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Ras-like protein 3 (Protein roughened)

 RAP1_DROME              Reviewed;         184 AA.
P08645; Q2XYB6; Q540V3; Q9V3N0;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 2.
12-SEP-2018, entry version 192.
RecName: Full=Ras-related protein Rap1 {ECO:0000312|FlyBase:FBgn0004636};
AltName: Full=Rap1 GTPase {ECO:0000312|FlyBase:FBgn0004636};
AltName: Full=Ras-like protein 3 {ECO:0000303|PubMed:3926484};
Flags: Precursor;
Name=Rap1 {ECO:0000312|FlyBase:FBgn0004636};
Synonyms=R {ECO:0000312|FlyBase:FBgn0004636},
RAP {ECO:0000303|PubMed:1934069}, ras3 {ECO:0000303|PubMed:3926484};
ORFNames=CG1956 {ECO:0000312|FlyBase:FBgn0004636};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3926484;
Schejter E.D., Shilo B.-Z.;
"Characterization of functional domains of p21 ras by use of chimeric
genes.";
EMBO J. 4:407-412(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=1934069; DOI=10.1016/0092-8674(91)90066-8;
Hariharan I.K., Carthew R.W., Rubin G.M.;
"The Drosophila roughened mutation: activation of a rap homolog
disrupts eye development and interferes with cell determination.";
Cell 67:717-722(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=A1;
PubMed=10552039; DOI=10.1007/PL00006579;
Gasperini R., Gibson G.;
"Absence of protein polymorphism in the Ras genes of Drosophila
melanogaster.";
J. Mol. Evol. 49:583-590(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-178.
STRAIN=Ral1;
PubMed=16120803; DOI=10.1093/molbev/msi246;
Comeron J.M., Guthrie T.B.;
"Intragenic Hill-Robertson interference influences selection intensity
on synonymous mutations in Drosophila.";
Mol. Biol. Evol. 22:2519-2530(2005).
-!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
activity. Plays a role in photoreceptor cell determination.
{ECO:0000269|PubMed:1934069}.
-!- ACTIVITY REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by a guanine
nucleotide-exchange factor (GEF) and inactivated by a GTPase-
activating protein (GAP).
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Flies exhibit disruption of the early stages
of photoreceptor cell determination, adult eyes lack the R7 cell.
{ECO:0000269|PubMed:1934069}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA26131.1; Type=Frameshift; Positions=76, 96, 160, 180; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X02200; CAA26131.1; ALT_FRAME; Genomic_DNA.
EMBL; M80535; AAA28845.1; -; Genomic_DNA.
EMBL; AF186654; AAF15520.1; -; Genomic_DNA.
EMBL; AE014296; AAF47583.1; -; Genomic_DNA.
EMBL; AY121688; AAM52015.1; -; mRNA.
EMBL; DQ138746; ABA86352.1; -; Genomic_DNA.
PIR; A41217; A41217.
PIR; S07187; TVFFR3.
RefSeq; NP_001189023.1; NM_001202094.2.
RefSeq; NP_001261295.1; NM_001274366.1.
RefSeq; NP_476857.1; NM_057509.5.
UniGene; Dm.822; -.
ProteinModelPortal; P08645; -.
SMR; P08645; -.
BioGrid; 63773; 47.
IntAct; P08645; 1.
STRING; 7227.FBpp0072746; -.
PaxDb; P08645; -.
PRIDE; P08645; -.
EnsemblMetazoa; FBtr0072867; FBpp0072746; FBgn0004636.
EnsemblMetazoa; FBtr0303154; FBpp0292253; FBgn0004636.
EnsemblMetazoa; FBtr0332671; FBpp0304917; FBgn0004636.
GeneID; 38244; -.
KEGG; dme:Dmel_CG1956; -.
CTD; 38244; -.
FlyBase; FBgn0004636; Rap1.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00860000133678; -.
InParanoid; P08645; -.
KO; K04353; -.
OMA; QINRQMP; -.
OrthoDB; EOG091G0OOG; -.
PhylomeDB; P08645; -.
Reactome; R-DME-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-DME-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-DME-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-DME-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-DME-392517; Rap1 signalling.
Reactome; R-DME-6798695; Neutrophil degranulation.
Reactome; R-DME-8875555; MET activates RAP1 and RAC1.
ChiTaRS; r; fly.
GenomeRNAi; 38244; -.
PRO; PR:P08645; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0004636; Expressed in 33 organ(s), highest expression level in embryonic/larval hemocyte (Drosophila).
ExpressionAtlas; P08645; baseline and differential.
Genevisible; P08645; DM.
GO; GO:0031252; C:cell leading edge; IDA:FlyBase.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
GO; GO:0034333; P:adherens junction assembly; IGI:FlyBase.
GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
GO; GO:0030718; P:germ-line stem cell population maintenance; IGI:FlyBase.
GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
GO; GO:0030713; P:ovarian follicle cell stalk formation; TAS:FlyBase.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:FlyBase.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:FlyBase.
GO; GO:0045874; P:positive regulation of sevenless signaling pathway; IGI:FlyBase.
GO; GO:0007465; P:R7 cell fate commitment; IMP:FlyBase.
GO; GO:0032486; P:Rap protein signal transduction; IDA:FlyBase.
GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IMP:FlyBase.
GO; GO:0008293; P:torso signaling pathway; IMP:FlyBase.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
CDD; cd04175; Rap1; 1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038851; Rap1.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; GTP-binding; Lipoprotein; Membrane;
Methylation; Nucleotide-binding; Prenylation; Reference proteome;
Sensory transduction; Vision.
CHAIN 1 181 Ras-related protein Rap1.
/FTId=PRO_0000030191.
PROPEP 182 184 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000030192.
NP_BIND 10 17 GTP. {ECO:0000250}.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 116 119 GTP. {ECO:0000250}.
MOTIF 32 40 Effector region.
MOD_RES 181 181 Cysteine methyl ester. {ECO:0000250}.
LIPID 181 181 S-geranylgeranyl cysteine. {ECO:0000250}.
VARIANT 157 157 F -> L (in roughened mutants).
CONFLICT 45 49 EVDGQ -> KVNER (in Ref. 1; CAA26131).
{ECO:0000305}.
CONFLICT 56 57 LD -> VN (in Ref. 1; CAA26131).
{ECO:0000305}.
CONFLICT 69 69 D -> N (in Ref. 1; CAA26131).
{ECO:0000305}.
SEQUENCE 184 AA; 20863 MW; 9A55889B61FEDE13 CRC64;
MREYKIVVLG SGGVGKSALT VQFVQCIFVE KYDPTIEDSY RKQVEVDGQQ CMLEILDTAG
TEQFTAMRDL YMKNGQGFVL VYSITAQSTF NDLQDLREQI LRVKDTDDVP MVLVGNKCDL
EEERVVGKEL GKNLATQFNC AFMETSAKAK VNVNDIFYDL VRQINKKSPE KKQKKPKKSL
CVLL


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