MTP_CAEEL
ID MTP_CAEEL Reviewed; 892 AA.
AC G5ECG7;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Microsomal triglyceride transfer protein homolog {ECO:0000303|PubMed:23639358};
DE AltName: Full=Defecation suppressor of clk-1 {ECO:0000312|WormBase:K02D7.4};
DE Flags: Precursor;
GN Name=dsc-4 {ECO:0000312|WormBase:K02D7.4};
GN ORFNames=K02D7.4 {ECO:0000312|WormBase:K02D7.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAR27937.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF SER-62 AND ALA-146.
RX PubMed=14657502; DOI=10.1126/science.1087167;
RA Shibata Y., Branicky R., Landaverde I.O., Hekimi S.;
RT "Redox regulation of germline and vulval development in Caenorhabditis
RT elegans.";
RL Science 302:1779-1782(2003).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17924655; DOI=10.1021/bi700762z;
RA Rava P., Hussain M.M.;
RT "Acquisition of triacylglycerol transfer activity by microsomal
RT triglyceride transfer protein during evolution.";
RL Biochemistry 46:12263-12274(2007).
RN [4] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF SER-62 AND ALA-146.
RX PubMed=23639358; DOI=10.1016/j.jmb.2013.04.020;
RA Zhang J., Hashmi S., Cheema F., Al-Nasser N., Bakheet R., Parhar R.S.,
RA Al-Mohanna F., Gaugler R., Hussain M.M., Hashmi S.;
RT "Regulation of lipoprotein assembly, secretion and fatty acid beta-
RT oxidation by Krueppel-like transcription factor, klf-3.";
RL J. Mol. Biol. 425:2641-2655(2013).
CC -!- FUNCTION: Catalyzes the transport of cholesteryl ester, and
CC phospholipid between phospholipid surfaces (By similarity). Does not
CC catalyze transport of triglycerides (PubMed:17924655). Required for the
CC assembly and secretion of plasma lipoproteins that contain
CC apolipoprotein B (PubMed:17924655, PubMed:14657502). Required for
CC normal expression of klf-3 (PubMed:23639358).
CC {ECO:0000250|UniProtKB:P55157, ECO:0000269|PubMed:14657502,
CC ECO:0000269|PubMed:17924655, ECO:0000269|PubMed:23639358}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with protein disulfide isomerase.
CC {ECO:0000269|PubMed:17924655}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:17924655}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the intestine throughout larval
CC stages and adulthood. {ECO:0000269|PubMed:23639358}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown suppresses the slow
CC germline development and the delayed egg-production of clk-1 mutants,
CC but does not affect the rate of postembryonic development.
CC {ECO:0000269|PubMed:14657502}.
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DR EMBL; AY428645; AAR27937.1; -; mRNA.
DR EMBL; BX284604; CCD69687.1; -; Genomic_DNA.
DR PIR; T32984; T32984.
DR RefSeq; NP_499903.3; NM_067502.5.
DR AlphaFoldDB; G5ECG7; -.
DR SMR; G5ECG7; -.
DR STRING; 6239.K02D7.4; -.
DR EPD; G5ECG7; -.
DR PaxDb; G5ECG7; -.
DR PeptideAtlas; G5ECG7; -.
DR EnsemblMetazoa; K02D7.4.1; K02D7.4.1; WBGene00001099.
DR GeneID; 176852; -.
DR KEGG; cel:CELE_K02D7.4; -.
DR CTD; 176852; -.
DR WormBase; K02D7.4; CE33667; WBGene00001099; dsc-4.
DR eggNOG; KOG4337; Eukaryota.
DR GeneTree; ENSGT00390000011412; -.
DR HOGENOM; CLU_323959_0_0_1; -.
DR InParanoid; G5ECG7; -.
DR OMA; PYREIFT; -.
DR OrthoDB; 170426at2759; -.
DR PhylomeDB; G5ECG7; -.
DR Reactome; R-CEL-8964041; LDL remodeling.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001099; Expressed in larva and 3 other tissues.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0005548; F:phospholipid transporter activity; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; HEP:WormBase.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0042953; P:lipoprotein transport; IDA:UniProtKB.
DR GO; GO:0034377; P:plasma lipoprotein particle assembly; IDA:UniProtKB.
DR InterPro; IPR045811; MTP_lip-bd.
DR InterPro; IPR039988; MTTP.
DR PANTHER; PTHR13024; PTHR13024; 1.
DR Pfam; PF19444; MTP_lip_bd; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Reference proteome;
KW Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..892
FT /note="Microsomal triglyceride transfer protein homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_5015091924"
FT MUTAGEN 62
FT /note="S->F: In qm182; lipid contents in the intestine
FT increases by 40%, and by 80% on a klf-3 mutant background.
FT Suppresses the delayed germline development and egg-laying
FT on a clk-1 mutant background, but does not affect the rate
FT of postembryonic development; when associated with T-146."
FT /evidence="ECO:0000269|PubMed:14657502,
FT ECO:0000269|PubMed:23639358"
FT MUTAGEN 146
FT /note="A->T: In qm182; lipid contents in the intestine
FT increases by 40%, and by 80% on a klf-3 mutant background.
FT Suppresses the delayed germline development and egg-laying
FT on a clk-1 mutant background, but does not affect the rate
FT of postembryonic development; when associated with F-62."
FT /evidence="ECO:0000269|PubMed:14657502,
FT ECO:0000269|PubMed:23639358"
SQ SEQUENCE 892 AA; 101017 MW; 325B80DFEB35968E CRC64;
MFSSRIWLLL AVTVGVCLAV PDLDEIKKNL RKHGPDYYKN QPKMNENTVR LLKVDYWFRT
ESMIYDDIDN KEKDPSTVIA GNFSFETLHH DVEGGMLGRF TLTQCNTDNC GNPSPIYIAF
RQGGNNAEHI LKASDESDAT WNFLYAIVNT IYTPAEYGEG DEQTVDTIYG RCFVNFGRPE
DKRFRRIIEK CDLGYGTNFT KFEGIESVQY DQDVWYTQNT KVDADIIMVD AIEMLAFKSP
LHEKYGFTLE SRTHVEITNR TRVFVTSYCN DTVPSAKCAE QAFGAVRVGG KLYEHVKIAQ
EQSNKLTKLI GTYRRHLQDM GDSHICEKHS LLYSQIAQEA RLAKRQDWEA AIQYPENDHV
LSLIASALGG VGTAESITTA REVLLTASPD YLDDLLFGIS QSSSNNEKWH KQLMYWLGSL
DKKSEEYWKV ANTIATVLNK RCEASTSSLN SCNKGKETIV NKFITDLTAG GVEVRVLEVL
ENIPIFGSYT FAKKFICETE SEDVQKAALN VILAASKNLY ETQLTHKLIK LFRNTCSQET
PTSHSQLAID ILLKCVPDHQ NVATLILRTE TLNPDDQEKW HYLYKAIEAS GNKDELKAEF
WSRMRKFKVF RPNFLHRALQ ADSHVHWQEI ADASNFQLFS TANTEFLQKS FKRSIFELSM
KKGRKEHNLF SLSIDTEHLE QFVTGSASSR SGAPQGSVRI GVAGHKLPTH HIFKGSTDLL
STVWEADGRT HKAFEGHVPV RDVRLSVPLL SGLTLDVDSV GAISMRVLAS AEVSLWNQRS
NAKAEAYTSG SLHLTASLYH HSEPVRHVES TISALSTFTT DTRAIFETLP YDFCLRTSNS
NVDINQKTVV QDQIGKHKKK TLNRKRVHPG VTYRLDDSTI RQCNSYLEQF RL
