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Vasodilator-stimulated phosphoprotein (VASP)

 VASP_MOUSE              Reviewed;         375 AA.
P70460; Q3TAP0; Q3TCD2; Q3U0C2; Q3UDF1; Q91VD2; Q9R214;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
12-SEP-2018, entry version 158.
RecName: Full=Vasodilator-stimulated phosphoprotein;
Short=VASP;
Name=Vasp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-209.
STRAIN=129;
PubMed=8812448; DOI=10.1006/geno.1996.0457;
Zimmer M., Fink T., Fischer L., Hauser W., Scherer K., Lichter P.,
Walter U.;
"Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in
human and mouse: structure, sequence, and chromosomal localization.";
Genomics 36:227-233(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION.
STRAIN=C57BL/6J;
PubMed=10085070; DOI=10.1074/jbc.274.13.8391;
Collins S.P., Uhler M.D.;
"Cyclic AMP- and cyclic GMP-dependent protein kinases differ in their
regulation of cyclic AMP response element-dependent gene
transcription.";
J. Biol. Chem. 274:8391-8404(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-209.
STRAIN=C57BL/6J, and NOD;
TISSUE=Adipose tissue, Bone marrow, Dendritic cell, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=10069337; DOI=10.1016/S0896-6273(00)81092-2;
Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M.,
Macklis J.D., Kwiatkowski D., Soriano P., Gertler F.B.;
"Mena is required for neurulation and commissure formation.";
Neuron 22:313-325(1999).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10660044; DOI=10.1016/S0092-8674(00)81559-7;
Vasioukhin V., Bauer C., Yin M., Fuchs E.;
"Directed actin polymerization is the driving force for epithelial
cell-cell adhesion.";
Cell 100:209-219(2000).
[7]
INTERACTION WITH ACTN1; PFN1; PFN2; VCL AND ZYX, PHOSPHORYLATION AT
SER-153 AND SER-235, AND MUTAGENESIS OF SER-153; SER-235 AND THR-274.
PubMed=10882740; DOI=10.1074/jbc.M005066200;
Harbeck B., Huttelmaier S., Schlueter K., Jockusch B.M.,
Illenberger S.;
"Phosphorylation of the vasodilator-stimulated phosphoprotein
regulates its interaction with actin.";
J. Biol. Chem. 275:30817-30825(2000).
[8]
INTERACTION WITH ACTG1, PHOSPHORYLATION, AND MUTAGENESIS OF
232-ARG-LYS-233.
PubMed=12372613; DOI=10.1016/S0014-5793(02)03356-2;
Walders-Harbeck B., Khaitlina S.Y., Hinssen H., Jockusch B.M.,
Illenberger S.;
"The vasodilator-stimulated phosphoprotein promotes actin
polymerisation through direct binding to monomeric actin.";
FEBS Lett. 529:275-280(2002).
[9]
INTERACTION WITH DNMBP.
PubMed=14506234; DOI=10.1074/jbc.M308104200;
Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
"Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
domains, links dynamin to regulation of the actin cytoskeleton.";
J. Biol. Chem. 278:49031-49043(2003).
[10]
INTERACTION WITH APBB1IP.
PubMed=15642358; DOI=10.1016/j.febslet.2004.10.110;
Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.;
"PREL1 provides a link from Ras signalling to the actin cytoskeleton
via Ena/VASP proteins.";
FEBS Lett. 579:455-463(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-317 AND
SER-320, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
PHOSPHORYLATION AT SER-318.
PubMed=21945940; DOI=10.1016/j.bbrc.2011.09.059;
Thomson D.M., Ascione M.P., Grange J., Nelson C., Hansen M.D.;
"Phosphorylation of VASP by AMPK alters actin binding and occurs at a
novel site.";
Biochem. Biophys. Res. Commun. 414:215-219(2011).
-!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved
in a range of processes dependent on cytoskeleton remodeling and
cell polarity such as axon guidance, lamellipodial and filopodial
dynamics, platelet activation and cell migration. VASP promotes
actin filament elongation. It protects the barbed end of growing
actin filaments against capping and increases the rate of actin
polymerization in the presence of capping protein. VASP stimulates
actin filament elongation by promoting the transfer of profilin-
bound actin monomers onto the barbed end of growing actin
filaments. Plays a role in actin-based mobility of Listeria
monocytogenes in host cells. Regulates actin dynamics in platelets
and plays an important role in regulating platelet aggregation (By
similarity). {ECO:0000250, ECO:0000269|PubMed:10660044}.
-!- SUBUNIT: Homotetramer (By similarity). Interacts with PFN1, PFN2,
LPP, ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the
Pro-rich regions of ZYX. This interaction is important for
targeting to focal adhesions and the formation of actin-rich
structures at the apical surface of cells. Interacts, via the EVH1
domain, with the Pro-rich domain of Listeria monocytogenes actA.
Interacts with APBB1IP. Interacts, via the Pro-rich domain, with
the C-terminal SH3 domain of DNMBP. Interacts weakly with MEFV (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10660044}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10660044}. Cell
junction, focal adhesion {ECO:0000269|PubMed:10660044}. Cell
junction, tight junction {ECO:0000250}. Cell projection,
lamellipodium membrane {ECO:0000269|PubMed:10660044}. Cell
projection, filopodium membrane {ECO:0000269|PubMed:10660044}.
Note=Targeted to stress fibers and focal adhesions through
interaction with a number of proteins including MRL family
members. Localizes to the plasma membrane in protruding
lamellipodia and filopodial tips. Stimulation by thrombin or PMA,
also translocates VASP to focal adhesions. Localized along the
sides of actin filaments throughout the peripheral cytoplasm under
basal conditions (By similarity). In pre-apoptotic cells,
colocalizes with MEFV in large specks (pyroptosomes) (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in thymus and spleen. Lower
levels in lung, ovary, placenta and fat.
{ECO:0000269|PubMed:10069337}.
-!- DEVELOPMENTAL STAGE: Expressed constantly throughout brain
development, with lower levels in adulthood.
{ECO:0000269|PubMed:10069337}.
-!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
thymosin-like domain required for G-actin binding. The KLKR motif
within this block is essential for the G-actin binding and for
actin polymerization. Block B is required for F-actin binding and
subcellular location, and Block C for tetramerization.
-!- DOMAIN: The WH1 domain mediates interaction with XIRP1.
{ECO:0000250}.
-!- PTM: Major substrate for cAMP-dependent (PKA) and cGMP-dependent
protein kinase (PKG) in platelets. The preferred site for PKA is
Ser-153, the preferred site for PKG, Ser-235. In ADP-activated
platelets, phosphorylation by PKA or PKG/PRKG1 on Ser-153 leads to
fibrinogen receptor inhibition. Phosphorylation on Thr-274
requires prior phosphorylation on Ser-153 and Ser-235. In response
to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA.
In response to thrombin, phosphorylated by both PKC and ROCK1.
Phosphorylation at Thr-274 by AMPK does not require prior
phosphorylation at Ser-153 or Ser-235. Phosphorylation at Ser-153
by PKA is required for localization to the tight junctions in
epithelial cells. Phosphorylation modulates F-actin binding, actin
filament elongation and platelet activation. Phosphorylation at
Ser-318 by AMPK also alters actin filament binding. Carbon
monoxide (CO) promotes phosphorylation at Ser-153, while nitric
oxide (NO) promotes phosphorylation at Ser-153, but also at Ser-
235. {ECO:0000269|PubMed:10085070, ECO:0000269|PubMed:10882740,
ECO:0000269|PubMed:12372613, ECO:0000269|PubMed:21945940}.
-!- SIMILARITY: Belongs to the Ena/VASP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA67108.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X98475; CAA67108.1; ALT_SEQ; Genomic_DNA.
EMBL; AF084548; AAD16045.1; -; mRNA.
EMBL; AK140329; BAE24338.1; -; mRNA.
EMBL; AK150103; BAE29310.1; -; mRNA.
EMBL; AK157021; BAE33933.1; -; mRNA.
EMBL; AK170780; BAE42025.1; -; mRNA.
EMBL; AK171715; BAE42628.1; -; mRNA.
EMBL; BC010223; AAH10223.1; -; mRNA.
EMBL; BC015289; AAH15289.1; -; mRNA.
CCDS; CCDS52056.1; -.
RefSeq; NP_001268950.1; NM_001282021.1.
RefSeq; NP_001268951.1; NM_001282022.1.
RefSeq; NP_033525.2; NM_009499.3.
UniGene; Mm.9684; -.
PDB; 2V8C; X-ray; 1.98 A; C=165-184.
PDBsum; 2V8C; -.
ProteinModelPortal; P70460; -.
SMR; P70460; -.
BioGrid; 204499; 4.
DIP; DIP-29360N; -.
IntAct; P70460; 5.
MINT; P70460; -.
STRING; 10090.ENSMUSP00000032561; -.
iPTMnet; P70460; -.
PhosphoSitePlus; P70460; -.
SwissPalm; P70460; -.
EPD; P70460; -.
MaxQB; P70460; -.
PaxDb; P70460; -.
PeptideAtlas; P70460; -.
PRIDE; P70460; -.
Ensembl; ENSMUST00000032561; ENSMUSP00000032561; ENSMUSG00000030403.
GeneID; 22323; -.
KEGG; mmu:22323; -.
UCSC; uc009fle.2; mouse.
CTD; 7408; -.
MGI; MGI:109268; Vasp.
eggNOG; KOG4590; Eukaryota.
eggNOG; ENOG41101TS; LUCA.
GeneTree; ENSGT00730000110272; -.
HOVERGEN; HBG006655; -.
InParanoid; P70460; -.
KO; K06274; -.
OMA; MSETVIC; -.
OrthoDB; EOG091G0QTE; -.
PhylomeDB; P70460; -.
TreeFam; TF321411; -.
Reactome; R-MMU-376176; Signaling by ROBO receptors.
Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
PRO; PR:P70460; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030403; Expressed in 272 organ(s), highest expression level in intestine.
CleanEx; MM_VASP; -.
Genevisible; P70460; MM.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030175; C:filopodium; IDA:MGI.
GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IDA:MGI.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005522; F:profilin binding; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
GO; GO:0007411; P:axon guidance; IGI:MGI.
GO; GO:0001843; P:neural tube closure; IGI:MGI.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:MGI.
GO; GO:0051289; P:protein homotetramerization; IEA:InterPro.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR034367; VASP.
InterPro; IPR017354; VASP/EVL.
InterPro; IPR038023; VASP_sf.
InterPro; IPR014885; VASP_tetra.
InterPro; IPR000697; WH1/EVH1_dom.
PANTHER; PTHR11202:SF12; PTHR11202:SF12; 1.
Pfam; PF08776; VASP_tetra; 1.
Pfam; PF00568; WH1; 1.
PIRSF; PIRSF038010; Vasodilator_Phospo; 1.
SMART; SM00461; WH1; 1.
SUPFAM; SSF118370; SSF118370; 1.
PROSITE; PS50229; WH1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Cell junction;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; SH3-binding; Tight junction.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P50552}.
CHAIN 2 375 Vasodilator-stimulated phosphoprotein.
/FTId=PRO_0000065768.
DOMAIN 2 113 WH1. {ECO:0000255|PROSITE-
ProRule:PRU00410}.
REPEAT 340 354 1.
REPEAT 355 369 2.
REGION 221 373 EVH2.
REGION 221 241 EVH2 block A.
REGION 257 274 EVH2 block B.
REGION 338 372 EVH2 block C.
REGION 339 368 2 X 15 AA tandem repeats of L-[EQ]-[KR]
[MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-
[KRV]-[KQ]-E.
COILED 337 367 {ECO:0000255}.
MOTIF 230 233 KLKR.
COMPBIAS 166 182 Poly-Pro.
COMPBIAS 317 320 Poly-Ser.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 39 39 Phosphotyrosine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 153 153 Phosphoserine; by PKA, PKC, PKG/PRKG1 and
ROCK1. {ECO:0000269|PubMed:10882740}.
MOD_RES 235 235 Phosphoserine; by PKA and PKG.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:10882740}.
MOD_RES 274 274 Phosphothreonine; by PKA, PKG/PRKG1 and
AMPK. {ECO:0000250|UniProtKB:P50552}.
MOD_RES 279 279 N6-acetyllysine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 311 311 Phosphothreonine.
{ECO:0000250|UniProtKB:P50552}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 318 318 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:21945940}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VARIANT 209 209 A -> T. {ECO:0000269|PubMed:16141072,
ECO:0000269|PubMed:8812448}.
MUTAGEN 153 153 S->D: Reduces actin polymerization to a
lesser extent than wild-type. Greater
effect on actin polymerization; when
associated with D-235 and E-274.
{ECO:0000269|PubMed:10882740}.
MUTAGEN 232 233 RK->GE,EE: Reduced binding to monomeric
actin. No VASP-induced actin
polymerization.
{ECO:0000269|PubMed:12372613}.
MUTAGEN 235 235 S->D: Reduces actin polymerization to a
lesser extent than wild-type.
{ECO:0000269|PubMed:10882740}.
MUTAGEN 274 274 T->E: Reduces actin polymerization to a
lesser extent than wild-type.
{ECO:0000269|PubMed:10882740}.
CONFLICT 106 115 Missing (in Ref. 3; BAE42025).
{ECO:0000305}.
CONFLICT 237 237 Missing (in Ref. 3; BAE33933).
{ECO:0000305}.
CONFLICT 337 337 S -> Y (in Ref. 3; BAE29310).
{ECO:0000305}.
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


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