of expression in
CC       liver, intestine, kidney and muscle, and very low levels in heart,
CC       spleen and gill. {ECO:0000269|PubMed:26210738}.
CC   -!- INDUCTION: By elevated dietary lipid levels in the intestine of the
CC       juvenile fish. {ECO:0000269|PubMed:26210738}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KM980090; AKN79614.1; -; mRNA.
DR   AlphaFoldDB; A0A0N6WHT4; -.
DR   SMR; A0A0N6WHT4; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:1902388; F:ceramide 1-phosphate transfer activity; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization 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: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; Lipid transport; Signal; Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..886
FT                   /note="Microsomal triglyceride transfer protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5006009902"
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"
FT   DISULFID        440..445
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
SQ   SEQUENCE   886 AA;  97483 MW;  BBBD2D543A6D4079 CRC64;
     MLRLAGLLLC VTSFLSTSSL GANAGPRLDN DRLYRYSYSA ELGLNRPTGS TRGNPGFRIS
     SDVDISLVWR NPEIQDEQLL QVQISNVQVE SAGKHSRKNN IFHGSSTESI LGKVRLEALQ
     RPFMVLWKMG KIRSLYAHKG EPATIKNLKR GVASMLMMQL KSGKMMEADS SGKCLVEYKA
     TKHQVIRTKH LDTCKTQEKG FTTYSPVLGV SGKSASETVI TLENGIIKSA DVEETHILSI
     NARHTAATKV LSRQSLTLKK IEVGPTEVAG KDVAGVVKSL DDKFMSVGVI VEKVKAKCKG
     CPNLMDTWKA VRSKLEPDSL SKAEAPRSFL TLLHSLRKAS KAEILTVLRN CSKTALPQLV
     DAVTSAQTTS SLSAILEFLD FSKKEGLVLQ ERFLYACGFA SHPTETMLQS LLDVSQGKIG
     SPDIKESVVI IMGALLRKLC LKGACELPTV VKVKELLLAG PDSTQVESEV QMYLLALKNA
     LLPEAVPLLA KYAESEVGAY STIAITALQR YDPVLITPEV KKTVNRIYHQ NQRIYEKNVR
     AAAADVIMSS SPSYMEVKNV LLSIGHLPHE MNKYMLSKVQ DILRFEMPAC KLVQQVMKDM
     ISHNYDRFSK TGSSSAFSGF MAQTADVIST YNLDILYSGS GVLRRSNMNI YGQSNNALLH
     GLQVTIEAQG LESLIAATAD EGEEELESFA GMSALLFDVQ LRPVTFFKGY SDLMSKMFSM
     SGDPINVVKG LILLTDHSQV IPLQSGLRAS AEFQGGLAID ISGGMEFSLW YRESKTSVNN
     RGALVVIGNV TVDMDFVSAG VEVGFETEAS LDFITTVQFS EYPFLVCMQM DKTTFPFREM
     VSKQEKLPSG QTFSTKRSRD QLVPGSEFPL HQENSNMCKK VFEQAW