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GOE_DROME
ID   GOE_DROME               Reviewed;         879 AA.
AC   Q9XZ14;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Protein gone early {ECO:0000312|FlyBase:FBgn0027528};
GN   Name=goe {ECO:0000312|FlyBase:FBgn0027528};
GN   ORFNames=CG9634 {ECO:0000312|FlyBase:FBgn0027528};
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 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:AAD34757.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAD34757.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAD34757.1};
RX   PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA   Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA   Harvey D.A.;
RT   "A Drosophila complementary DNA resource.";
RL   Science 287:2222-2224(2000).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=25420147; DOI=10.1371/journal.pone.0113423;
RA   Matsuoka S., Gupta S., Suzuki E., Hiromi Y., Asaoka M.;
RT   "gone early, a novel germline factor, ensures the proper size of the stem
RT   cell precursor pool in the Drosophila ovary.";
RL   PLoS ONE 9:E113423-E113423(2014).
CC   -!- FUNCTION: Plays a role in the ovary in limiting the number of
CC       primordial germ cells (PGCs) that develop directly into gametes,
CC       allowing them instead to enter the developmental pathway that produces
CC       germline stem cells (GSCs) from PGCs and ensuring lifelong production
CC       of gametes from these GSCs. Negatively regulates epidermal growth
CC       factor receptor (Egfr) signaling. Probably down-regulates EGFR
CC       signaling on intermingled cells, a type of somatic stromal cell which
CC       contacts PGCs, and the resultant low level of signaling limits the
CC       proportion of PGCs which start gametogenesis, maintaining them in an
CC       undifferentiated proliferative state. {ECO:0000269|PubMed:25420147}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25420147};
CC       Single-pass type II membrane protein {ECO:0000255}. Note=Not uniformly
CC       present at the cell membrane but is concentrated at the interface
CC       between germ cells. {ECO:0000269|PubMed:25420147}.
CC   -!- TISSUE SPECIFICITY: In late third larval instar ovaries, detected in
CC       germ cells but not in somatic intermingled cells and is expressed
CC       uniformly in the wing disk. In the embryo, expressed in the ventral
CC       midline, tracheal placodes, and cells forming the anterior-most row in
CC       each segment. {ECO:0000269|PubMed:25420147}.
CC   -!- DEVELOPMENTAL STAGE: In the larva, becomes detectable at the late
CC       second larval instar stage and continues to be expressed throughout the
CC       larval period. {ECO:0000269|PubMed:25420147}.
CC   -!- DISRUPTION PHENOTYPE: Increase in the number of differentiating germ
CC       cells. {ECO:0000269|PubMed:25420147}.
CC   -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01233, ECO:0000305}.
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DR   EMBL; AE014298; AAF48659.1; -; Genomic_DNA.
DR   EMBL; AE014298; AHN59820.1; -; Genomic_DNA.
DR   EMBL; AF132169; AAD34757.1; -; mRNA.
DR   RefSeq; NP_001285350.1; NM_001298421.1.
DR   RefSeq; NP_573160.1; NM_132932.3.
DR   AlphaFoldDB; Q9XZ14; -.
DR   SMR; Q9XZ14; -.
DR   IntAct; Q9XZ14; 1.
DR   STRING; 7227.FBpp0074133; -.
DR   GlyGen; Q9XZ14; 4 sites.
DR   PaxDb; Q9XZ14; -.
DR   EnsemblMetazoa; FBtr0074359; FBpp0074133; FBgn0027528.
DR   EnsemblMetazoa; FBtr0343364; FBpp0310021; FBgn0027528.
DR   GeneID; 32660; -.
DR   KEGG; dme:Dmel_CG9634; -.
DR   UCSC; CG9634-RA; d. melanogaster.
DR   CTD; 32660; -.
DR   FlyBase; FBgn0027528; goe.
DR   VEuPathDB; VectorBase:FBgn0027528; -.
DR   eggNOG; KOG3624; Eukaryota.
DR   GeneTree; ENSGT00940000164877; -.
DR   InParanoid; Q9XZ14; -.
DR   OrthoDB; 198642at2759; -.
DR   PhylomeDB; Q9XZ14; -.
DR   Reactome; R-DME-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 32660; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 32660; -.
DR   PRO; PR:Q9XZ14; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0027528; Expressed in capitellum (Drosophila) and 33 other tissues.
DR   ExpressionAtlas; Q9XZ14; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   Gene3D; 1.10.1380.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR042089; Peptidase_M13_dom_2.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733; PTHR11733; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PROSITE; PS51885; NEPRILYSIN; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Differentiation; Disulfide bond; Glycoprotein; Membrane;
KW   Oogenesis; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..879
FT                   /note="Protein gone early"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000437210"
FT   TOPO_DOM        1..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        128..148
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..879
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          162..878
FT                   /note="Peptidase M13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        539
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        701
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        853
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        163..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        186..868
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        194..826
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        254..504
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT   DISULFID        732..875
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
SQ   SEQUENCE   879 AA;  100068 MW;  5D06C9000BF5BB48 CRC64;
     MAINQGKYKP SICAIDEVDD RSFKLHNSQD EIGGKQQLQQ IEGSETAPLT TNQQKLHMDD
     GSHLTPKDLE AARQDALNEV AAGGAGGRTP AAITPNSTHP SANGLRALLL PGRRSFDALM
     SLSRKRRILY VTTACLCALL LLIIILLLAF WPEVPFYLRA PLCLDKECVE SSRQLLLWAN
     TSKSPCHETY EWACGNFASD YANHEYFVIK RGEWNYETYN EYQELNELNR FIAMLPNSQE
     GSVESTVSSL YRSCRETDVL DKSQSDLLLK RAINAVYGWQ AFRDSNRLQS WEYKRVLVVL
     QAKHGIFPYY RVTVENGFSN PHDYVITLDE GELGLPDKYF YGNDADEEVV RGYKLLLRDF
     AINMGIVSRE ADLFADDIFH YERRIVNHIE DAKADANRPI NKLMRLADLK IKAPSLPILE
     SLQAIFPKTK ITEDTEVLVR DPEVMHALSV LLSTSDKKPI NNFIVWSLAR KMLPHLSKEY
     RTLAETFDHA LYGRTASYPR WLICSKVVRD WLPFAVDALQ QQPPRQQFET MTSKSRGLNK
     TQGNEELLKL MFFSLRNQLK DSLEQAKWLE PAARQFIQKK LNEMRLQFGI PDEVLQQPTY
     LAQYYNELIL NNVFFVEHLE WIWTFRRSQM EKKLGPLAIL DVIVSEMYTR DNPQAIAYSN
     KLNMLLVSKV LISSNYYDYR YPVAVNFARI GTDILEALID NFSTFLLQFN TQSTDISDAA
     PEIRYAQPDV NCLAAGQPPR LVHELNELSS NALKSFHVTL SAARTAARAL SNFVNAIDAG
     SAIQGSGIDQ ANTYEALGLT RRLRIPGLRS FNENELFTLS YMQQHCSTTI ADKDYARIKP
     LVESQLAESY LFNATWQHIQ FLPRSTNCAA AEATCSNLL
 
 
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