VTU1_DROME
ID VTU1_DROME Reviewed; 141 AA.
AC P11449; A0JQ49; Q1RKQ5; Q9VMK4;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Vitelline membrane protein Vm26Aa;
DE AltName: Full=Protein SV17.5;
DE AltName: Full=Protein TU-2;
DE Flags: Precursor;
GN Name=Vm26Aa; Synonyms=VM26A.1; ORFNames=CG9048;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=3119397; DOI=10.1016/0012-1606(87)90497-0;
RA Burke T., Waring G.L., Popodi E., Minoo P.;
RT "Characterization and sequence of follicle cell genes selectively expressed
RT during vitelline membrane formation in Drosophila.";
RL Dev. Biol. 124:441-450(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8293994; DOI=10.1016/0378-1119(93)90455-c;
RA Scherer L.J., Harris D.H., White M.K., Steel L.S., Jin J., Petri W.H.;
RT "Comparative analysis of the sequence and structure of two Drosophila
RT melanogaster genes encoding vitelline membrane proteins.";
RL Gene 136:121-127(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17244601; DOI=10.1093/molbev/msm009;
RA Jagadeeshan S., Singh R.S.;
RT "Rapid evolution of outer egg membrane proteins in the Drosophila
RT melanogaster subgroup: a case of ecologically driven evolution of female
RT reproductive traits.";
RL Mol. Biol. Evol. 24:929-938(2007).
RN [4]
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 [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Kapadia B.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-108.
RC STRAIN=Oregon-R;
RX PubMed=3143615; DOI=10.1016/0012-1606(88)90367-3;
RA Scherer L.J., Harris D.H., Petri W.H.;
RT "Drosophila vitelline membrane genes contain a 114 base pair region of
RT highly conserved coding sequence.";
RL Dev. Biol. 130:786-788(1988).
CC -!- FUNCTION: Major early eggshell protein. {ECO:0000269|PubMed:3119397}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Follicle cells. {ECO:0000269|PubMed:3119397}.
CC -!- DEVELOPMENTAL STAGE: Expressed during vitelline membrane biosynthesis.
CC {ECO:0000269|PubMed:3119397}.
CC -!- SIMILARITY: Belongs to the vitelline membrane protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK57076.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M18280; AAA29015.1; -; Genomic_DNA.
DR EMBL; L08788; AAC37191.1; -; Genomic_DNA.
DR EMBL; EF441664; ABO71705.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52310.1; -; Genomic_DNA.
DR EMBL; BT025155; ABE73325.1; -; mRNA.
DR EMBL; BT029419; ABK57076.1; ALT_INIT; mRNA.
DR EMBL; M22699; AAA29017.1; -; Genomic_DNA.
DR PIR; A27249; A27249.
DR RefSeq; NP_001260115.1; NM_001273186.1.
DR RefSeq; NP_476783.1; NM_057435.3.
DR AlphaFoldDB; P11449; -.
DR BioGRID; 59994; 2.
DR DIP; DIP-21684N; -.
DR IntAct; P11449; 1.
DR STRING; 7227.FBpp0305434; -.
DR PaxDb; P11449; -.
DR DNASU; 33829; -.
DR EnsemblMetazoa; FBtr0079239; FBpp0078869; FBgn0003979.
DR EnsemblMetazoa; FBtr0333232; FBpp0305434; FBgn0003979.
DR GeneID; 33829; -.
DR KEGG; dme:Dmel_CG9048; -.
DR CTD; 33829; -.
DR FlyBase; FBgn0003979; Vm26Aa.
DR VEuPathDB; VectorBase:FBgn0003979; -.
DR eggNOG; ENOG502TCVM; Eukaryota.
DR HOGENOM; CLU_1940274_0_0_1; -.
DR InParanoid; P11449; -.
DR OMA; SIQAPPC; -.
DR OrthoDB; 1565055at2759; -.
DR PhylomeDB; P11449; -.
DR BioGRID-ORCS; 33829; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33829; -.
DR PRO; PR:P11449; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003979; Expressed in adult abdomen and 16 other tissues.
DR ExpressionAtlas; P11449; baseline and differential.
DR Genevisible; P11449; DM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0060388; C:vitelline envelope; IDA:FlyBase.
DR GO; GO:0048477; P:oogenesis; HMP:FlyBase.
DR GO; GO:0007305; P:vitelline membrane formation involved in chorion-containing eggshell formation; IEP:FlyBase.
DR InterPro; IPR013135; Vitelline_membr_Cys-rich-dom.
DR Pfam; PF10542; Vitelline_membr; 1.
DR PROSITE; PS51137; VM; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..141
FT /note="Vitelline membrane protein Vm26Aa"
FT /id="PRO_0000022675"
FT DOMAIN 71..108
FT /note="VM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00483"
FT REGION 23..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 21..24
FT /note="TNVA -> PTWP (in Ref. 2; AAC37191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 14321 MW; B9F27FB516EEDBDA CRC64;
MKSFVCIALV AFAAAALASP TNVASATGST GSSVTTQDGE LEGVTGQGFG DLTRLRKSAY
GGSSGGYGGS SIPAPPCPKN YLFSCQPNLA PVPCSAPAPS YGSAGAYSSP VATYVAPNYG
VPQHQQQLYS AYVPQTYGYQ Y
