CNI_DROME
ID CNI_DROME Reviewed; 144 AA.
AC P49858; A4V0S2; Q53XF2; Q9V423;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein cornichon;
GN Name=cni; ORFNames=CG5855;
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 [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=7540118; DOI=10.1016/0092-8674(95)90016-0;
RA Roth S., Neuman-Silberberg F.S., Barcelo G., Schuepbach T.;
RT "Cornichon and the EGF receptor signaling process are necessary for both
RT anterior-posterior and dorsal-ventral pattern formation in Drosophila.";
RL Cell 81:967-978(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
RN [3]
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INTERACTION WITH GRK.
RX PubMed=16396907; DOI=10.1242/dev.02219;
RA Boekel C., Dass S., Wilsch-Braeuninger M., Roth S.;
RT "Drosophila Cornichon acts as cargo receptor for ER export of the TGFalpha-
RT like growth factor Gurken.";
RL Development 133:459-470(2006).
CC -!- FUNCTION: Acts as cargo receptor necessary for the transportation of
CC gurken (grk) to a transitional endoplasmic reticulum (tER) site and
CC promotes its incorporation into coat protein complex II (COPII)
CC vesicles. Associated with gurken, produces a signal received by torpedo
CC resulting in a signaling pathway that first establishes posterior
CC follicle cell fates and normal localization of the anterior and
CC posterior determinants, later they act in a signaling event inducing
CC dorsal follicle cell fates and regulating the dorsal-ventral pattern of
CC egg and embryo. {ECO:0000269|PubMed:16396907,
CC ECO:0000269|PubMed:7540118}.
CC -!- SUBUNIT: Interacts with grk. {ECO:0000269|PubMed:16396907}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16396907}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16396907}.
CC -!- TISSUE SPECIFICITY: Expressed in male and female somatic tissues.
CC {ECO:0000269|PubMed:16396907}.
CC -!- DEVELOPMENTAL STAGE: Detectable in the germline from germarium stages
CC onwards and becomes enriched within the oocyte during early and middle
CC stages of oogenesis. In early stages, it is present in the nurse cell
CC oocyte cluster. It is highly expressed in stage 1-6 egg chambers,
CC expression ceases during stage 7 and cannot be detected in stages 8 and
CC 9. During stage 10, it is reexpressed in the nurse cells.
CC {ECO:0000269|PubMed:16396907, ECO:0000269|PubMed:7540118}.
CC -!- SIMILARITY: Belongs to the cornichon family. {ECO:0000305}.
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DR EMBL; U28069; AAA86527.1; -; mRNA.
DR EMBL; AE014134; AAF53521.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53522.1; -; Genomic_DNA.
DR EMBL; BT011529; AAS15665.1; -; mRNA.
DR PIR; A56724; A56724.
DR RefSeq; NP_001260495.1; NM_001273566.1.
DR RefSeq; NP_477068.1; NM_057720.3.
DR RefSeq; NP_723959.1; NM_165151.2.
DR AlphaFoldDB; P49858; -.
DR SMR; P49858; -.
DR BioGRID; 60978; 4.
DR IntAct; P49858; 19.
DR STRING; 7227.FBpp0080405; -.
DR TCDB; 8.A.61.1.6; the endoplasmic reticulum-derived vesicle protein, erv14 (erv14) family.
DR PaxDb; P49858; -.
DR PRIDE; P49858; -.
DR DNASU; 34967; -.
DR EnsemblMetazoa; FBtr0080848; FBpp0080405; FBgn0000339.
DR EnsemblMetazoa; FBtr0080849; FBpp0080406; FBgn0000339.
DR EnsemblMetazoa; FBtr0337082; FBpp0308005; FBgn0000339.
DR GeneID; 34967; -.
DR KEGG; dme:Dmel_CG5855; -.
DR UCSC; CG5855-RA; d. melanogaster.
DR UCSC; CG5855-RB; d. melanogaster.
DR CTD; 34967; -.
DR FlyBase; FBgn0000339; cni.
DR VEuPathDB; VectorBase:FBgn0000339; -.
DR eggNOG; KOG2729; Eukaryota.
DR GeneTree; ENSGT00950000182834; -.
DR HOGENOM; CLU_112942_1_0_1; -.
DR InParanoid; P49858; -.
DR OMA; WIAFLLN; -.
DR OrthoDB; 1602458at2759; -.
DR PhylomeDB; P49858; -.
DR Reactome; R-DME-204005; COPII-mediated vesicle transport.
DR Reactome; R-DME-5694530; Cargo concentration in the ER.
DR BioGRID-ORCS; 34967; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34967; -.
DR PRO; PR:P49858; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000339; Expressed in Malpighian tubule and 24 other tissues.
DR ExpressionAtlas; P49858; baseline and differential.
DR Genevisible; P49858; DM.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:FlyBase.
DR GO; GO:0007350; P:blastoderm segmentation; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:FlyBase.
DR InterPro; IPR003377; Cornichon.
DR InterPro; IPR033466; Cornichon_conserved.
DR Pfam; PF03311; Cornichon; 1.
DR SMART; SM01398; Cornichon; 1.
DR PROSITE; PS01340; CORNICHON; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Protein transport; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..144
FT /note="Protein cornichon"
FT /id="PRO_0000122234"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..122
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Interaction with grk"
SQ SEQUENCE 144 AA; 16931 MW; 27692A3F68ECE1A9 CRC64;
MAFNFTAFTY IVALIGDAFL IFFAIFHVIA FDELKTDYKN PIDQCNSLNP LVLPEYLLHI
FLNLLFLFCG EWFSLCINIP LIAYHIWRYK NRPVMSGPGL YDPTTVLKTD TLYRNMREGW
IKLAVYLISF FYYIYGMVYS LIST
