ID A0A091PXI2_LEPDC Unreviewed; 873 AA.
AC A0A091PXI2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Microsomal triglyceride transfer protein large subunit {ECO:0000313|EMBL:KFQ12046.1};
DE Flags: Fragment;
GN ORFNames=N330_10989 {ECO:0000313|EMBL:KFQ12046.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ12046.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ12046.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ12046.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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; KK679865; KFQ12046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PXI2; -.
DR PhylomeDB; A0A091PXI2; -.
DR Proteomes; UP000053001; 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 Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 8..642
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ12046.1"
FT NON_TER 873
FT /evidence="ECO:0000313|EMBL:KFQ12046.1"
SQ SEQUENCE 873 AA; 98157 MW; 57FE186FE3A8CBBB CRC64;
GHTTGPSLNN DKLYKFAYST EVYVDRVKAS LQKSAGYRIS SGVDVNLLWR NPDNDDDQLI
KITIRDVQVE NVNERPAAKN IFKGKSTEKI IGKEYLEALQ RPIVIELVRG KVKNFYSYQN
EPGFTQNIKR GLASLFQLQL HSGAAYEVDV SGKCNTTYHV RQDQVTKIKA LDSCEIEKQG
FTSYNRILDV STKASSATIY VLEDSFIKSI KAEENYVLLL NFRRKTGAKI VSKQRLELKS
VQAGPGLIAG KQVTSVIKTL DSSYTAVSLV AEPVKSECKK CPSLSEHWQS IREHMYPEKL
SKAEAARSFL SFIQNIRKAT KEEILQIIRS ENKELLPQIV DAITSAQTPA SLEAIVEFLD
FKDASTSTLQ ERFLYACGFA SHPSEMLLKS LTAKFKGDIA NEEIRETLVI VMGALIRKLC
DREGCKLPAV VEAKRLILNR LEKAKKDDNV RMYLLALKNA LLPEAIPLLL KYVESEEGAI
SNLAATALQR YNPSFLTKEV KETMNRIYHQ NRKVHEKTVR TTAAAIILNS NPSYMEVKNI
LLSIGELPPE MSKYMLSMIQ DILHFEMPSS KTVRQVLKDM HAHNYDRFSK MGSSSAYSGY
ITRGPDVSST YSFDILYSGS GILRRSNMNI RIFDRNAELH AIQVVIEAQG LESIIAATPD
EGEENLDSFA GMSAILFDVQ LRPVTFFQGY GDLMSKMFSA TGDPINVVKG LILLTDYSQE
IQLQSGPKAS VEFLGSLAID ISGGMEFSLW YRESKTNVKN RVAMFVAGNA EVDSFFVKTG
METTLEVETT LDFISTVQFS QYPFLVCMQM DRVESPFRRY MTKYESLPSG RRYTARRGKA
ELLAGNEYPL HQENSNMCKK VFSAKSDSSS NWF
//
