SRGP2_MOUSE
ID SRGP2_MOUSE Reviewed; 1071 AA.
AC Q91Z67; B2RY13; Q3V1V8; Q61054;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=SLIT-ROBO Rho GTPase-activating protein 2 {ECO:0000303|PubMed:11672528};
DE Short=srGAP2 {ECO:0000303|PubMed:11672528};
DE AltName: Full=Formin-binding protein 2;
DE AltName: Full=Formin-binding protein 27 {ECO:0000303|PubMed:8605874};
DE Short=FBP-27 {ECO:0000303|PubMed:8605874};
GN Name=Srgap2 {ECO:0000303|PubMed:11672528, ECO:0000312|MGI:MGI:109605};
GN Synonyms=Fbp27 {ECO:0000303|PubMed:8605874}, Fnbp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 432-836.
RX PubMed=11672528; DOI=10.1016/s0092-8674(01)00530-x;
RA Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H., Wen L.,
RA Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.;
RT "Signal transduction in neuronal migration: roles of GTPase activating
RT proteins and the small GTPase Cdc42 in the Slit-Robo pathway.";
RL Cell 107:209-221(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1071.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 732-782.
RC STRAIN=FVB/NJ;
RX PubMed=8605874; DOI=10.1002/j.1460-2075.1996.tb00442.x;
RA Chan D.C., Bedford M.T., Leder P.;
RT "Formin binding proteins bear WWP/WW domains that bind proline-rich
RT peptides and functionally resemble SH3 domains.";
RL EMBO J. 15:1045-1054(1996).
RN [6]
RP FUNCTION IN NEURON MIGRATION AND MORPHOGENESIS, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, SUBUNIT, INTERACTION WITH RAC1, AND MUTAGENESIS OF
RP ARG-527 AND TRP-765.
RX PubMed=19737524; DOI=10.1016/j.cell.2009.06.047;
RA Guerrier S., Coutinho-Budd J., Sassa T., Gresset A., Jordan N.V., Chen K.,
RA Jin W.L., Frost A., Polleux F.;
RT "The F-BAR domain of srGAP2 induces membrane protrusions required for
RT neuronal migration and morphogenesis.";
RL Cell 138:990-1004(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500; SER-695 AND SER-990, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH FMNL1; FMNL3 AND ROBO2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21148482; DOI=10.1074/jbc.m110.190397;
RA Mason F.M., Heimsath E.G., Higgs H.N., Soderling S.H.;
RT "Bi-modal regulation of a formin by srGAP2.";
RL J. Biol. Chem. 286:6577-6586(2011).
RN [9]
RP INTERACTION WITH GPHN.
RX PubMed=22126966; DOI=10.1126/scisignal.2002189;
RA Okada H., Uezu A., Mason F.M., Soderblom E.J., Moseley M.A. III,
RA Soderling S.H.;
RT "SH3 domain-based phototrapping in living cells reveals Rho family GAP
RT signaling complexes.";
RL Sci. Signal. 4:RS13-RS13(2011).
RN [10]
RP FUNCTION IN DENDRITIC SPINE MATURATION, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22559944; DOI=10.1016/j.cell.2012.03.034;
RA Charrier C., Joshi K., Coutinho-Budd J., Kim J.E., Lambert N.,
RA de Marchena J., Jin W.L., Vanderhaeghen P., Ghosh A., Sassa T., Polleux F.;
RT "Inhibition of SRGAP2 function by its human-specific paralogs induces
RT neoteny during spine maturation.";
RL Cell 149:923-935(2012).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GPHN AND HOMER1, AND
RP MUTAGENESIS OF 340-PRO--PHE-343 AND TRP-765.
RX PubMed=27373832; DOI=10.1016/j.neuron.2016.06.013;
RA Fossati M., Pizzarelli R., Schmidt E.R., Kupferman J.V., Stroebel D.,
RA Polleux F., Charrier C.;
RT "SRGAP2 and its human-specific paralog co-regulate the development of
RT excitatory and inhibitory synapses.";
RL Neuron 91:356-369(2016).
RN [12]
RP FUNCTION.
RX PubMed=26439400; DOI=10.1016/j.devcel.2015.09.002;
RA Fritz R.D., Menshykau D., Martin K., Reimann A., Pontelli V., Pertz O.;
RT "SrGAP2-dependent integration of membrane geometry and Slit-Robo-repulsive
RT cues regulates fibroblast contact inhibition of locomotion.";
RL Dev. Cell 35:78-92(2015).
CC -!- FUNCTION: Postsynaptic RAC1 GTPase activating protein (GAP) that plays
CC a key role in neuronal morphogenesis and migration mainly during
CC development of the cerebral cortex (PubMed:19737524, PubMed:22559944,
CC PubMed:27373832). Regulates excitatory and inhibitory synapse
CC maturation and density in cortical pyramidal neurons (PubMed:19737524,
CC PubMed:22559944, PubMed:27373832). SRGAP2/SRGAP2A limits excitatory and
CC inhibitory synapse density through its RAC1-specific GTPase activating
CC activity, while it promotes maturation of both excitatory and
CC inhibitory synapses through its ability to bind to the postsynaptic
CC scaffolding protein HOMER1 at excitatory synapses, and the postsynaptic
CC protein GPHN at inhibitory synapses (PubMed:27373832). Mechanistically,
CC acts by binding and deforming membranes, thereby regulating actin
CC dynamics to regulate cell migration and differentiation
CC (PubMed:19737524, PubMed:22559944, PubMed:26439400). Promotes cell
CC repulsion and contact inhibition of locomotion: localizes to
CC protrusions with curved edges and controls the duration of RAC1
CC activity in contact protrusions (PubMed:26439400). In non-neuronal
CC cells, may also play a role in cell migration by regulating the
CC formation of lamellipodia and filopodia (PubMed:22559944).
CC {ECO:0000269|PubMed:19737524, ECO:0000269|PubMed:22559944,
CC ECO:0000269|PubMed:26439400, ECO:0000269|PubMed:27373832}.
CC -!- SUBUNIT: Homodimer (PubMed:19737524). Forms a heterooligomer with
CC SRGAP1 and SRGAP3 through its F-BAR domain (By similarity). Interacts
CC (via SH3 domain) with GPHN (PubMed:22126966, PubMed:27373832).
CC Interacts (via SH3 domain) with FMNL1 (activated by RAC1); regulates
CC the actin filament severing activity of FMNL1 and actin dynamics
CC (PubMed:21148482). Interacts (via SH3 domain) with FMNL3
CC (PubMed:21148482). Interacts with RAC1; specifically stimulates RAC1
CC GTPase activity (PubMed:19737524). Interacts (via F-BAR domain) with
CC HOMER1 (PubMed:27373832). Interacts with ROBO1 and ROBO2
CC (PubMed:21148482). Interacts with FASLG (By similarity). Interacts with
CC PRMT5 (By similarity). {ECO:0000250|UniProtKB:O75044,
CC ECO:0000269|PubMed:19737524, ECO:0000269|PubMed:21148482,
CC ECO:0000269|PubMed:22126966, ECO:0000269|PubMed:27373832}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19737524}. Cell
CC projection, dendritic spine {ECO:0000269|PubMed:27373832}. Postsynaptic
CC density {ECO:0000269|PubMed:22559944}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:22559944}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:O75044}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:21148482}. Nucleus {ECO:0000250|UniProtKB:D4A208}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:21148482}. Note=Recruited to
CC actin-rich phagosomes during phagocytosis (PubMed:21148482).
CC Translocates from nucleus to cytoplasm during development (By
CC similarity). {ECO:0000250|UniProtKB:D4A208,
CC ECO:0000269|PubMed:21148482}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout cortical development
CC culminating at P1. Expression is reduced but still present in the adult
CC cortex. Expressed in the cortical wall both in neuronal progenitors in
CC the ventricular zone and post-mitotic neurons in the cortical plate (at
CC protein level). {ECO:0000269|PubMed:19737524}.
CC -!- DOMAIN: The F-BAR domain mediates oligomerization, binds membranes, and
CC induces plasma membrane protrusions. {ECO:0000250|UniProtKB:O75044}.
CC -!- PTM: Methylation at Arg-927 is required for the stimulation of cell
CC migration, dimerization and localization at the plasma membrane
CC protrusions. {ECO:0000250|UniProtKB:O75044}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and show no abnormality of
CC cortical lamination. However, a delay in dendritic spine maturation
CC coupled to an increase in spine neck and spine density is observed.
CC {ECO:0000269|PubMed:22559944}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Branching out - Issue 143 of
CC October 2012;
CC URL="https://web.expasy.org/spotlight/back_issues/143";
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DR EMBL; AC109299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151081; AAI51082.1; -; mRNA.
DR EMBL; BC151082; AAI51083.1; -; mRNA.
DR EMBL; BC158055; AAI58056.1; -; mRNA.
DR EMBL; BC172152; AAI72152.1; -; mRNA.
DR EMBL; AY057900; AAL27032.1; -; mRNA.
DR EMBL; AK132220; BAE21041.1; -; mRNA.
DR EMBL; U40752; AAC52480.1; -; mRNA.
DR CCDS; CCDS48355.1; -.
DR PIR; S64712; S64712.
DR RefSeq; NP_001074480.2; NM_001081011.2.
DR RefSeq; XP_006529197.1; XM_006529134.3.
DR AlphaFoldDB; Q91Z67; -.
DR SMR; Q91Z67; -.
DR BioGRID; 199721; 48.
DR IntAct; Q91Z67; 5.
DR MINT; Q91Z67; -.
DR STRING; 10090.ENSMUSP00000095195; -.
DR iPTMnet; Q91Z67; -.
DR PhosphoSitePlus; Q91Z67; -.
DR EPD; Q91Z67; -.
DR jPOST; Q91Z67; -.
DR MaxQB; Q91Z67; -.
DR PaxDb; Q91Z67; -.
DR PeptideAtlas; Q91Z67; -.
DR PRIDE; Q91Z67; -.
DR ProteomicsDB; 263343; -.
DR DNASU; 14270; -.
DR Ensembl; ENSMUST00000097588; ENSMUSP00000095195; ENSMUSG00000026425.
DR GeneID; 14270; -.
DR KEGG; mmu:14270; -.
DR UCSC; uc007cng.2; mouse.
DR CTD; 23380; -.
DR MGI; MGI:109605; Srgap2.
DR VEuPathDB; HostDB:ENSMUSG00000026425; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000182824; -.
DR InParanoid; Q91Z67; -.
DR OMA; EDFCDSP; -.
DR OrthoDB; 1245523at2759; -.
DR PhylomeDB; Q91Z67; -.
DR TreeFam; TF315892; -.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 14270; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Srgap2; mouse.
DR PRO; PR:Q91Z67; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91Z67; protein.
DR Bgee; ENSMUSG00000026425; Expressed in embryonic brain and 257 other tissues.
DR ExpressionAtlas; Q91Z67; baseline and differential.
DR Genevisible; Q91Z67; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0044327; C:dendritic spine head; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; ISS:UniProtKB.
DR GO; GO:0060996; P:dendritic spine development; IMP:UniProtKB.
DR GO; GO:1904861; P:excitatory synapse assembly; IMP:UniProtKB.
DR GO; GO:0021816; P:extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration; IMP:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; IDA:UniProtKB.
DR GO; GO:1904862; P:inhibitory synapse assembly; IMP:UniProtKB.
DR GO; GO:0003363; P:lamellipodium assembly involved in ameboidal cell migration; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR CDD; cd11955; SH3_srGAP1-3; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035648; srGAP1/2/3_SH3.
DR InterPro; IPR030252; srGAP2.
DR PANTHER; PTHR14166:SF6; PTHR14166:SF6; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; GTPase activation; Membrane; Methylation;
KW Neurogenesis; Nucleus; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; SH3 domain; Synapse.
FT CHAIN 1..1071
FT /note="SLIT-ROBO Rho GTPase-activating protein 2"
FT /id="PRO_0000056768"
FT DOMAIN 22..325
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 489..679
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 728..787
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 181..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..401
FT /evidence="ECO:0000255"
FT COILED 940..968
FT /evidence="ECO:0000255"
FT COMPBIAS 181..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A208"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A208"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A208"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75044"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75044"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75044"
FT MOD_RES 927
FT /note="Symmetric dimethylarginine; by PRMT5"
FT /evidence="ECO:0000250|UniProtKB:O75044"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75044"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 994
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75044"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75044"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75044"
FT MUTAGEN 340..343
FT /note="PMKF->LMKC: Abolished interaction with HOMER1."
FT /evidence="ECO:0000269|PubMed:27373832"
FT MUTAGEN 527
FT /note="R->L: Abolished RAC1 GTPase activity. Abolished
FT ability to induce neurite branching. No effect on filopodia
FT biogenesis and neurite outgrowth."
FT /evidence="ECO:0000269|PubMed:19737524,
FT ECO:0000269|PubMed:27373832"
FT MUTAGEN 765
FT /note="W->A: Loss of the ability to induce filopodia and to
FT initiate neurite outgrowht. Abolished interaction with
FT GPHN."
FT /evidence="ECO:0000269|PubMed:19737524,
FT ECO:0000269|PubMed:27373832"
FT CONFLICT 598
FT /note="A -> V (in Ref. 3; AAL27032)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="T -> S (in Ref. 3; AAL27032)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="A -> S (in Ref. 3; AAL27032)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="F -> C (in Ref. 3; AAL27032)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="W -> L (in Ref. 3; AAL27032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1071 AA; 120798 MW; 9093C63476BA605D CRC64;
MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ DFFRKKAEIE
MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN LLLNQVKRES RDHTTLSDIY
LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ DDLMKVLNEL YSVMKTYHMY NADSISAQSK
LKEAEKQEEK QIGKSVKQED RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT
ENKLKAIKAR NEYLLALEAT NASVFKYYIH DLSDIIDQCC DLGYHASLNR ALRTFLSAEL
NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG DMASQLCAQQ
PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD IVTVEDFDVS DCFQYSNSME
SVKSTVSETF MSKPSIAKRR ANQQETEQFY FTKMKEYLEG RNLITKLQAK HDLLQKTLGE
SQRTDCSLAR RSSTVRKQDS SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN
AFERGEDPLA GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLIACVT MDNLQERAVH
IRKVLLVLPK PTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS VPEGHDQVSC
QAHVNELIKT IIIQHENIFP NPRELEGPIY SRGGSMEDYC DSTHGETTSA EDSTQDVTAE
HHTSDDECEP IEAIAKFDYV GRTARELSFK KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ
YIVVQDTEDG VVERSSPKSE IEVMSEPPEE KVTARTGASC PSGGHVADIY LANINKQRKR
PESGSIRKAF RSDSHGLGSS LTDSSSLGVG ASCRPSSQPI MSQNLPKEGP DKCSISGHGS
LNSISRHSSL KNRMDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM NSALNELQEL
ERQSSAKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL LKDPEPAFQR SASTAGDIAC
AFRPVKSVKM AAPVKPPATR PKPTVFPKTN ATSPGVNSSA SPQATDKSCT V
