MTSS2_HUMAN
ID MTSS2_HUMAN Reviewed; 747 AA.
AC Q765P7; A6NJI7; Q9BUA8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein MTSS 2 {ECO:0000305};
DE AltName: Full=Actin-bundling with BAIAP2 homology protein 1;
DE Short=ABBA-1;
DE AltName: Full=MTSS1-like protein;
GN Name=MTSS2 {ECO:0000312|HGNC:HGNC:25094};
GN Synonyms=MTSS1L {ECO:0000312|HGNC:HGNC:25094};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DOMAIN.
RX PubMed=14752106; DOI=10.1074/jbc.m309408200;
RA Yamagishi A., Masuda M., Ohki T., Onishi H., Mochizuki N.;
RT "A novel actin bundling/filopodium-forming domain conserved in insulin
RT receptor tyrosine kinase substrate p53 and missing in metastasis protein.";
RL J. Biol. Chem. 279:14929-14936(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-747 (ISOFORM 2).
RC TISSUE=Skin;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601; SER-639 AND THR-643, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; SER-579; SER-612;
RP SER-624; SER-634 AND SER-639, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP FUNCTION, INTERACTION WITH RAC1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-115; LYS-116; LYS-123; LYS-127; LYS-130; LYS-137; LYS-138; LYS-139;
RP LYS-145; LYS-148; LYS-149; LYS-152 AND LYS-157.
RX PubMed=20875796; DOI=10.1016/j.bbrc.2010.09.087;
RA Zheng D., Niu S., Yu D., Zhan X.H., Zeng X., Cui B., Chen Y., Yoon J.,
RA Martin S.S., Lu X., Zhan X.;
RT "Abba promotes PDGF-mediated membrane ruffling through activation of the
RT small GTPase Rac1.";
RL Biochem. Biophys. Res. Commun. 401:527-532(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; SER-601 AND SER-612, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-639, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in plasma membrane dynamics. Potentiated PDGF-
CC mediated formation of membrane ruffles and lamellipodia in fibroblasts,
CC acting via RAC1 activation (PubMed:14752106). May function in actin
CC bundling (PubMed:14752106). {ECO:0000269|PubMed:14752106}.
CC -!- SUBUNIT: Interacts (via IMD domain) with RAC1; this interaction may be
CC important to potentiate PDGF-induced RAC1 activation.
CC {ECO:0000269|PubMed:20875796}.
CC -!- INTERACTION:
CC Q765P7; P13196: ALAS1; NbExp=3; IntAct=EBI-2815102, EBI-3905054;
CC Q765P7; Q9H7N4: SCAF1; NbExp=3; IntAct=EBI-2815102, EBI-1222181;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20875796}. Cell
CC projection, ruffle {ECO:0000269|PubMed:20875796}. Note=Colocalizes with
CC RAC1 within membrane ruffles. {ECO:0000269|PubMed:20875796}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q765P7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q765P7-2; Sequence=VSP_031513, VSP_031514, VSP_031515;
CC -!- SIMILARITY: Belongs to the MTSS family. {ECO:0000305}.
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DR EMBL; AB115770; BAC98378.1; -; mRNA.
DR EMBL; AC020763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002770; AAH02770.1; -; mRNA.
DR CCDS; CCDS32476.1; -. [Q765P7-1]
DR RefSeq; NP_612392.1; NM_138383.2. [Q765P7-1]
DR AlphaFoldDB; Q765P7; -.
DR SMR; Q765P7; -.
DR BioGRID; 124914; 41.
DR IntAct; Q765P7; 3.
DR STRING; 9606.ENSP00000341171; -.
DR GlyGen; Q765P7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q765P7; -.
DR PhosphoSitePlus; Q765P7; -.
DR BioMuta; MTSS1L; -.
DR DMDM; 74727332; -.
DR EPD; Q765P7; -.
DR jPOST; Q765P7; -.
DR MassIVE; Q765P7; -.
DR MaxQB; Q765P7; -.
DR PaxDb; Q765P7; -.
DR PeptideAtlas; Q765P7; -.
DR PRIDE; Q765P7; -.
DR ProteomicsDB; 68659; -. [Q765P7-1]
DR ProteomicsDB; 68660; -. [Q765P7-2]
DR Antibodypedia; 58925; 32 antibodies from 12 providers.
DR DNASU; 92154; -.
DR Ensembl; ENST00000338779.11; ENSP00000341171.6; ENSG00000132613.16. [Q765P7-1]
DR GeneID; 92154; -.
DR KEGG; hsa:92154; -.
DR MANE-Select; ENST00000338779.11; ENSP00000341171.6; NM_138383.3; NP_612392.1.
DR UCSC; uc002ezj.4; human. [Q765P7-1]
DR CTD; 92154; -.
DR DisGeNET; 92154; -.
DR GeneCards; MTSS2; -.
DR HGNC; HGNC:25094; MTSS2.
DR HPA; ENSG00000132613; Tissue enhanced (brain).
DR MIM; 616951; gene.
DR neXtProt; NX_Q765P7; -.
DR OpenTargets; ENSG00000132613; -.
DR PharmGKB; PA164723215; -.
DR VEuPathDB; HostDB:ENSG00000132613; -.
DR eggNOG; ENOG502QRG4; Eukaryota.
DR GeneTree; ENSGT00950000183156; -.
DR HOGENOM; CLU_004805_2_1_1; -.
DR InParanoid; Q765P7; -.
DR OMA; CVFYTDD; -.
DR OrthoDB; 529252at2759; -.
DR PhylomeDB; Q765P7; -.
DR TreeFam; TF320619; -.
DR PathwayCommons; Q765P7; -.
DR SignaLink; Q765P7; -.
DR BioGRID-ORCS; 92154; 16 hits in 1079 CRISPR screens.
DR ChiTaRS; MTSS1L; human.
DR GenomeRNAi; 92154; -.
DR Pharos; Q765P7; Tbio.
DR PRO; PR:Q765P7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q765P7; protein.
DR Bgee; ENSG00000132613; Expressed in C1 segment of cervical spinal cord and 130 other tissues.
DR ExpressionAtlas; Q765P7; baseline and differential.
DR Genevisible; Q765P7; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0003785; F:actin monomer binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0097581; P:lamellipodium organization; IEA:Ensembl.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:0097178; P:ruffle assembly; IEA:InterPro.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR030127; MTSS1/MTSS2.
DR InterPro; IPR030059; MTSS2.
DR PANTHER; PTHR15708; PTHR15708; 1.
DR PANTHER; PTHR15708:SF8; PTHR15708:SF8; 1.
DR Pfam; PF08397; IMD; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51338; IMD; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..747
FT /note="Protein MTSS 2"
FT /id="PRO_0000319610"
FT DOMAIN 1..252
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 719..736
FT /note="WH2"
FT REGION 256..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..159
FT /evidence="ECO:0000255"
FT COMPBIAS 256..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9S0"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P9S0"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"
FT MOD_RES 643
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT VAR_SEQ 153..155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031513"
FT VAR_SEQ 264..294
FT /note="SPSSSSSRKSSMCSAPSSSSSAKGGGAPWPG -> VPSEPFVSFLSVRFWKN
FT SPLLPAPSTPSSPI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031514"
FT VAR_SEQ 295..747
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031515"
FT MUTAGEN 115
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-116,
FT D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 116
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 123
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-127, D-130, D-137, D-138, D-139, D-145, D-148, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 127
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-130, D-137, D-138, D-139, D-145, D-148, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 130
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-127, D-137, D-138, D-139, D-145, D-148, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 137
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-127, D-130, D-138, D-139, D-145, D-148, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 138
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-127, D-130, D-137, D-139, D-145, D-148, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 139
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-127, D-130, D-137, D-138, D-145, D-148, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 145
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-148, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 148
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-
FT 149, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 149
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-
FT 148, D-152 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 152
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-
FT 148, D-149 and D-157."
FT /evidence="ECO:0000269|PubMed:20875796"
FT MUTAGEN 157
FT /note="K->D: Marked reduction in RAC1-binding, loss of
FT increase in RAC1 activity and of dorsal ruffles formation
FT in response to PDGF treatment; when associated with D-115,
FT D-116, D-123, D-127, D-130, D-137, D-138, D-139, D-145, D-
FT 148, D-149 and D-152."
FT /evidence="ECO:0000269|PubMed:20875796"
SQ SEQUENCE 747 AA; 79929 MW; 9D0EEF31702E9736 CRC64;
METAEKECGA LGGLFQAIVN DMKSSYPIWE DFNSKATKLH SQLRTTVLAA VAFLDAFQKV
ADMATNTRGA TRDIGSALTR MCMRHRSIET KLRQFTNALL ESLINPLQER IEDWKKAANQ
LDKDHAKEYK RARHEIKKKS SDTLKLQKKA RKELLGKGDL QPQLDSALQD VNDMYLLLEE
TEKQAVRRAL IEERGRFCTF ITFLQPVVNG ELTMLGEITH LQGIIDDLVV LTAEPHKLPP
ASEQVIKDLK GSDYSWSYQT PPSSPSSSSS RKSSMCSAPS SSSSAKGGGA PWPGGAQTYS
PSSTCRYRSL AQPATTTARL SSVSSHDSGF VSQDATYSKP PSPMPSDITS QKSSSSASSE
ASETCQSVSE CSSPTSDWSK VGSHEQPSGA TLQRRKDRVE LLRDTEPGPA SGGTLGPSGE
EAPRPRMSPA TIAAKHGEEV SPAASDLAMV LTRGLSLEHQ KSSRDSLQYS SGYSTQTTTP
SCSEDTIPSQ GSDYDCYSVN GDADSEGPPE FDKSSTIPRN SNIAQNYRRL IQTKRPASTA
GLPTAGLPTA TGLPSGAPPG VATIRRTPST KPTVRRALSS AGPIPIRPPI VPVKTPTVPD
SPGYMGPTRA GSEECVFYTD ETASPLAPDL AKASPKRLSL PNTAWGSPSP EAAGYPGAGA
EDEQQQLAAN RHSLVEKLGE LVAGAHALGE GQFPFPTALS ATPTEETPTP PPAATSDPPA
EDMLVAIRRG VRLRRTVTND RSAPRIL
