TIAM2_MOUSE
ID TIAM2_MOUSE Reviewed; 1715 AA.
AC Q6ZPF3; Q3TSM6; Q3TZ33; Q6AXF2; Q6NXJ2; Q9JLY2; Q9WVS3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Rho guanine nucleotide exchange factor TIAM2 {ECO:0000305|PubMed:10364228};
DE AltName: Full=SIF and TIAM1-like exchange factor;
DE AltName: Full=T-lymphoma invasion and metastasis-inducing protein 2 {ECO:0000305};
DE Short=TIAM-2;
GN Name=Tiam2 {ECO:0000312|MGI:MGI:1344338};
GN Synonyms=Kiaa2016, Stef {ECO:0000303|PubMed:11707441,
GN ECO:0000303|PubMed:14550769};
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 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=10364228; DOI=10.1074/jbc.274.25.17837;
RA Hoshino M., Sone M., Fukata M., Kuroda S., Kaibuchi K., Nabeshima Y.,
RA Hama C.;
RT "Identification of the stef gene that encodes a novel guanine nucleotide
RT exchange factor specific for Rac1.";
RL J. Biol. Chem. 274:17837-17844(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Inner ear, and Olfactory bulb;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1232-1498, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=10512681; DOI=10.1006/geno.1999.5936;
RA Chiu C.-Y., Leng S., Martin K.A., Kim E., Gorman S., Duhl D.M.;
RT "Cloning and characterization of T-cell lymphoma invasion and metastasis 2
RT (TIAM2), a novel guanine nucleotide exchange factor related to TIAM1.";
RL Genomics 61:66-73(1999).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11707441; DOI=10.1074/jbc.m106186200;
RA Matsuo N., Hoshino M., Yoshizawa M., Nabeshima Y.;
RT "Characterization of STEF, a guanine nucleotide exchange factor for Rac1,
RT required for neurite growth.";
RL J. Biol. Chem. 277:2860-2868(2002).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11900975; DOI=10.1016/s0925-4773(01)00650-5;
RA Yoshizawa M., Hoshino M., Sone M., Nabeshima Y.;
RT "Expression of stef, an activator of Rac1, correlates with the stages of
RT neuronal morphological development in the mouse brain.";
RL Mech. Dev. 113:65-68(2002).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=12912917; DOI=10.1093/emboj/cdg413;
RA Kawauchi T., Chihama K., Nabeshima Y., Hoshino M.;
RT "The in vivo roles of STEF/Tiam1, Rac1 and JNK in cortical neuronal
RT migration.";
RL EMBO J. 22:4190-4201(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14550769; DOI=10.1016/s1044-7431(03)00122-2;
RA Matsuo N., Terao M., Nabeshima Y., Hoshino M.;
RT "Roles of STEF/Tiam1, guanine nucleotide exchange factors for Rac1, in
RT regulation of growth cone morphology.";
RL Mol. Cell. Neurosci. 24:69-81(2003).
RN [10]
RP FUNCTION, INTERACTION WITH MAP1A; MAP1B; PARP1 AND YWHAE, PHOSPHORYLATION
RP AT THR-1662, AND MUTAGENESIS OF SER-1655; THR-1656; THR-1662; THR-1668 AND
RP SER-1672.
RX PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
RA Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T., Nakayama M.,
RA Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K., Amano M.;
RT "Rho-kinase modulates the function of STEF, a Rac GEF, through its
RT phosphorylation.";
RL Biochem. Biophys. Res. Commun. 355:788-794(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 500-757, AND INTERACTION WITH
RP CD44; PARD3 AND MAPK8IP2.
RX PubMed=19893486; DOI=10.1038/emboj.2009.323;
RA Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N., Watanabe T.,
RA Kaibuchi K., Hakoshima T.;
RT "The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding
RT module.";
RL EMBO J. 29:236-250(2010).
CC -!- FUNCTION: Modulates the activity of RHO-like proteins and connects
CC extracellular signals to cytoskeletal activities. Acts as a GDP-
CC dissociation stimulator protein that stimulates the GDP-GTP exchange
CC activity of RHO-like GTPases and activates them. Activates specifically
CC RAC1, but not CDC42 and RHOA. Mediates extracellular laminin signals to
CC activate Rac1, contributing to neurite growth. Involved in
CC lamellipodial formation and advancement of the growth cone of embryonic
CC hippocampal neurons. Promotes migration of neurons in the cerebral
CC cortex. When overexpressed, induces membrane ruffling accompanied by
CC the accumulation of actin filaments along the altered plasma membrane.
CC {ECO:0000269|PubMed:10364228, ECO:0000269|PubMed:11707441,
CC ECO:0000269|PubMed:12912917, ECO:0000269|PubMed:14550769,
CC ECO:0000269|PubMed:17320046}.
CC -!- SUBUNIT: Interacts with MAP1A, MAP1B, PARP1 and YWHAE. Interacts with
CC CD44, PARD3 and MAPK8IP2. {ECO:0000269|PubMed:17320046,
CC ECO:0000269|PubMed:19893486}.
CC -!- INTERACTION:
CC Q6ZPF3; P15379: Cd44; NbExp=8; IntAct=EBI-7565978, EBI-7565891;
CC Q6ZPF3; Q8TEW0: PARD3; Xeno; NbExp=2; IntAct=EBI-7565978, EBI-81968;
CC Q6ZPF3; Q8TEW0-2: PARD3; Xeno; NbExp=6; IntAct=EBI-7565978, EBI-9118204;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14550769}. Cell
CC projection, lamellipodium {ECO:0000269|PubMed:14550769}. Cell
CC projection, filopodium {ECO:0000269|PubMed:14550769}. Cell projection,
CC growth cone {ECO:0000269|PubMed:11707441, ECO:0000269|PubMed:14550769}.
CC Cell projection, neuron projection {ECO:0000269|PubMed:11707441,
CC ECO:0000269|PubMed:14550769}. Perikaryon {ECO:0000269|PubMed:11707441}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6ZPF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZPF3-2; Sequence=VSP_030977;
CC Name=3;
CC IsoId=Q6ZPF3-3; Sequence=VSP_030976;
CC Name=4;
CC IsoId=Q6ZPF3-4; Sequence=VSP_030978, VSP_030979;
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain (at protein level).
CC Expressed in the olfactory bulb, cortical plate of the cerebral cortex,
CC caudate putamen, hippocampus, ependymal cells of the lateral surface of
CC the lateral ventricles of the brain. Weakly expressed in heart, lung,
CC liver, skeletal muscle, kidney and testis.
CC {ECO:0000269|PubMed:10364228, ECO:0000269|PubMed:10512681,
CC ECO:0000269|PubMed:11707441, ECO:0000269|PubMed:11900975,
CC ECO:0000269|PubMed:12912917, ECO:0000269|PubMed:14550769}.
CC -!- DEVELOPMENTAL STAGE: Expressed in cerebral cortex, predominantly in the
CC cortical plate and intermediate zone and weakly in the ventricular
CC zone, in neurites and the growth cone of neurites of the hippocampus at
CC 15 dpc (at protein level). Expressed in embryo at 7, 11, 15 and 17 dpc.
CC Expressed in the preplate which consists of the Cajal-Retzius cells and
CC the precursors of subplate neurons, in neurons of the telecephalon, in
CC primordia of cerebral cortex and hippocampus at 12 dpc. Expressed in
CC the cortical plate, striatum and fourth ventricle of the brain, in the
CC cartilaginous tissues including Meckel, costal, vertebral and tracheal
CC cartilage at 14.5 dpc. Expressed in cerebral cortex, hippocampus,
CC olfactory bulbs, rostral migratory pathway and the striatum at 17 dpc.
CC {ECO:0000269|PubMed:10364228, ECO:0000269|PubMed:10512681,
CC ECO:0000269|PubMed:11707441, ECO:0000269|PubMed:11900975,
CC ECO:0000269|PubMed:12912917}.
CC -!- DOMAIN: The PH 1 domain and amino acids 619-780 (a region called TSS;
CC otherwise known as CC-Ex) are necessary for membrane localization. PH 1
CC and TSS domains are necessary for Rac1 activity. The PH 2 domain is
CC engaged in the enhancement of the catalytic activity of the adjacent DH
CC domain. The PH 1, TSS and DH domains are necessary to induce neurite-
CC like structure.
CC -!- PTM: Phosphorylated on serine and threonine residues. Phosphorylated on
CC Thr-1662 by Rho-kinase. Its phosphorylation by Rho-kinase inhibits its
CC guanine nucleotide exchange activity, its interaction with MAP1A,
CC MAP1B, PARP1 and YWHAE and reduces its ability to promote neurite
CC growth. {ECO:0000269|PubMed:17320046}.
CC -!- SIMILARITY: Belongs to the TIAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98284.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB022915; BAA81823.1; -; mRNA.
DR EMBL; AK129474; BAC98284.1; ALT_INIT; mRNA.
DR EMBL; AK158137; BAE34377.1; -; mRNA.
DR EMBL; AK161947; BAE36649.1; -; mRNA.
DR EMBL; BC067048; AAH67048.1; -; mRNA.
DR EMBL; BC079600; AAH79600.1; -; mRNA.
DR EMBL; AF121102; AAF28865.1; -; mRNA.
DR CCDS; CCDS37421.1; -. [Q6ZPF3-1]
DR RefSeq; NP_001116470.1; NM_001122998.1. [Q6ZPF3-1]
DR RefSeq; NP_001273686.1; NM_001286757.1. [Q6ZPF3-3]
DR RefSeq; NP_001273687.1; NM_001286758.1.
DR RefSeq; NP_036008.2; NM_011878.2. [Q6ZPF3-1]
DR RefSeq; XP_006523288.1; XM_006523225.3. [Q6ZPF3-1]
DR RefSeq; XP_006523289.1; XM_006523226.1. [Q6ZPF3-1]
DR RefSeq; XP_006523296.1; XM_006523233.1. [Q6ZPF3-3]
DR PDB; 3A8P; X-ray; 2.10 A; A/B/C/D=500-757.
DR PDB; 3A8Q; X-ray; 3.20 A; A/B/C/D=500-757.
DR PDBsum; 3A8P; -.
DR PDBsum; 3A8Q; -.
DR AlphaFoldDB; Q6ZPF3; -.
DR SMR; Q6ZPF3; -.
DR BioGRID; 204849; 19.
DR IntAct; Q6ZPF3; 8.
DR MINT; Q6ZPF3; -.
DR STRING; 10090.ENSMUSP00000125842; -.
DR iPTMnet; Q6ZPF3; -.
DR PhosphoSitePlus; Q6ZPF3; -.
DR MaxQB; Q6ZPF3; -.
DR PaxDb; Q6ZPF3; -.
DR PeptideAtlas; Q6ZPF3; -.
DR PRIDE; Q6ZPF3; -.
DR ProteomicsDB; 258879; -. [Q6ZPF3-1]
DR ProteomicsDB; 258880; -. [Q6ZPF3-2]
DR ProteomicsDB; 258881; -. [Q6ZPF3-3]
DR ProteomicsDB; 258882; -. [Q6ZPF3-4]
DR Antibodypedia; 2773; 184 antibodies from 25 providers.
DR DNASU; 24001; -.
DR Ensembl; ENSMUST00000072156; ENSMUSP00000072020; ENSMUSG00000023800. [Q6ZPF3-1]
DR Ensembl; ENSMUST00000169838; ENSMUSP00000125842; ENSMUSG00000023800. [Q6ZPF3-1]
DR GeneID; 24001; -.
DR KEGG; mmu:24001; -.
DR UCSC; uc008aeo.1; mouse. [Q6ZPF3-1]
DR UCSC; uc008aep.1; mouse. [Q6ZPF3-4]
DR UCSC; uc008aer.1; mouse. [Q6ZPF3-3]
DR CTD; 26230; -.
DR MGI; MGI:1344338; Tiam2.
DR VEuPathDB; HostDB:ENSMUSG00000023800; -.
DR eggNOG; KOG3519; Eukaryota.
DR GeneTree; ENSGT00940000157012; -.
DR HOGENOM; CLU_000494_3_1_1; -.
DR InParanoid; Q6ZPF3; -.
DR OMA; SHFKSHQ; -.
DR OrthoDB; 34437at2759; -.
DR PhylomeDB; Q6ZPF3; -.
DR TreeFam; TF319686; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 24001; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Tiam2; mouse.
DR EvolutionaryTrace; Q6ZPF3; -.
DR PRO; PR:Q6ZPF3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6ZPF3; protein.
DR Bgee; ENSMUSG00000023800; Expressed in cortical plate and 162 other tissues.
DR ExpressionAtlas; Q6ZPF3; baseline and differential.
DR Genevisible; Q6ZPF3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR043537; Tiam1/Tiam2/Sif.
DR InterPro; IPR040655; TIAM1_CC-Ex.
DR PANTHER; PTHR46001; PTHR46001; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF18385; Tiam_CC_Ex; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00455; RBD; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50898; RBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Guanine-nucleotide releasing factor; Lipoprotein; Myristate;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..1715
FT /note="Rho guanine nucleotide exchange factor TIAM2"
FT /id="PRO_0000317468"
FT DOMAIN 504..618
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 831..902
FT /note="RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 911..997
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1120..1314
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1347..1478
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1515..1582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 665..692
FT /evidence="ECO:0000255"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1662
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17320046"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..1096
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030976"
FT VAR_SEQ 616
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030977"
FT VAR_SEQ 786..788
FT /note="MFD -> VSS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030978"
FT VAR_SEQ 789..1715
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030979"
FT MUTAGEN 1655
FT /note="S->A: No change of phosphorylation by Rho-kinase."
FT /evidence="ECO:0000269|PubMed:17320046"
FT MUTAGEN 1656
FT /note="T->A: No change of phosphorylation by Rho-kinase."
FT /evidence="ECO:0000269|PubMed:17320046"
FT MUTAGEN 1662
FT /note="T->A: Strongly decrease phosphorylation by Rho-
FT kinase. No change in promoting neurite growth; when
FT associated with A-1668 and A-1672."
FT /evidence="ECO:0000269|PubMed:17320046"
FT MUTAGEN 1668
FT /note="T->A: Slight decrease phosphorylation by Rho-kinase.
FT No change in promoting neurite growth; when associated with
FT A-1662 and A-1672."
FT /evidence="ECO:0000269|PubMed:17320046"
FT MUTAGEN 1672
FT /note="S->A: Slight decrease phosphorylation by Rho-kinase.
FT No change in promoting neurite growth; when associated with
FT A-1662 and A-1668."
FT /evidence="ECO:0000269|PubMed:17320046"
FT CONFLICT 45
FT /note="G -> D (in Ref. 3; BAE34377)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="T -> A (in Ref. 2; BAC98284)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="E -> D (in Ref. 2; BAC98284)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="K -> Q (in Ref. 1; BAA81823)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="V -> I (in Ref. 1; BAA81823)"
FT /evidence="ECO:0000305"
FT CONFLICT 860
FT /note="V -> A (in Ref. 1; BAA81823 and 2; BAC98284)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="L -> P (in Ref. 1; BAA81823)"
FT /evidence="ECO:0000305"
FT CONFLICT 1234
FT /note="R -> K (in Ref. 5; AAF28865)"
FT /evidence="ECO:0000305"
FT CONFLICT 1248
FT /note="F -> C (in Ref. 5; AAF28865)"
FT /evidence="ECO:0000305"
FT CONFLICT 1397
FT /note="N -> D (in Ref. 5; AAF28865)"
FT /evidence="ECO:0000305"
FT CONFLICT 1446
FT /note="I -> V (in Ref. 5; AAF28865)"
FT /evidence="ECO:0000305"
FT CONFLICT 1611
FT /note="I -> L (in Ref. 2; BAC98284)"
FT /evidence="ECO:0000305"
FT STRAND 505..520
FT /evidence="ECO:0007829|PDB:3A8P"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:3A8P"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:3A8P"
FT STRAND 534..541
FT /evidence="ECO:0007829|PDB:3A8P"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:3A8P"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:3A8P"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:3A8P"
FT STRAND 583..589
FT /evidence="ECO:0007829|PDB:3A8P"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:3A8P"
FT HELIX 603..624
FT /evidence="ECO:0007829|PDB:3A8P"
FT HELIX 630..659
FT /evidence="ECO:0007829|PDB:3A8P"
FT HELIX 665..700
FT /evidence="ECO:0007829|PDB:3A8P"
FT HELIX 707..711
FT /evidence="ECO:0007829|PDB:3A8P"
FT HELIX 716..725
FT /evidence="ECO:0007829|PDB:3A8P"
FT HELIX 730..739
FT /evidence="ECO:0007829|PDB:3A8P"
SQ SEQUENCE 1715 AA; 192567 MW; 96C1E063BC6F36C0 CRC64;
MGNSESQYTF QGSKNHSNTV TGAKQKPCSL KIRSVHAKDE KSLHGWTHGS SGAGYKSRSL
ARSCLSHFKN HQPYATRLSG PTCKVSKGTT YSKHRANTPG NDFQGNSGAF LPENGFHYVD
RESEESHITS NGHLLTCYGR KESLASTPPG EDHRSPRVLI KTLGKLDGCL RVEFHNGGNP
HKGTSEDPSG PVRLLRYSPT LASETCPVRE TRRHSAAGSP SSQRPSPTDS RLRSSKGSSL
SSESSWYDSP WGNAGEVSEV EGSFLAPSTP DPSLPSSFPP SDTKKPFNQS SSLSSLRELY
KDPNLGCRSP SGTCLSSNEY ISSQVSLNNR VSFASDMDVP SRVDHRDPLH YSSFTLPCRK
SKALTEDAAK KDTLKARMRR FSDWTGSLSR KKRKLQEPRS MEGSEYFDSH SDGLNAEGQV
PAQTSSLLWS GGSAQTLPHR SESTHAISVD PLRQNIYENF MRELEMSRSN TEHVETSTET
MESSSESVSS LEQLDLLFEK EQGVVRKAGW LFFKPLVTLQ KERKLELVAR RKWKQYWVTL
KGCTLLFYET YGKNSTEQNS APRCALFAED SIVQSVPEHP KKEHVFCLSN SCGDVYLFQA
TSQTDLENWV TAIHSACASL FAKKHGKEDT VRLLKSQTRS LLQKIDMDSK MKKMAELQLS
VVSDPKNRKA IENQIRQWEQ NLEKFHMDLF RMRCYLASLQ GGELPNPKSL LAATSRPSKL
ALGRLGVLSV SSFHALVCSR DDSTLRKRTL SLTQRGKSKK GIFSSLKGLD TLARKGREKR
ASITQMFDSS HSHGFLGTQL PQKSTNSNKA HDLHLYGSAV DSALRDSMWE VQTYVHFQDN
EGVTVTIKPE HRVEDVLALV CKMRQLEPTH YGLQLRKVVD KSVEWCVPAL YEYMQEQVYD
EIEVFPLSVY DVQLTKTGDM TDFGFAVTVQ VDEHQHLNRI FISDVLPDSL AYGGGLRKGN
EITSLNGEPV SDLDIQQMEA LFSEKSVGLT LVARPVTTRR TLCASWSDSD LFSRDQKSLP
PSPNQSQLLE EFLDNFRKTA TSDFSNVPEI TTGLKRSQTE GTLDQVPHRE KMEQTFLSAD
QIAELCRDLN NTHTNSMEAP TESHDPPPRP LARHLSDADR LRKVIQELVD TEKSYVKDLS
CLFELYLEPL QNETFLTQDE MESLFGSLPE MLEFQKVFLE TLEDAISASS DFSVLETPSQ
FRKLLFSLGG SFLYYADHFK LYSGFCANHI KVQRVLERAK TDKAFKAFLD ARNPTKQHSS
TLESYLIKPV QRVLKYPLLL KELVSLTDHE SEEHYHLTEA LKAMEKVASH INEMQKIYED
YGMVFDQLVA EQSGTEKEVT ELSMGELLMH STVSWLNPFL SLGKARKDIE LTVFVFKRAV
ILVYKENCKL KKKLPSNSRP AHNSADLDPF KFRWLIPISA LQVRLGNTAG TENNSTWELI
HTKSEIEGRP ETIFQLCCSD SENKTSIVKV IRSILRENFR RHIKCELPLE KTCKDRLVPL
KNRVPVSAKL ASSRSLKGLR TSSSSEWPSE PSKGNSLDSD ECSLSSGTQS SGCPVAESRR
DSKSTELEKD AQEGLAEFPD GLIKESDILS DEDEDFHHPL KQGSPTKDIE IQFQRLKISE
ESDVHPVGQQ PLTESGEQPK LVRGHFCPIK RKANSTKRGR GTLLKAQTRH QSLDSHPETA
SIDLNLVLER EFSVQSLTSV VNEEGFYETQ SHGKS
