MTP_DROME
ID MTP_DROME Reviewed; 886 AA.
AC Q9VIH3; Q961S9;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Microsomal triacylglycerol transfer protein {ECO:0000303|PubMed:16478722};
DE Short=MTP {ECO:0000303|PubMed:16478722};
DE Flags: Precursor;
GN Name=Mtp {ECO:0000312|FlyBase:FBgn0266369};
GN ORFNames=CG9342 {ECO:0000312|FlyBase:FBgn0266369};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|EMBL:AAF53946.2, ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
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 phospholipids such as
CC phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine)
CC and phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine)
CC between membranes. Required for the assembly and secretion of plasma
CC lipoproteins that contain apolipoprotein B.
CC {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 -!- 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:16478722};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16478722}. Golgi apparatus
CC {ECO:0000269|PubMed:16478722}.
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DR EMBL; AE014134; AAF53946.2; -; Genomic_DNA.
DR EMBL; AY050228; AAK84927.1; -; mRNA.
DR RefSeq; NP_610075.2; NM_136231.4.
DR AlphaFoldDB; Q9VIH3; -.
DR SMR; Q9VIH3; -.
DR IntAct; Q9VIH3; 6.
DR STRING; 7227.FBpp0080968; -.
DR SwissLipids; SLP:000000412; -.
DR PaxDb; Q9VIH3; -.
DR PRIDE; Q9VIH3; -.
DR EnsemblMetazoa; FBtr0081439; FBpp0080968; FBgn0266369.
DR GeneID; 35362; -.
DR KEGG; dme:Dmel_CG9342; -.
DR UCSC; CG9342-RA; d. melanogaster.
DR CTD; 35362; -.
DR FlyBase; FBgn0266369; Mtp.
DR VEuPathDB; VectorBase:FBgn0266369; -.
DR eggNOG; KOG4337; Eukaryota.
DR GeneTree; ENSGT00390000011412; -.
DR HOGENOM; CLU_014703_0_0_1; -.
DR InParanoid; Q9VIH3; -.
DR OMA; HVWGGSA; -.
DR OrthoDB; 673565at2759; -.
DR PhylomeDB; Q9VIH3; -.
DR Reactome; R-DME-8964041; LDL remodeling.
DR BioGRID-ORCS; 35362; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35362; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0266369; Expressed in arthropod fat body and 13 other tissues.
DR ExpressionAtlas; Q9VIH3; baseline and differential.
DR Genevisible; Q9VIH3; DM.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IDA:FlyBase.
DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0042157; P:lipoprotein metabolic process; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
DR GO; GO:0008039; P:synaptic target recognition; IMP:FlyBase.
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 Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..886
FT /note="Microsomal triacylglycerol transfer protein"
FT /id="PRO_5004334712"
FT DOMAIN 30..653
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 65
FT /note="D -> H (in Ref. 3; AAK84927)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="E -> D (in Ref. 3; AAK84927)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> Q (in Ref. 3; AAK84927)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="N -> H (in Ref. 3; AAK84927)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="A -> S (in Ref. 3; AAK84927)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="S -> R (in Ref. 3; AAK84927)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="V -> L (in Ref. 3; AAK84927)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="A -> G (in Ref. 3; AAK84927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 98776 MW; 98A8E3ADD052E1A3 CRC64;
MENKNKKCLR TLLLLALFLG LLEDGKTALI APNSQQIFKL QNQVILQELG RDSSSAETSY
TFETDLKINS VWSGDEDQLL EVFISGSKVD ASGKARSITR IPDRPFYISL VRGQPDKVIA
HTSKDQSLLN LERGIASLLQ LRLDASQEEE LDVSGLCRVS YNVKSSTKVE KTKRDCSLWD
LRVNYNPEEA LGVTQQAQET VFYELSSEGT LLHAESQENH RLNLAAKPDV GSFVKSSLIL
QHVSQGSEEV KQLQLGSLDK AIQSLLEWYR VFELESDVDG MISAIKEQTL EDQLKASLTE
LQSADVGKSS LALAYVKLIP LARITRQEQF EDLLTEHAEV LPQLVDLLGA VQTFDAHNAT
FGFLYKESET TSEQLDLLEK YLQSLAVATH PDRKIVEHLF GLLEQESIKK HLKLRESVIQ
TVATLTRQSG LDVEDPLLKE VRSYLLQGLT SKEPTLYIRA LQNLQDPATI EALLEHAQTG
EAPNLSVAAL QALKAFPLGS FNSSHRLQFE SIFYQRKRRF DSSARTLALD IILSLRPTQE
QLGNFLDYLA SNDRQFEIKT YVLQKLRMLA EKCPRFRALF KSELVKRRHV NNYNVLGQKG
LTTVLTRQLS QAPAFNETLL STQEVYQGIL KRGSVEFLLH AGRSQASSFK LGIYTAGLGS
LVGDGDSGDG NDAIPADDEF SEDEAVTAGM EISVQGAQLR PLVFFSGQTE LMGHVWGGSA
SDSTPAYQAT TLSQDNEHYI ILTSGATLHW RVLGARSVDL NGKVGFSLWN RNAQTEIQQN
TGSAVLGHLA VGFTYAKLVQ DFSITHEPKL SLNADLDFYS GIKLCMQLQR PEQLLKQTNV
RSVFLQSVDR PYAKHVRSTL SHKTAGCTFA LNQKNNEMCN LIFRDL
