ID A0A091DYE9_FUKDA Unreviewed; 894 AA.
AC A0A091DYE9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Microsomal triglyceride transfer protein large subunit {ECO:0000256|ARBA:ARBA00013847};
GN ORFNames=H920_01458 {ECO:0000313|EMBL:KFO37134.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO37134.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO37134.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO37134.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00023723};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572;
CC Evidence={ECO:0000256|ARBA:ARBA00023723};
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:0000256|ARBA:ARBA00023724};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896;
CC Evidence={ECO:0000256|ARBA:ARBA00023724};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cholesterol ester(in) = a cholesterol ester(out);
CC Xref=Rhea:RHEA:39007, ChEBI:CHEBI:17002;
CC Evidence={ECO:0000256|ARBA:ARBA00023670};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39008;
CC Evidence={ECO:0000256|ARBA:ARBA00023670};
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:0000256|ARBA:ARBA00023680};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39012;
CC Evidence={ECO:0000256|ARBA:ARBA00023680};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
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DR EMBL; KN121093; KFO37134.1; -; Genomic_DNA.
DR RefSeq; XP_010601789.1; XM_010603487.1.
DR AlphaFoldDB; A0A091DYE9; -.
DR STRING; 885580.ENSFDAP00000017397; -.
DR Ensembl; ENSFDAT00000009560; ENSFDAP00000017397; ENSFDAG00000005966.
DR GeneID; 104847882; -.
DR CTD; 4547; -.
DR eggNOG; KOG4337; Eukaryota.
DR OMA; HVWGGSA; -.
DR OrthoDB; 5305490at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0120013; F:lipid transfer activity; IEA:UniProt.
DR GO; GO:0005548; F:phospholipid transporter activity; IEA:InterPro.
DR Gene3D; 1.25.10.20; Vitellinogen, superhelical; 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:SF1; MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN LARGE SUBUNIT; 1.
DR PANTHER; PTHR13024; MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN, LARGE SUBUNIT; 1.
DR Pfam; PF19444; MTP_lip_bd; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR SMART; SM00638; LPD_N; 1.
DR SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR PROSITE; PS51211; VITELLOGENIN; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..894
FT /note="Microsomal triglyceride transfer protein large
FT subunit"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001872031"
FT DOMAIN 28..659
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
SQ SEQUENCE 894 AA; 99326 MW; 8951871B39F787C8 CRC64;
MILLAVLFLC FISSYSASVK GHTTGLSLNN DRIYKLTYSA EVFLDGGKGK HQDSIGYRIS
SSVDAVLLWR SPDGDDDQLI QIKMTDIKVE DVNQQRGEKS IFKGKKSPKI LGKQNLEALQ
RPTLLHLIRG KVKEFYSYQN EPVAIENLKR GLASLFQMQL SSGTTNEVDI SGNCKMTYQA
QQDKVVKIKA LDSCKIERSG FTTPNQVLGV SSKATSVTTY KIEDSFVLAV FSEEIHTFAL
NFLNTIQGRI VSKQKLELKT TDAGPRLIPG KQVATVIKAV DSKYTSIPIV GQVFQSACKR
CPSLSEHWQS IRKHLQPDNL SKAEAVRSFL AFVQHLRTAK REDILQVLKT SSPDVLPQLV
DAITSAQTPD SLEAILDFLD FKSDSSIILQ ERFLYACGFA SHPDEELLRV LIGKFKGSFG
SNDIRETVMI IIGALVRKLC QNEGCKLKAV VEAKKLILGG LEKPAKKEDT KMYLLALKNA
LLPEGIPLLL KYAEASEGPI SHLATTTLQR YDVPFITDEV KKTLNRIYHQ NHKVHEKTVR
TTAAAVILNS NPSYMEVKNI LLSIGELPKE MNKYMLAMIQ DILRFETPAS KMVRRVLKEM
VAHNYDRFSK SGSSSAFTGY IDRSSHSAST YSLDILYSGS GILRRSNLNI FQYIGKADLH
GSQVVIEAQG LEALIAATPD EGEEDLDSYA GLSAILFDVQ LRPVTFFTGY SDLMSKMLSA
SSDPVSVVKG LILLIDHSQE LQLQSGLKAN IEVQGGLAID ISGSMEFSLW YRESKTRVKN
RVAVVINADI TVDSSFVKAG LEARTESEAG LEFVSTVQFS QYPFLVCMQM DKADIPLRQS
ETKYERLSTG RGYVIRKRRE SLLAGCELPL HQENSDMCNM VFAPQPESSS SGWF
//
