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VTU4_DROME
ID   VTU4_DROME              Reviewed;         116 AA.
AC   Q9VKI3; A4UM13; Q24588; Q29QF0; Q629J1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Vitelline membrane protein Vm32E {ECO:0000312|EMBL:ABO71722.1};
DE   Flags: Precursor;
GN   Name=Vm32E {ECO:0000312|EMBL:AAF53085.1}; ORFNames=CG16874;
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] {ECO:0000305, ECO:0000312|EMBL:AAA29019.1, ECO:0000312|PIR:A48321}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Oregon-R {ECO:0000312|EMBL:CAA31103.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:CAA31103.1};
RX   PubMed=2495206; DOI=10.1002/dvg.1020100106;
RA   Gigliotti S., Graziani F., De Ponti L., Rafti F., Manzi A., Lavorgna G.,
RA   Gargiulo G., Malva C.;
RT   "Sex-, tissue-, and stage-specific expression of a vitelline membrane
RT   protein gene from region 32 of the second chromosome of Drosophila
RT   melanogaster.";
RL   Dev. Genet. 10:33-41(1989).
RN   [2] {ECO:0000312|EMBL:ABO71722.1}
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   [3] {ECO:0000312|EMBL:AAF53085.1}
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   [4] {ECO:0000305, ECO:0000312|EMBL:AAF53085.1}
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   [5] {ECO:0000312|EMBL:ABC86502.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Booth B., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Major early eggshell protein. {ECO:0000269|PubMed:2495206}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2495206}.
CC   -!- TISSUE SPECIFICITY: Expressed in stage 10 egg-chambers, localized in
CC       the outer eggshell (chorion membrane). {ECO:0000269|PubMed:2495206}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during vitelline membrane biosynthesis.
CC       {ECO:0000269|PubMed:2495206}.
CC   -!- SIMILARITY: Belongs to the vitelline membrane family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC86502.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M27647; AAA29019.1; -; Genomic_DNA.
DR   EMBL; X12590; CAA31103.1; -; Genomic_DNA.
DR   EMBL; EF441681; ABO71722.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAF53085.1; -; Genomic_DNA.
DR   EMBL; BT024440; ABC86502.2; ALT_INIT; mRNA.
DR   PIR; A48321; A48321.
DR   RefSeq; NP_001285837.1; NM_001298908.1.
DR   RefSeq; NP_477103.1; NM_057755.2.
DR   AlphaFoldDB; Q9VKI3; -.
DR   BioGRID; 60618; 4.
DR   IntAct; Q9VKI3; 1.
DR   STRING; 7227.FBpp0079805; -.
DR   PaxDb; Q9VKI3; -.
DR   DNASU; 34558; -.
DR   EnsemblMetazoa; FBtr0080216; FBpp0079805; FBgn0014076.
DR   EnsemblMetazoa; FBtr0343618; FBpp0310213; FBgn0014076.
DR   GeneID; 34558; -.
DR   KEGG; dme:Dmel_CG16874; -.
DR   UCSC; CG16874-RA; d. melanogaster.
DR   CTD; 34558; -.
DR   FlyBase; FBgn0014076; Vm32E.
DR   VEuPathDB; VectorBase:FBgn0014076; -.
DR   HOGENOM; CLU_169196_0_0_1; -.
DR   InParanoid; Q9VKI3; -.
DR   OMA; FHQRIGM; -.
DR   OrthoDB; 1606944at2759; -.
DR   PhylomeDB; Q9VKI3; -.
DR   SignaLink; Q9VKI3; -.
DR   BioGRID-ORCS; 34558; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 34558; -.
DR   PRO; PR:Q9VKI3; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0014076; Expressed in adult abdomen and 10 other tissues.
DR   ExpressionAtlas; Q9VKI3; baseline and differential.
DR   Genevisible; Q9VKI3; DM.
DR   GO; GO:0042600; C:egg chorion; IDA:FlyBase.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0060388; C:vitelline envelope; IDA:FlyBase.
DR   GO; GO:0008316; F:structural constituent of vitelline membrane; IMP:UniProtKB.
DR   GO; GO:0007305; P:vitelline membrane formation involved in chorion-containing eggshell formation; IMP:UniProtKB.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..116
FT                   /note="Vitelline membrane protein Vm32E"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000398796"
FT   DOMAIN          36..73
FT                   /note="VM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00483"
FT   CONFLICT        14
FT                   /note="I -> L (in Ref. 2; ABO71722)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="G -> R (in Ref. 1; AAA29019)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        78..81
FT                   /note="HYVG -> TTWT (in Ref. 1; AAA29019/CAA31103)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   116 AA;  12100 MW;  CB448C9A3CDD9A99 CRC64;
     MQIVALTLVA FVAIAGASCP YAAPAPAYSA PAASSGYPAP PCPTNYLFSC QPNLAPAPCA
     QEAPAYGSAG AYTEQVPHYV GSPNREQLQQ FHQRIGMAAL MEELRGLGQG IQGQQY
 
 
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