TRIO_MOUSE
ID TRIO_MOUSE Reviewed; 3102 AA.
AC Q0KL02; Q3U522; Q6P9K6; Q80W23;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Triple functional domain protein;
DE EC=2.7.11.1;
GN Name=Trio;
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 [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, MUTAGENESIS OF
RP GLN-1427 AND LEU-1435, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16943433; DOI=10.1128/mcb.02474-05;
RA Sun Y.-J., Nishikawa K., Yuda K., Wang Y.-L., Osaka H., Fukazawa N.,
RA Naito A., Wada K., Aoki S.;
RT "Solo/Trio8, a membrane-associated short isoform of Trio, modulates
RT endosome dynamics and neurite elongation.";
RL Mol. Cell. Biol. 26:6923-6935(2006).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2062-3102 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1145-3102 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2521-3102 (ISOFORM 4).
RC STRAIN=NOD; TISSUE=Thymus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2458, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1627; SER-2282; SER-2458 AND
RP SER-2462, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=22155786; DOI=10.1126/scisignal.2002060;
RA Deinhardt K., Kim T., Spellman D.S., Mains R.E., Eipper B.A., Neubert T.A.,
RA Chao M.V., Hempstead B.L.;
RT "Neuronal growth cone retraction relies on proneurotrophin receptor
RT signaling through Rac.";
RL Sci. Signal. 4:RA82-RA82(2011).
RN [8]
RP FUNCTION.
RX PubMed=22666460; DOI=10.1371/journal.pone.0038130;
RA Liu X.F., Bera T.K., Kahue C., Escobar T., Fei Z., Raciti G.A., Pastan I.;
RT "ANKRD26 and its interacting partners TRIO, GPS2, HMMR and DIPA regulate
RT adipogenesis in 3T3-L1 cells.";
RL PLoS ONE 7:E38130-E38130(2012).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RHOA and RAC1
CC GTPases. Involved in coordinating actin remodeling, which is necessary
CC for cell migration and growth (By similarity). Plays a key role in the
CC regulation of neurite outgrowth and lamellipodia formation (By
CC similarity). In developing hippocampal neurons, limits dendrite
CC formation, without affecting the establishment of axon polarity. Once
CC dendrites are formed, involved in the control of synaptic function by
CC regulating the endocytosis of AMPA-selective glutamate receptors
CC (AMPARs) at CA1 excitatory synapses (By similarity). May act as a
CC regulator of adipogenesis (PubMed:22666460).
CC {ECO:0000250|UniProtKB:F1M0Z1, ECO:0000250|UniProtKB:O75962,
CC ECO:0000269|PubMed:22666460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with CARMIL1. Interacts with PTPRF/LAR. Interacts
CC with ANKRD26 (By similarity). Interacts with Bassoon/BSN and
CC Piccolo/PCLO (By similarity). Interacts with the cytoplasmic region of
CC the heterodimer formed by NGFR and SORCS2. ProNGF binding mediates
CC dissociation of TRIO from the receptor complex (By similarity).
CC {ECO:0000250|UniProtKB:F1M0Z1, ECO:0000250|UniProtKB:O75962}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16943433}. Cell
CC projection {ECO:0000269|PubMed:16141072}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Early endosome
CC {ECO:0000269|PubMed:16943433}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q0KL02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0KL02-2; Sequence=VSP_023308, VSP_023309;
CC Name=3;
CC IsoId=Q0KL02-3; Sequence=VSP_037863, VSP_037864, VSP_037865;
CC Name=4;
CC IsoId=Q0KL02-4; Sequence=VSP_037863;
CC -!- TISSUE SPECIFICITY: Widespread in the brain, with more intense signals
CC in the hippocampus, olfactory bulb, cortical layers and cerebellum.
CC Isoform 2 is predominantly expressed in Purkinje neurons of brain.
CC {ECO:0000269|PubMed:16943433}.
CC -!- DOMAIN: The N-terminal DBL/GEF domain specifically catalyzes nucleotide
CC exchange for RAC1, leading to the activation of Jun kinase and the
CC production of membrane ruffles. The second DBL/GEF domain is an
CC exchange factor for rhoa and induces the formation of stress fibers (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32258.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB106872; BAF30811.1; -; mRNA.
DR EMBL; AC107452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051169; AAH51169.1; -; mRNA.
DR EMBL; BC060724; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK153924; BAE32258.1; ALT_INIT; mRNA.
DR CCDS; CCDS49587.1; -. [Q0KL02-4]
DR RefSeq; NP_001074771.1; NM_001081302.1. [Q0KL02-4]
DR RefSeq; XP_006520117.1; XM_006520054.3. [Q0KL02-2]
DR SMR; Q0KL02; -.
DR BioGRID; 230148; 10.
DR IntAct; Q0KL02; 6.
DR MINT; Q0KL02; -.
DR STRING; 10090.ENSMUSP00000087714; -.
DR iPTMnet; Q0KL02; -.
DR PhosphoSitePlus; Q0KL02; -.
DR SwissPalm; Q0KL02; -.
DR EPD; Q0KL02; -.
DR MaxQB; Q0KL02; -.
DR PaxDb; Q0KL02; -.
DR PeptideAtlas; Q0KL02; -.
DR PRIDE; Q0KL02; -.
DR ProteomicsDB; 259098; -. [Q0KL02-1]
DR ProteomicsDB; 259099; -. [Q0KL02-2]
DR ProteomicsDB; 259100; -. [Q0KL02-3]
DR ProteomicsDB; 259101; -. [Q0KL02-4]
DR Antibodypedia; 2116; 80 antibodies from 19 providers.
DR Ensembl; ENSMUST00000090247; ENSMUSP00000087714; ENSMUSG00000022263. [Q0KL02-4]
DR GeneID; 223435; -.
DR KEGG; mmu:223435; -.
DR UCSC; uc007vjw.1; mouse. [Q0KL02-4]
DR UCSC; uc007vjx.1; mouse. [Q0KL02-3]
DR CTD; 7204; -.
DR MGI; MGI:1927230; Trio.
DR VEuPathDB; HostDB:ENSMUSG00000022263; -.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG4240; Eukaryota.
DR GeneTree; ENSGT00940000154766; -.
DR HOGENOM; CLU_000373_1_0_1; -.
DR InParanoid; Q0KL02; -.
DR OMA; HTHVKEX; -.
DR OrthoDB; 5761at2759; -.
DR PhylomeDB; Q0KL02; -.
DR TreeFam; TF318080; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-418885; DCC mediated attractive signaling.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 223435; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Trio; mouse.
DR PRO; PR:Q0KL02; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q0KL02; protein.
DR Bgee; ENSMUSG00000022263; Expressed in lateral septal nucleus and 259 other tissues.
DR ExpressionAtlas; Q0KL02; baseline and differential.
DR Genevisible; Q0KL02; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IEA:InterPro.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 6.
DR Gene3D; 1.20.900.10; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR028570; Kalirin/TRIO.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF104; PTHR22826:SF104; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00150; SPEC; 6.
DR SUPFAM; SSF48065; SSF48065; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR SUPFAM; SSF52087; SSF52087; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm;
KW Disulfide bond; Endosome; Guanine-nucleotide releasing factor;
KW Immunoglobulin domain; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; SH3 domain;
KW Transferase.
FT CHAIN 1..3102
FT /note="Triple functional domain protein"
FT /id="PRO_0000278474"
FT DOMAIN 65..210
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REPEAT 218..338
FT /note="Spectrin 1"
FT REPEAT 340..446
FT /note="Spectrin 2"
FT REPEAT 566..672
FT /note="Spectrin 3"
FT REPEAT 673..784
FT /note="Spectrin 4"
FT REPEAT 907..1012
FT /note="Spectrin 5"
FT REPEAT 1138..1244
FT /note="Spectrin 6"
FT DOMAIN 1292..1467
FT /note="DH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1479..1591
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1656..1721
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1969..2145
FT /note="DH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 2157..2271
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 2554..2619
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 2688..2778
FT /note="Ig-like C2-type"
FT DOMAIN 2799..3053
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1781..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2287..2555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2642..2665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1836..1855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1878..1906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1931..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2287..2341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2354..2389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2400..2417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2424..2440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2484..2512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2527..2555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2918
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 2805..2813
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2828
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M0Z1"
FT MOD_RES 1633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M0Z1"
FT MOD_RES 1824
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:F1M0Z1"
FT MOD_RES 2282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2634
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75962"
FT DISULFID 2709..2762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1890..1908
FT /note="ASSRLLVRPTSSETPSAAE -> HYVDLCSVSVLAQFPYLSI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16943433"
FT /id="VSP_023308"
FT VAR_SEQ 1909..3102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16943433"
FT /id="VSP_023309"
FT VAR_SEQ 2548
FT /note="G -> GS (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_037863"
FT VAR_SEQ 2549..2568
FT /note="EGSSSSNISTMLVTHEYTAV -> VRVPGSLRPSTPPPLSRQLF (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037864"
FT VAR_SEQ 2569..3102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037865"
FT MUTAGEN 1427
FT /note="Q->A: Abolishes Rac1 activation; when associated
FT with E-1435."
FT /evidence="ECO:0000269|PubMed:16943433"
FT MUTAGEN 1435
FT /note="L->E: Abolishes Rac1 activation; when associated
FT with A-1427."
FT /evidence="ECO:0000269|PubMed:16943433"
FT CONFLICT 2863
FT /note="E -> K (in Ref. 4; BAE32258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3102 AA; 347861 MW; 8E8F7C44CB4F72D0 CRC64;
MSGSSGGATA PAASSGPAAA ASAAGSGCGG GAGEGAEEAA KDLADIAAFF RSGFRKNDEM
KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRIR QEDLRRLISY LACIPSEEVC
KRGFTVIVDM RGSKWDSIKP LLKILQESFP CCIHIALIIK PDNFWQKQRT NFGSSKFEFE
TNMVSLEGLT KVVDPSQLTP EFDGCLEYNH EEWIEIRVAF EEYISNAAHM LSRLEELQDV
LAKKELPQDL EGARNMIDEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSD SFPKKNSGSG
NADLQNLLPK VSTMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE KMFDWITHNK
GLFLNSYTEI GTSHPHAMEL QTQHNHFAMN CMNVYVNINR IMSVANRLVE SGHYASQQIK
QIANQLEQEW KAFAAALDER STLLDMSSIF HQKAEKYMSN VDSWCKACGE VDLPSELQDL
EDAIHHHQGI YEHITLAYSE VSQDGKSLLD KLQRPLTPGS SDSLTASANY SKAVHHVLDV
IHEVLHHQRQ LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL
HRARALQKRH EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH QLEDRIQDFV
RRVEQRKILL DMSVSFHTHV KELWTWLEEL QKELLDDVYA ESVEAVQDLI KRFGQQQQTT
LQVTVNVIKE GEDLIQQLRD SAISSNKTPH NSSINHIETV LQQLDEAQSQ MEELFQERKI
KLELFLQLRI FERDAIDIIS DLESWNDELS QQMNDFDTED LTIAEQRLQH HADKALTMNN
LTFDVIHQGQ DLLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQQ ELDLAAEQHR
KHLEQCVQLR HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH EQFQHAIEKT
HQSALQVQQK AEAMLQANHY DMDMIRDCAE KVASHWQQLM LKMEDRLKLV NASVAFYKTS
EQVCSVLESL EQEYKREEDW CGGADKLGPN SETDHVTPMI SKHLEQKEAF LKACTLARRN
ADVFLKYLHR NSVSMPGMVT HIKAPEQQVK NILNELFQRE NRVLHYWTMR KRRLDQCQQY
VVFERSAKQA LEWIHDNGEF YLSTHTSTGS SIQHTQELLK EHEEFQITAK QTKERVKLLI
QLADGFCEKG HAHAAEIKKC VTAVDKRYRD FSLRMEKYRT SLEKALGISS DSNKSSKSLQ
LDIIPASIPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL IQTEKAYVRD LRECMDTYLW
EMTSGVEEIP PGIVNKELII FGNMQEIYEF HNNIFLKELE KYEQLPEDVG HCFVTWADKF
QMYVTYCKNK PDSTQLILEH AGSYFDEIQQ RHGLANSISS YLIKPVQRIT KYQLLLKELL
TCCEEGKGEI KDGLEVMLSV PKRANDAMHL SMLEGFDENI ESQGELILQE SFQVWDPKTL
IRKGRERHLF LFEMSLVFSK EVKDSSGRSK YLYKSKLFTS ELGVTEHVEG DPCKFALWVG
RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTVHLRGA LKEPIHIPKT APAARQKGRR
DGEDLDSQGD GSSQPDTISI ASRTSQNTLD SDKLSGGCEL TVVIHDFTAC NSNELTIRRG
QTVEVLERPH DKPDWCLVRT TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS
SNDASPPASV ASLQPHMIGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHAKKLAHKH
KKSREVRKSA DAGSQKDSDD SAATPQDETI EERGRNEGLS SGTLSKSSSS GMQSCGEEEG
EEGADAVPLP PPMAIQQHSL LQPDSQDDKA SSRLLVRPTS SETPSAAELV SAIEELVKSK
MALEDRPSSL LVDQGDSSSP SFNPSDNSLL SSSSPIDEME ERKCSSLKRR HYVLQELVET
ERDYVRDLGC VVEGYMALMK EDGVPDDMKG KDKIVFGNIH QIYDWHRDFF LGELEKCLED
PEKLGSLFVK HERRLHMYIV YCQNKPKSEH IVSEYIDTFF EDLKQRLGHR LQLTDLLIKP
VQRIMKYQLL LKDFLKYSKK ASLDTSELEK AVEVMCIVPK RCNDMMNVGR LQGFDGKIVA
QGKLLLQDTF LVTDQDAGLL PRCKERRVFL FEQIVIFSEP LDKKKGFSMP GFLFKNSIKV
SCLCLEENVE SDPCKFALTS RTGDAVETFV LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL
TSPIEYQRNH SGGGGSGSGG SSGGGGGSGG SGASSGGSSS HGSGPSSCSS GPSSSRSRPS
RIPQPVRHHP PMLVSSAASS QAEADKMSGM SAPSPSLPTP SSSLALEASL GQPSRLPLSG
DSEGHERETE PIPKMKVMES PRKAPGSTSG TSQDGNTKDA RGNLGSLPLG KTRPGAVSPL
NSPLSTTFPS PFGKEAFPPS SPLQKGGSFW SSIPASPASR PSSFTFPGDS DSLQRQTHRH
AAPSKDTDRM STCSSASEQS VQSTQSNGEG SSSSNISTML VTHEYTAVKE DEINVYQGEV
VQILASNQQN MFLVFRAATD QCPAAEGWIP GFVLGHTSAV IMENPDGTLK KSTSWHTALR
LRKKSEKKDK DGKRDGKLEN GYRKPREGLS NKVSVKLLNP NYIYDVPPEF VIPLSEVTCE
TGETVVFRCR VCGRPKASIT WKGPEHNTLN NDDHYSISYS DIGEATLKII GVSTEDDGIY
TCIAVNDMGS ASSSASLRVL GPGSDGIVVT WKDNFDAFYS EVAELGRGRF AVVKKCDQKG
TKRAVATKFV NKKLMKRDQV THELGILQNL QHPLLVSLLD TFETPTSYVL VLEMADQGRL
LDCVVRWGSL TEGKVRAHLG EVLEAVRYLH NCRIAHLDLK PENILVDQSL AKPTIKLADF
GDAVQLNTTY YIHQLLGNPE FAAPEIILGN PVSLTADTWS VGVLTYVLLS GVSPFLDDSV
EETCLNICRL DFSFPEDYFQ GVSQKAKEFV CFLLQEDPAK RPSAALALQE QWLQAGNGSG
KGTGVLDTSR LTSFIERRKH QNDVRPIRSI KNFLQSRLLP RV
