ID A0A0M4ESK4_DROBS Unreviewed; 872 AA.
AC A0A0M4ESK4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Mtp {ECO:0000313|EMBL:ALC40337.1};
GN ORFNames=Dbus_chr2Lg2422 {ECO:0000313|EMBL:ALC40337.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC40337.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC40337.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC40337.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012523; ALC40337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4ESK4; -.
DR STRING; 30019.A0A0M4ESK4; -.
DR OMA; HVWGGSA; -.
DR Proteomes; UP000494163; Chromosome 2l sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0005548; F:phospholipid transporter activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
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:SF0; MICROSOMAL TRIACYLGLYCEROL TRANSFER PROTEIN; 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:UP000494163};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..872
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005793975"
FT DOMAIN 27..628
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
SQ SEQUENCE 872 AA; 97566 MW; 25D13252C9607822 CRC64;
MHLNRRKNNN NVWLLLLLST VTAGASLIPP GTQQLYTLQS QVSLDQLQSA ASQELGYNFE
TKLKINSVWS KNEEQLLQLY FGESRVAAGD KQREIKTLPD RPFYIALVKG QPQQVIAHTS
RDESLLNLER GIASLLQLRH SDSEETELDV SGHCRVRYEV KSSTRVEKTK TDCALWDLRV
SYHPEQALGV DQQSQEQVQY ELSADGALLR AQSTETHRLS LAAKSDAGSL VRASLKLEHV
AEGAETVQQL QHESLEAAIE SLLEWYRVFE LEANLLQQFE HLSPQLQSEH VGKSSLALAF
AQLLPLARLA KQPEFEQLLQ SQSKLAVQLV DLLGAVQTFE AHNATFAHLY QGSQTKTEQM
ELLEKYLQSL AVATHPERRI VEHLYNFLQQ ADNKAKQSKL RDTVLQTLAV LARQSGFADN
DQLLQQIRVY LLEGLATDDA TLYIRALQNL RDLGTIDALL EQATHSKDVK VSVAALQALK
AFPANSFAQP QRRQFESIFY QHRRRYDSSA RTLALDVLLS MRPDAAQLGA LLDYLASNDR
QFEIKTYVLQ KLRMLSELCP RFRAAFLTSL RQRSHVNNYH VLGQRGLTTV LSRQLSHSPA
FNESLLSIQE VSQGILKRGS VEFLLHAGRE QASSFKLGIY TAGLGSMVGD SDADAGSDNI
PADDELEQEE TITAGMEISV QGSQLRPLVF FSGQTELMGH VWGGTASDST PAYQATTLAQ
DHEQYIVLSS GATLYWRILG ARSVDLNGKV NFSLWNRNAQ TEIQQNTGSA VVGRIAVGFT
YAKLVQDFSL THEPKLSLNA DLDFYSGIKL CMQLQSPDQL LTYNNTRAAH LQAVAKPYVK
YLRSSRTHKS AGRTFSLNQK NNDMCNMIFA DY
//
