ID VASP_MOUSE Reviewed; 375 AA. AC P70460; Q3TAP0; Q3TCD2; Q3U0C2; Q3UDF1; Q91VD2; Q9R214; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 24-JAN-2024, entry version 186. DE RecName: Full=Vasodilator-stimulated phosphoprotein; DE Short=VASP; GN Name=Vasp; 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 [GENOMIC DNA], AND VARIANT THR-209. RC STRAIN=129; RX PubMed=8812448; DOI=10.1006/geno.1996.0457; RA Zimmer M., Fink T., Fischer L., Hauser W., Scherer K., Lichter P., RA Walter U.; RT "Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human RT and mouse: structure, sequence, and chromosomal localization."; RL Genomics 36:227-233(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION. RC STRAIN=C57BL/6J; RX PubMed=10085070; DOI=10.1074/jbc.274.13.8391; RA Collins S.P., Uhler M.D.; RT "Cyclic AMP- and cyclic GMP-dependent protein kinases differ in their RT regulation of cyclic AMP response element-dependent gene transcription."; RL J. Biol. Chem. 274:8391-8404(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-209. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Adipose tissue, Bone marrow, Dendritic cell, and Spleen; 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]. RC STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor; 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 DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RX PubMed=10069337; DOI=10.1016/s0896-6273(00)81092-2; RA Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M., Macklis J.D., RA Kwiatkowski D., Soriano P., Gertler F.B.; RT "Mena is required for neurulation and commissure formation."; RL Neuron 22:313-325(1999). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10660044; DOI=10.1016/s0092-8674(00)81559-7; RA Vasioukhin V., Bauer C., Yin M., Fuchs E.; RT "Directed actin polymerization is the driving force for epithelial cell- RT cell adhesion."; RL Cell 100:209-219(2000). RN [7] RP INTERACTION WITH ACTN1; PFN1; PFN2; VCL AND ZYX, PHOSPHORYLATION AT SER-153 RP AND SER-235, AND MUTAGENESIS OF SER-153; SER-235 AND THR-274. RX PubMed=10882740; DOI=10.1074/jbc.m005066200; RA Harbeck B., Huttelmaier S., Schlueter K., Jockusch B.M., Illenberger S.; RT "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its RT interaction with actin."; RL J. Biol. Chem. 275:30817-30825(2000). RN [8] RP INTERACTION WITH ACTG1, PHOSPHORYLATION, AND MUTAGENESIS OF RP 232-ARG-LYS-233. RX PubMed=12372613; DOI=10.1016/s0014-5793(02)03356-2; RA Walders-Harbeck B., Khaitlina S.Y., Hinssen H., Jockusch B.M., RA Illenberger S.; RT "The vasodilator-stimulated phosphoprotein promotes actin polymerisation RT through direct binding to monomeric actin."; RL FEBS Lett. 529:275-280(2002). RN [9] RP INTERACTION WITH DNMBP. RX PubMed=14506234; DOI=10.1074/jbc.m308104200; RA Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H., RA Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.; RT "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology RT domains, links dynamin to regulation of the actin cytoskeleton."; RL J. Biol. Chem. 278:49031-49043(2003). RN [10] RP INTERACTION WITH APBB1IP. RX PubMed=15642358; DOI=10.1016/j.febslet.2004.10.110; RA Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.; RT "PREL1 provides a link from Ras signalling to the actin cytoskeleton via RT Ena/VASP proteins."; RL FEBS Lett. 579:455-463(2005). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-317 AND SER-320, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, 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 [14] RP PHOSPHORYLATION AT SER-318. RX PubMed=21945940; DOI=10.1016/j.bbrc.2011.09.059; RA Thomson D.M., Ascione M.P., Grange J., Nelson C., Hansen M.D.; RT "Phosphorylation of VASP by AMPK alters actin binding and occurs at a novel RT site."; RL Biochem. Biophys. Res. Commun. 414:215-219(2011). CC -!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a CC range of processes dependent on cytoskeleton remodeling and cell CC polarity such as axon guidance, lamellipodial and filopodial dynamics, CC platelet activation and cell migration. VASP promotes actin filament CC elongation. It protects the barbed end of growing actin filaments CC against capping and increases the rate of actin polymerization in the CC presence of capping protein. VASP stimulates actin filament elongation CC by promoting the transfer of profilin-bound actin monomers onto the CC barbed end of growing actin filaments. Plays a role in actin-based CC mobility of Listeria monocytogenes in host cells. Regulates actin CC dynamics in platelets and plays an important role in regulating CC platelet aggregation (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:10660044}. CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with PFN1, PFN2, LPP, CC ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the Pro-rich CC regions of ZYX. This interaction is important for targeting to focal CC adhesions and the formation of actin-rich structures at the apical CC surface of cells. Interacts, via the EVH1 domain, with the Pro-rich CC domain of Listeria monocytogenes actA. Interacts with APBB1IP. CC Interacts, via the Pro-rich domain, with the C-terminal SH3 domain of CC DNMBP. Interacts weakly with MEFV (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10660044}. CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10660044}. Cell junction, CC focal adhesion {ECO:0000269|PubMed:10660044}. Cell junction, tight CC junction {ECO:0000250}. Cell projection, lamellipodium membrane CC {ECO:0000269|PubMed:10660044}. Cell projection, filopodium membrane CC {ECO:0000269|PubMed:10660044}. Note=Targeted to stress fibers and focal CC adhesions through interaction with a number of proteins including MRL CC family members. Localizes to the plasma membrane in protruding CC lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also CC translocates VASP to focal adhesions. Localized along the sides of CC actin filaments throughout the peripheral cytoplasm under basal CC conditions (By similarity). In pre-apoptotic cells, colocalizes with CC MEFV in large specks (pyroptosomes) (By similarity). {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Highly expressed in thymus and spleen. Lower levels CC in lung, ovary, placenta and fat. {ECO:0000269|PubMed:10069337}. CC -!- DEVELOPMENTAL STAGE: Expressed constantly throughout brain development, CC with lower levels in adulthood. {ECO:0000269|PubMed:10069337}. CC -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a CC thymosin-like domain required for G-actin binding. The KLKR motif CC within this block is essential for the G-actin binding and for actin CC polymerization. Block B is required for F-actin binding and subcellular CC location, and Block C for tetramerization. CC -!- DOMAIN: The WH1 domain mediates interaction with XIRP1. {ECO:0000250}. CC -!- PTM: Major substrate for cAMP-dependent (PKA) and cGMP-dependent CC protein kinase (PKG) in platelets. The preferred site for PKA is Ser- CC 153, the preferred site for PKG, Ser-235. In ADP-activated platelets, CC phosphorylation by PKA or PKG/PRKG1 on Ser-153 leads to fibrinogen CC receptor inhibition. Phosphorylation on Thr-274 requires prior CC phosphorylation on Ser-153 and Ser-235. In response to phorbol ester CC (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to CC thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr- CC 274 by AMPK does not require prior phosphorylation at Ser-153 or Ser- CC 235. Phosphorylation at Ser-153 by PKA is required for localization to CC the tight junctions in epithelial cells. Phosphorylation modulates F- CC actin binding, actin filament elongation and platelet activation. CC Phosphorylation at Ser-318 by AMPK also alters actin filament binding. CC Carbon monoxide (CO) promotes phosphorylation at Ser-153, while nitric CC oxide (NO) promotes phosphorylation at Ser-153, but also at Ser-235. CC {ECO:0000269|PubMed:10085070, ECO:0000269|PubMed:10882740, CC ECO:0000269|PubMed:12372613, ECO:0000269|PubMed:21945940}. CC -!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA67108.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X98475; CAA67108.1; ALT_SEQ; Genomic_DNA. DR EMBL; AF084548; AAD16045.1; -; mRNA. DR EMBL; AK140329; BAE24338.1; -; mRNA. DR EMBL; AK150103; BAE29310.1; -; mRNA. DR EMBL; AK157021; BAE33933.1; -; mRNA. DR EMBL; AK170780; BAE42025.1; -; mRNA. DR EMBL; AK171715; BAE42628.1; -; mRNA. DR EMBL; BC010223; AAH10223.1; -; mRNA. DR EMBL; BC015289; AAH15289.1; -; mRNA. DR CCDS; CCDS52056.1; -. DR RefSeq; NP_001268950.1; NM_001282021.1. DR RefSeq; NP_001268951.1; NM_001282022.1. DR RefSeq; NP_033525.2; NM_009499.3. DR PDB; 2V8C; X-ray; 1.98 A; C=165-184. DR PDBsum; 2V8C; -. DR AlphaFoldDB; P70460; -. DR SMR; P70460; -. DR BioGRID; 204499; 8. DR DIP; DIP-29360N; -. DR IntAct; P70460; 4. DR MINT; P70460; -. DR STRING; 10090.ENSMUSP00000032561; -. DR iPTMnet; P70460; -. DR PhosphoSitePlus; P70460; -. DR SwissPalm; P70460; -. DR EPD; P70460; -. DR jPOST; P70460; -. DR MaxQB; P70460; -. DR PaxDb; 10090-ENSMUSP00000032561; -. DR PeptideAtlas; P70460; -. DR ProteomicsDB; 300166; -. DR Pumba; P70460; -. DR Antibodypedia; 1491; 1269 antibodies from 46 providers. DR DNASU; 22323; -. DR Ensembl; ENSMUST00000032561.9; ENSMUSP00000032561.9; ENSMUSG00000030403.10. DR GeneID; 22323; -. DR KEGG; mmu:22323; -. DR UCSC; uc009fle.2; mouse. DR AGR; MGI:109268; -. DR CTD; 7408; -. DR MGI; MGI:109268; Vasp. DR VEuPathDB; HostDB:ENSMUSG00000030403; -. DR eggNOG; KOG4590; Eukaryota. DR GeneTree; ENSGT00940000156765; -. DR HOGENOM; CLU_017790_0_0_1; -. DR InParanoid; P70460; -. DR OMA; TSEAHPC; -. DR OrthoDB; 2884005at2759; -. DR PhylomeDB; P70460; -. DR TreeFam; TF321411; -. DR Reactome; R-MMU-376176; Signaling by ROBO receptors. DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions. DR BioGRID-ORCS; 22323; 1 hit in 77 CRISPR screens. DR ChiTaRS; Vasp; mouse. DR PRO; PR:P70460; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; P70460; Protein. DR Bgee; ENSMUSG00000030403; Expressed in granulocyte and 250 other cell types or tissues. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0030175; C:filopodium; IDA:MGI. DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005925; C:focal adhesion; IDA:MGI. DR GO; GO:0030027; C:lamellipodium; IDA:MGI. DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005522; F:profilin binding; ISO:MGI. DR GO; GO:0017124; F:SH3 domain binding; IBA:GO_Central. DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI. DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro. DR GO; GO:0007411; P:axon guidance; IGI:MGI. DR GO; GO:0001843; P:neural tube closure; IGI:MGI. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:MGI. DR GO; GO:0051289; P:protein homotetramerization; IEA:InterPro. DR CDD; cd01207; EVH1_Ena_VASP-like; 1. DR CDD; cd22185; WH2_hVASP-like; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR017354; VASP/EVL. DR InterPro; IPR038023; VASP_sf. DR InterPro; IPR014885; VASP_tetra. DR InterPro; IPR000697; WH1/EVH1_dom. DR PANTHER; PTHR11202; SPROUTY-RELATED, EVH1 DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1. DR PANTHER; PTHR11202:SF12; VASODILATOR-STIMULATED PHOSPHOPROTEIN; 1. DR Pfam; PF08776; VASP_tetra; 1. DR Pfam; PF00568; WH1; 1. DR PIRSF; PIRSF038010; Vasodilator_Phospo; 1. DR SMART; SM00461; WH1; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF118370; Vasodilator-stimulated phosphoprotein, VASP, tetramerisation domain; 1. DR PROSITE; PS50229; WH1; 1. DR Genevisible; P70460; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Cell junction; Cell membrane; KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Membrane; KW Phosphoprotein; Reference proteome; Repeat; SH3-binding; Tight junction. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P50552" FT CHAIN 2..375 FT /note="Vasodilator-stimulated phosphoprotein" FT /id="PRO_0000065768" FT DOMAIN 2..113 FT /note="WH1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410" FT REPEAT 340..354 FT /note="1" FT REPEAT 355..369 FT /note="2" FT REGION 111..340 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 221..373 FT /note="EVH2" FT REGION 221..241 FT /note="EVH2 block A" FT REGION 257..274 FT /note="EVH2 block B" FT REGION 338..372 FT /note="EVH2 block C" FT REGION 339..368 FT /note="2 X 15 AA tandem repeats of L-[EQ]-[KR] [MV]-K-[EQ]- FT E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-E" FT COILED 337..367 FT /evidence="ECO:0000255" FT MOTIF 230..233 FT /note="KLKR" FT COMPBIAS 159..186 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 265..290 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 310..333 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P50552" FT MOD_RES 39 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P50552" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50552" FT MOD_RES 153 FT /note="Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK1" FT /evidence="ECO:0000269|PubMed:10882740" FT MOD_RES 235 FT /note="Phosphoserine; by PKA and PKG" FT /evidence="ECO:0000269|PubMed:10882740, FT ECO:0007744|PubMed:21183079" FT MOD_RES 274 FT /note="Phosphothreonine; by PKA, PKG/PRKG1 and AMPK" FT /evidence="ECO:0000250|UniProtKB:P50552" FT MOD_RES 279 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P50552" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50552" FT MOD_RES 311 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P50552" FT MOD_RES 317 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 318 FT /note="Phosphoserine; by AMPK" FT /evidence="ECO:0000269|PubMed:21945940" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VARIANT 209 FT /note="A -> T" FT /evidence="ECO:0000269|PubMed:16141072, FT ECO:0000269|PubMed:8812448" FT MUTAGEN 153 FT /note="S->D: Reduces actin polymerization to a lesser FT extent than wild-type. Greater effect on actin FT polymerization; when associated with D-235 and E-274." FT /evidence="ECO:0000269|PubMed:10882740" FT MUTAGEN 232..233 FT /note="RK->GE,EE: Reduced binding to monomeric actin. No FT VASP-induced actin polymerization." FT /evidence="ECO:0000269|PubMed:12372613" FT MUTAGEN 235 FT /note="S->D: Reduces actin polymerization to a lesser FT extent than wild-type." FT /evidence="ECO:0000269|PubMed:10882740" FT MUTAGEN 274 FT /note="T->E: Reduces actin polymerization to a lesser FT extent than wild-type." FT /evidence="ECO:0000269|PubMed:10882740" FT CONFLICT 106..115 FT /note="Missing (in Ref. 3; BAE42025)" FT /evidence="ECO:0000305" FT CONFLICT 237 FT /note="Missing (in Ref. 3; BAE33933)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="S -> Y (in Ref. 3; BAE29310)" FT /evidence="ECO:0000305" SQ SEQUENCE 375 AA; 39667 MW; 19369286CF4276C7 CRC64; MSETVICSSR ATVMLYDDSN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV VINCAIIRGV KYNQATPIFH QWRDARQVWG LNFGSKEDAI QFATGMANAL EALEGGGPPP APAPPAWSAQ NGPSPEELEQ QKRQPEHMER RVSNAGGPPA PPAGGPPPPP GPPPPPGPPP PPGLPSSGVS GAGHGAGAAP PPAPPLPTAQ GPNSGGSGAP GLAAAIAGAK LRKVSKQEEA SGGPLAPKAE NSRSTGGGLM EEMNAMLARR RKATQVGEKP PKDESASEES EARLPAQSEP VRRPWEKNST TLPRMKSSSS VTTSEAHPST PCSSDDSDLE RVKQELLEEV RKELQKMKEE IIEVFVQELR KRGSP //