VASP_MOUSE
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 03-AUG-2022, entry version 178.
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, Pancreas,
RC 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};
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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; 7.
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; P70460; -.
DR PeptideAtlas; P70460; -.
DR PRIDE; P70460; -.
DR ProteomicsDB; 300166; -.
DR Antibodypedia; 1491; 1135 antibodies from 46 providers.
DR DNASU; 22323; -.
DR Ensembl; ENSMUST00000032561; ENSMUSP00000032561; ENSMUSG00000030403.
DR GeneID; 22323; -.
DR KEGG; mmu:22323; -.
DR UCSC; uc009fle.2; mouse.
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; 972128at2759; -.
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 72 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 247 other tissues.
DR Genevisible; P70460; MM.
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 Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR034367; VASP.
DR InterPro; IPR017354; VASP/EVL.
DR InterPro; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR PANTHER; PTHR11202:SF12; PTHR11202:SF12; 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; SSF118370; SSF118370; 1.
DR PROSITE; PS50229; WH1; 1.
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
