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Protein

Protein gurken

Gene

grk

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Critical for defining the anterior-posterior and dorsal-ventral axes of the egg. May signal directly to dorsal follicle cells through the receptor torpedo (top). During oogenesis this signaling pathway instructs follicle cells to follow a dorsal pathway of development rather than the default ventral pathway.1 Publication

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: FlyBase
  • gurken receptor binding Source: FlyBase

GO - Biological processi

  • anterior/posterior axis specification, follicular epithelium Source: FlyBase
  • anterior/posterior pattern specification Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • cargo loading into COPII-coated vesicle Source: UniProtKB
  • cell fate determination Source: FlyBase
  • cell fate specification Source: FlyBase
  • chorion-containing eggshell pattern formation Source: FlyBase
  • dorsal/ventral axis specification, ovarian follicular epithelium Source: FlyBase
  • dorsal appendage formation Source: FlyBase
  • embryonic axis specification Source: FlyBase
  • epidermal growth factor receptor signaling pathway Source: FlyBase
  • establishment of oocyte nucleus localization involved in oocyte dorsal/ventral axis specification Source: FlyBase
  • gurken signaling pathway Source: FlyBase
  • maternal determination of dorsal/ventral axis, ovarian follicular epithelium, germ-line encoded Source: FlyBase
  • oocyte anterior/posterior axis specification Source: FlyBase
  • oocyte axis specification Source: FlyBase
  • oocyte dorsal/ventral axis specification Source: FlyBase
  • oocyte microtubule cytoskeleton organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Oogenesis

Enzyme and pathway databases

SignaLinkiP42287.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein gurken
Gene namesi
Name:grk
ORF Names:CG17610
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0001137. grk.

Subcellular locationi

  • Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

  • Note: Associates with the membranous cortex of yolk granules. Transiently inserted into the cell membrane, and then reinternalized during yolk uptake. cni is required for its transport to the oocyte cell membrane.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 247221ExtracellularSequence analysisAdd
BLAST
Transmembranei248 – 26821HelicalSequence analysisAdd
BLAST
Topological domaini269 – 29527CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: FlyBase
  • extracellular region Source: FlyBase
  • Golgi membrane Source: GOC
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 295269Protein gurkenPRO_0000007607Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi183 ↔ 198PROSITE-ProRule annotation
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence analysis
Disulfide bondi192 ↔ 212PROSITE-ProRule annotation
Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence analysis
Disulfide bondi214 ↔ 223PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP42287.

Miscellaneous databases

PMAP-CutDBP42287.

Expressioni

Tissue specificityi

Expressed in nurse cells and oocyte up to oogenesis stage 7. Specifically accumulates in dorsal anterior corner of the oocyte during stages 9/10, at later stages expression is seen as an anterior ring. In stage 10 ovaries, it is concentrated between the oocyte nucleus and the adjacent oolemma. During vitellogenesis stage it can be detected at the oocyte surface, especially on the microvilli. It is also found at the microvilli covering the apical surface of the follicular epithelium and within follicle cells.2 Publications

Gene expression databases

BgeeiP42287.
GenevisibleiP42287. DM.

Interactioni

Subunit structurei

Interacts with cni.1 Publication

GO - Molecular functioni

  • epidermal growth factor receptor binding Source: FlyBase
  • gurken receptor binding Source: FlyBase

Protein-protein interaction databases

BioGridi60293. 32 interactions.
DIPiDIP-20922N.
IntActiP42287. 2 interactions.
MINTiMINT-320623.
STRINGi7227.FBpp0079313.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5F5KX-ray2.40B241-246[»]
ProteinModelPortaliP42287.
SMRiP42287. Positions 187-225.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini179 – 22446EGF-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni215 – 24531Interaction with cniAdd
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KC03. Eukaryota.
ENOG4110MRC. LUCA.
InParanoidiP42287.
KOiK02447.
OMAiMHEHAHE.
OrthoDBiEOG7S4X7H.
PhylomeDBiP42287.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42287-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMQIPFTRIF KVIFVLSTIV AVTDCCSSRI LLLREHTLKI VQHQHSHMHE
60 70 80 90 100
HAHELQQQIQ ETAVELLNRL ELQRKQLEAS AQEEADQLHP DTDPNPDSGG
110 120 130 140 150
QLPNADDSIA ADPEQDGIIL GSSTDTWLAS ESSTPITDSE TVTTPETVTH
160 170 180 190 200
TGEPPPDPSS SSTPDSTTPS PNDKETEIQM LPCSEAYNTS FCLNGGHCFQ
210 220 230 240 250
HPMVNNTVFH SCLCVNDYDG ERCAYKSWNG DYIYSPPTAQ RKVRMAHIVF
260 270 280 290
SFPVLLMLSS LYVLFAAVFM LRNVPDYRRK QQQLHLHKQR FFVRC
Length:295
Mass (Da):33,280
Last modified:January 17, 2003 - v2
Checksum:i80E993704DE3123B
GO

Sequence cautioni

The sequence AAA28598.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF72000.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22531 mRNA. Translation: AAA28598.1. Different initiation.
AF223394 Genomic DNA. Translation: AAF72000.1. Different initiation.
AE014134 Genomic DNA. Translation: AAF52675.4.
AY051814 mRNA. Translation: AAK93238.1.
PIRiA48844.
RefSeqiNP_476568.2. NM_057220.3.
UniGeneiDm.355.

Genome annotation databases

EnsemblMetazoaiFBtr0079708; FBpp0079313; FBgn0001137.
GeneIDi34171.
KEGGidme:Dmel_CG17610.
UCSCiCG17610-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22531 mRNA. Translation: AAA28598.1. Different initiation.
AF223394 Genomic DNA. Translation: AAF72000.1. Different initiation.
AE014134 Genomic DNA. Translation: AAF52675.4.
AY051814 mRNA. Translation: AAK93238.1.
PIRiA48844.
RefSeqiNP_476568.2. NM_057220.3.
UniGeneiDm.355.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5F5KX-ray2.40B241-246[»]
ProteinModelPortaliP42287.
SMRiP42287. Positions 187-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60293. 32 interactions.
DIPiDIP-20922N.
IntActiP42287. 2 interactions.
MINTiMINT-320623.
STRINGi7227.FBpp0079313.

Proteomic databases

PaxDbiP42287.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079708; FBpp0079313; FBgn0001137.
GeneIDi34171.
KEGGidme:Dmel_CG17610.
UCSCiCG17610-RA. d. melanogaster.

Organism-specific databases

CTDi34171.
FlyBaseiFBgn0001137. grk.

Phylogenomic databases

eggNOGiENOG410KC03. Eukaryota.
ENOG4110MRC. LUCA.
InParanoidiP42287.
KOiK02447.
OMAiMHEHAHE.
OrthoDBiEOG7S4X7H.
PhylomeDBiP42287.

Enzyme and pathway databases

SignaLinkiP42287.

Miscellaneous databases

GenomeRNAii34171.
NextBioi787225.
PMAP-CutDBP42287.
PROiP42287.

Gene expression databases

BgeeiP42287.
GenevisibleiP42287. DM.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila dorsoventral patterning gene gurken produces a dorsally localized RNA and encodes a TGF alpha-like protein."
    Neuman-Silberberg F.S., Schuepbach T.
    Cell 75:165-174(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  2. "Localization of gurken RNA in Drosophila oogenesis requires elements in the 5' and 3' regions of the transcript."
    Thio G.L., Ray R.P., Barcelo G., Schuepbach T.
    Dev. Biol. 221:435-446(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: Oregon-R.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Drosophila Cornichon acts as cargo receptor for ER export of the TGFalpha-like growth factor Gurken."
    Boekel C., Dass S., Wilsch-Braeuninger M., Roth S.
    Development 133:459-470(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CNI.

Entry informationi

Entry nameiGRK_DROME
AccessioniPrimary (citable) accession number: P42287
Secondary accession number(s): Q9VLL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 17, 2003
Last modified: May 11, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.