GRK_DROME
ID GRK_DROME Reviewed; 295 AA.
AC P42287; Q9VLL2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein gurken;
DE Flags: Precursor;
GN Name=grk; ORFNames=CG17610;
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].
RC TISSUE=Ovary;
RX PubMed=7691414; DOI=10.1016/s0092-8674(05)80093-5;
RA Neuman-Silberberg F.S., Schuepbach T.;
RT "The Drosophila dorsoventral patterning gene gurken produces a dorsally
RT localized RNA and encodes a TGF alpha-like protein.";
RL Cell 75:165-174(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R;
RX PubMed=10790337; DOI=10.1006/dbio.2000.9690;
RA Thio G.L., Ray R.P., Barcelo G., Schuepbach T.;
RT "Localization of gurken RNA in Drosophila oogenesis requires elements in
RT the 5' and 3' regions of the transcript.";
RL Dev. Biol. 221:435-446(2000).
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;
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 [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH CNI.
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: Critical for defining the anterior-posterior and dorsal-
CC ventral axes of the egg. May signal directly to dorsal follicle cells
CC through the receptor torpedo (top). During oogenesis this signaling
CC pathway instructs follicle cells to follow a dorsal pathway of
CC development rather than the default ventral pathway.
CC {ECO:0000269|PubMed:10790337}.
CC -!- SUBUNIT: Interacts with cni. {ECO:0000269|PubMed:16396907}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16396907};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16396907}.
CC Note=Associates with the membranous cortex of yolk granules.
CC Transiently inserted into the cell membrane, and then reinternalized
CC during yolk uptake. cni is required for its transport to the oocyte
CC cell membrane.
CC -!- TISSUE SPECIFICITY: Expressed in nurse cells and oocyte up to oogenesis
CC stage 7. Specifically accumulates in dorsal anterior corner of the
CC oocyte during stages 9/10, at later stages expression is seen as an
CC anterior ring. In stage 10 ovaries, it is concentrated between the
CC oocyte nucleus and the adjacent oolemma. During vitellogenesis stage it
CC can be detected at the oocyte surface, especially on the microvilli. It
CC is also found at the microvilli covering the apical surface of the
CC follicular epithelium and within follicle cells.
CC {ECO:0000269|PubMed:10790337, ECO:0000269|PubMed:16396907}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28598.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF72000.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L22531; AAA28598.1; ALT_INIT; mRNA.
DR EMBL; AF223394; AAF72000.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014134; AAF52675.4; -; Genomic_DNA.
DR EMBL; AY051814; AAK93238.1; -; mRNA.
DR PIR; A48844; A48844.
DR RefSeq; NP_476568.2; NM_057220.3.
DR PDB; 5F5K; X-ray; 2.40 A; B=241-246.
DR PDB; 6PJP; X-ray; 2.45 A; B=241-253.
DR PDB; 6PJQ; X-ray; 2.50 A; B=241-253.
DR PDB; 6PJR; X-ray; 2.40 A; B=241-253.
DR PDB; 6PJU; X-ray; 2.50 A; B=241-253.
DR PDBsum; 5F5K; -.
DR PDBsum; 6PJP; -.
DR PDBsum; 6PJQ; -.
DR PDBsum; 6PJR; -.
DR PDBsum; 6PJU; -.
DR AlphaFoldDB; P42287; -.
DR SMR; P42287; -.
DR BioGRID; 60293; 63.
DR DIP; DIP-20922N; -.
DR IntAct; P42287; 4.
DR STRING; 7227.FBpp0079313; -.
DR GlyGen; P42287; 2 sites.
DR PaxDb; P42287; -.
DR PRIDE; P42287; -.
DR DNASU; 34171; -.
DR EnsemblMetazoa; FBtr0079708; FBpp0079313; FBgn0001137.
DR GeneID; 34171; -.
DR KEGG; dme:Dmel_CG17610; -.
DR UCSC; CG17610-RA; d. melanogaster.
DR CTD; 34171; -.
DR FlyBase; FBgn0001137; grk.
DR VEuPathDB; VectorBase:FBgn0001137; -.
DR eggNOG; ENOG502QS97; Eukaryota.
DR GeneTree; ENSGT00520000062215; -.
DR HOGENOM; CLU_880737_0_0_1; -.
DR InParanoid; P42287; -.
DR OMA; NTVFHSC; -.
DR OrthoDB; 1371173at2759; -.
DR PhylomeDB; P42287; -.
DR SignaLink; P42287; -.
DR BioGRID-ORCS; 34171; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34171; -.
DR PRO; PR:P42287; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001137; Expressed in crop (Drosophila) and 22 other tissues.
DR Genevisible; P42287; DM.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0030714; P:anterior/posterior axis specification, follicular epithelium; TAS:FlyBase.
DR GO; GO:0009952; P:anterior/posterior pattern specification; TAS:FlyBase.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030381; P:chorion-containing eggshell pattern formation; HMP:FlyBase.
DR GO; GO:0048263; P:determination of dorsal identity; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0008069; P:dorsal/ventral axis specification, ovarian follicular epithelium; TAS:FlyBase.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0008070; P:maternal determination of dorsal/ventral axis, ovarian follicular epithelium, germ-line encoded; IMP:FlyBase.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; TAS:FlyBase.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR043403; Gurken/Spitz.
DR PANTHER; PTHR12332; PTHR12332; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Developmental protein; Differentiation;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Oogenesis;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..295
FT /note="Protein gurken"
FT /id="PRO_0000007607"
FT TOPO_DOM 27..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 179..224
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 78..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..245
FT /note="Interaction with cni"
FT COMPBIAS 124..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 192..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 214..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6PJU"
SQ SEQUENCE 295 AA; 33280 MW; 80E993704DE3123B CRC64;
MMQIPFTRIF KVIFVLSTIV AVTDCCSSRI LLLREHTLKI VQHQHSHMHE HAHELQQQIQ
ETAVELLNRL ELQRKQLEAS AQEEADQLHP DTDPNPDSGG QLPNADDSIA ADPEQDGIIL
GSSTDTWLAS ESSTPITDSE TVTTPETVTH TGEPPPDPSS SSTPDSTTPS PNDKETEIQM
LPCSEAYNTS FCLNGGHCFQ HPMVNNTVFH SCLCVNDYDG ERCAYKSWNG DYIYSPPTAQ
RKVRMAHIVF SFPVLLMLSS LYVLFAAVFM LRNVPDYRRK QQQLHLHKQR FFVRC
