TMEDE_DROME
ID TMEDE_DROME Reviewed; 216 AA.
AC Q9I7K5; Q961C1;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Transmembrane emp24 domain-containing protein eca;
DE AltName: Full=Protein eclair {ECO:0000312|EMBL:AAG22137.2};
DE Flags: Precursor;
GN Name=eca {ECO:0000312|EMBL:AAG22137.2, ECO:0000312|FlyBase:FBgn0069242};
GN ORFNames=CG33104;
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:0000312|EMBL:AAG22137.2}
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAG22137.2}
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 [3] {ECO:0000312|EMBL:AAK93117.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93117.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15327786; DOI=10.1016/j.mod.2004.05.006;
RA Bartoszewski S., Luschnig S., Desjeux I., Grosshans J.,
RA Nusslein-Volhard C.;
RT "Drosophila p24 homologues eclair and baiser are necessary for the activity
RT of the maternally expressed Tkv receptor during early embryogenesis.";
RL Mech. Dev. 121:1259-1273(2004).
RN [5]
RP FUNCTION.
RX PubMed=21383842; DOI=10.1371/journal.pone.0017173;
RA Kondylis V., Tang Y., Fuchs F., Boutros M., Rabouille C.;
RT "Identification of ER proteins involved in the functional organisation of
RT the early secretory pathway in Drosophila cells by a targeted RNAi
RT screen.";
RL PLoS ONE 6:E17173-E17173(2011).
CC -!- FUNCTION: Eca and bai are essential, though not redundant, for
CC dorsoventral patterning of the embryo. Specifically required during
CC early embryogenesis for the activity of maternal tkv, while the zygotic
CC tkv is not affected. Involved in Golgi organization.
CC {ECO:0000269|PubMed:15327786, ECO:0000269|PubMed:21383842}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:15327786}.
CC -!- DISRUPTION PHENOTYPE: Mutant embryos exhibit reduced dpp signaling
CC during early embryogenesis. Maternal tkv is not active and is not
CC secreted. {ECO:0000269|PubMed:15327786}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000255}.
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DR EMBL; AE014297; AAG22137.2; -; Genomic_DNA.
DR EMBL; AY051693; AAK93117.1; -; mRNA.
DR RefSeq; NP_788616.1; NM_176439.3.
DR AlphaFoldDB; Q9I7K5; -.
DR SMR; Q9I7K5; -.
DR BioGRID; 66336; 6.
DR IntAct; Q9I7K5; 1.
DR STRING; 7227.FBpp0081576; -.
DR TCDB; 9.B.188.1.5; the transmembrane emp24 domain-containing protein (tmed) family.
DR PaxDb; Q9I7K5; -.
DR PRIDE; Q9I7K5; -.
DR DNASU; 41177; -.
DR EnsemblMetazoa; FBtr0082098; FBpp0081576; FBgn0069242.
DR GeneID; 41177; -.
DR KEGG; dme:Dmel_CG33104; -.
DR UCSC; CG33104-RA; d. melanogaster.
DR CTD; 41177; -.
DR FlyBase; FBgn0069242; eca.
DR VEuPathDB; VectorBase:FBgn0069242; -.
DR eggNOG; KOG1690; Eukaryota.
DR GeneTree; ENSGT00940000159012; -.
DR HOGENOM; CLU_066963_2_2_1; -.
DR InParanoid; Q9I7K5; -.
DR OMA; STAIKWS; -.
DR OrthoDB; 1294924at2759; -.
DR PhylomeDB; Q9I7K5; -.
DR BioGRID-ORCS; 41177; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41177; -.
DR PRO; PR:Q9I7K5; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0069242; Expressed in spermathecum and 37 other tissues.
DR Genevisible; Q9I7K5; DM.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0038024; F:cargo receptor activity; ISM:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:FlyBase.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0048193; P:Golgi vesicle transport; ISM:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR GO; GO:0061355; P:Wnt protein secretion; IMP:FlyBase.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Developmental protein; Endoplasmic reticulum; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..216
FT /note="Transmembrane emp24 domain-containing protein eca"
FT /evidence="ECO:0000255"
FT /id="PRO_0000393927"
FT TOPO_DOM 21..182
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..126
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT COILED 134..164
FT /evidence="ECO:0000255"
FT MOTIF 213..216
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
SQ SEQUENCE 216 AA; 25159 MW; 877A2BDD1FBB442D CRC64;
MRDQFISLAL ILCVLHSACG LYFHISETER KCFIEEVPDE TTVIVNYKVE LYDPRSNGFM
PSSPGIGMHV EVRDSDDKIV LSRVYSSQGR ISFTSHTPGE HVICMFSNST AWFSGAQLRV
HLDIQVGEHA IDYAHVAQKE KLTELQLRIR QLLDQVEQIT KEQNYQRYRE ERFRHTSEST
NSRVLWWSLA QTVVLVCMGF WQMRHLKSFF EAKKLV
