FOG_DROME
ID FOG_DROME Reviewed; 730 AA.
AC P40795; Q9VR71;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein folded gastrulation;
DE Contains:
DE RecName: Full=Protein folded gastrulation;
DE Contains:
DE RecName: Full=G protein-coupled receptor ligand;
DE Flags: Precursor;
GN Name=fog; ORFNames=CG9559;
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, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RX PubMed=8137424; DOI=10.1016/0092-8674(94)90384-0;
RA Costa M., Wilson E.T., Wieschaus E.;
RT "A putative cell signal encoded by the folded gastrulation gene coordinates
RT cell shape changes during Drosophila gastrulation.";
RL Cell 76:1075-1089(1994).
RN [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 [3]
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 [4]
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).
CC -!- FUNCTION: Coordinates cell shape changes during formation of the
CC ventral furrow and invagination of the posterior midgut primordium, by
CC inducing apical constriction of cells in spatially and temporally
CC defined manners. Could function as a secreted signal to initiate apical
CC constriction by acting as a ligand for an unidentified G protein-
CC coupled receptor, which in turn activates the G protein alpha subunit
CC encoded by concertina, in neighboring cells. Such an intracellular
CC pathway would ultimately induce contraction of the apical actin-myosin
CC network. In the ventral furrow, fog appears to ensure that all the
CC cells initiate constriction within several minutes of each other. In
CC the posterior midgut invagination, fog appears to direct the ordered
CC progression of constriction initiations out from a central region and
CC also to delimit the peripheral extent of this spreading.
CC {ECO:0000269|PubMed:8137424}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the invagination primordia in a
CC pattern that precisely precedes the pattern of constrictions.
CC {ECO:0000269|PubMed:8137424}.
CC -!- DEVELOPMENTAL STAGE: Maternal transcripts are deposited into the egg
CC and uniformly distributed throughout the cortex of cleavage stage and
CC syncytial blastoderm embryos. Zygotic transcription is first found in
CC the ventral furrow primordium during the beginning of cellularization,
CC about 30 min before the start of constrictions also expressed about 30
CC min before the start of constrictions in the posterior midgut
CC primordium. The ventral-most cells are last to express fog.
CC {ECO:0000269|PubMed:8137424}.
CC -!- INDUCTION: Controlled by zygotic patterning genes.
CC {ECO:0000269|PubMed:8137424}.
CC -!- PTM: May be highly O-glycosylated in its Ser/Thr-rich C-terminal part.
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DR EMBL; U03717; AAA18955.1; -; mRNA.
DR EMBL; AE014298; AAF50935.1; -; Genomic_DNA.
DR EMBL; AY095205; AAM12298.1; -; mRNA.
DR PIR; A53064; A53064.
DR RefSeq; NP_001033860.1; NM_001038771.3.
DR RefSeq; NP_001259781.1; NM_001272852.1.
DR RefSeq; NP_001259782.1; NM_001272853.2.
DR RefSeq; NP_001259783.1; NM_001272854.1.
DR RefSeq; NP_001259784.1; NM_001272855.2.
DR RefSeq; NP_523438.1; NM_078714.6.
DR AlphaFoldDB; P40795; -.
DR BioGRID; 59419; 13.
DR IntAct; P40795; 1.
DR STRING; 7227.FBpp0305384; -.
DR GlyGen; P40795; 8 sites.
DR PaxDb; P40795; -.
DR DNASU; 33148; -.
DR EnsemblMetazoa; FBtr0077342; FBpp0077034; FBgn0000719.
DR EnsemblMetazoa; FBtr0100538; FBpp0099983; FBgn0000719.
DR EnsemblMetazoa; FBtr0333179; FBpp0305381; FBgn0000719.
DR EnsemblMetazoa; FBtr0333180; FBpp0305382; FBgn0000719.
DR EnsemblMetazoa; FBtr0333181; FBpp0305383; FBgn0000719.
DR EnsemblMetazoa; FBtr0333182; FBpp0305384; FBgn0000719.
DR GeneID; 33148; -.
DR KEGG; dme:Dmel_CG9559; -.
DR CTD; 33148; -.
DR FlyBase; FBgn0000719; fog.
DR VEuPathDB; VectorBase:FBgn0000719; -.
DR eggNOG; ENOG502S1G9; Eukaryota.
DR HOGENOM; CLU_373096_0_0_1; -.
DR InParanoid; P40795; -.
DR OMA; TPFWWLP; -.
DR OrthoDB; 815660at2759; -.
DR PhylomeDB; P40795; -.
DR BioGRID-ORCS; 33148; 0 hits in 1 CRISPR screen.
DR ChiTaRS; fog; fly.
DR GenomeRNAi; 33148; -.
DR PRO; PR:P40795; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000719; Expressed in embryonic/larval hemocyte (Drosophila) and 32 other tissues.
DR ExpressionAtlas; P40795; baseline and differential.
DR Genevisible; P40795; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IDA:FlyBase.
DR GO; GO:0070252; P:actin-mediated cell contraction; IDA:FlyBase.
DR GO; GO:0003383; P:apical constriction; IMP:FlyBase.
DR GO; GO:0003384; P:apical constriction involved in gastrulation; IMP:FlyBase.
DR GO; GO:0110072; P:apical constriction involved in ventral furrow formation; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0021782; P:glial cell development; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0048383; P:mesectoderm development; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; TAS:FlyBase.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; IMP:FlyBase.
DR GO; GO:0000266; P:mitochondrial fission; IMP:FlyBase.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0007374; P:posterior midgut invagination; IMP:FlyBase.
DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; IMP:FlyBase.
DR GO; GO:0043519; P:regulation of myosin II filament organization; IMP:FlyBase.
DR GO; GO:0060662; P:salivary gland cavitation; IMP:FlyBase.
DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR InterPro; IPR031761; FOG_N.
DR Pfam; PF15888; FOG_N; 1.
PE 2: Evidence at transcript level;
KW Cell shape; Developmental protein; Extracellular matrix; Gastrulation;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..730
FT /note="Protein folded gastrulation"
FT /id="PRO_0000021283"
FT CHAIN 57..167
FT /note="G protein-coupled receptor ligand"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021284"
FT REGION 197..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..382
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 730 AA; 78251 MW; D00D426139AB987C CRC64;
MSPPNCLLAV LALTVFIGAN NALPITSRPI EGNVQRMVWE DWVNLDPEQR NLTKEKKITA
KSIFTLPFRH CPQGHTLFNQ LCIPQSNIDP TDLVKQELIL AGGSNGSPPP PPIGDYDYGD
DEESEEIVYD LSVIPTAMQD GLPPSVGTGD QALPSEDAPL KFNIFEKKFP TGTGEHEEMP
LPPDMAAATY AKNISTTPET STSITPTSTT TFAVPSVPSG EASNRIPGGV DLLAAPSDAF
STSTTLSMPT SNTTTTSNKD IGQVESIVLP ADQEHDGLVH LVTSSLSDND SDDSSTTLNG
FNAEADLAQL LKVDAFWPVY DGSIELLPPL FSHRKVAPPL SADQDVKTKH AVDAAEKVGA
ELEEEVGEEE VTATDILPSE EDEYTTETAT TTGDTTVAEA SMDTSTATST SGQSSPHPPE
EPEIDERENR LVLIKSKVQP VQLTTTTSAT ATTAADVANS SSSTDRFHYQ HFVEDESSTT
TATPEPSSST PGDPIEQSDM PASDNDNLMT NTIGGRGDDD DDGGHKATSE IHVQQELRLI
NELVKGKQRQ QHQPQKQQLE PTSTEITSAL TSTSTEDATT TTTTTTAYTN WSKVMPQLGQ
STSETAATTE TVATSGQVNE ISLTATSAST EVKHFSITNR SYRNSKIIRE DRLTVEPEGI
VESAASTESA GTAATTPNSS SNPDGYTPLW WLPSIGWRLD RHLDGNGEDQ SLLLRFFSTF
RGSNTAATTR
