ID   VINC_CHICK              Reviewed;        1135 AA.
AC   P12003; Q91024;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Vinculin;
DE   AltName: Full=Metavinculin;
GN   Name=VCL; Synonyms=VINC1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=3141928; DOI=10.1073/pnas.85.22.8535;
RA   Coutu M.D., Craig S.W.;
RT   "cDNA-derived sequence of chicken embryo vinculin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:8535-8539(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=2497736; DOI=10.1042/bj2590453;
RA   Price G.J., Jones P., Davison M.D., Patel B., Bendori R., Geiger B.,
RA   Critchley D.R.;
RT   "Primary sequence and domain structure of chicken vinculin.";
RL   Biochem. J. 259:453-461(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RX   PubMed=1618784; DOI=10.1016/s0021-9258(18)42353-8;
RA   Byrne B.J., Kaczorowski Y.J., Coutu M.D., Craig S.W.;
RT   "Chicken vinculin and meta-vinculin are derived from a single gene by
RT   alternative splicing of a 207-base pair exon unique to meta-vinculin.";
RL   J. Biol. Chem. 267:12845-12850(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-881.
RC   TISSUE=Embryo;
RX   PubMed=3117046; DOI=10.1042/bj2450595;
RA   Price G.J., Jones P., Davison M.D., Patel B., Eperon I.C., Critchley D.R.;
RT   "Isolation and characterization of a vinculin cDNA from chick-embryo
RT   fibroblasts.";
RL   Biochem. J. 245:595-603(1987).
RN   [5]
RP   ACETYLATION.
RX   PubMed=3030822; DOI=10.1016/0014-5793(87)81536-3;
RA   Kellie S., Wigglesworth N.M.;
RT   "The cytoskeletal protein vinculin is acylated by myristic acid.";
RL   FEBS Lett. 213:428-432(1987).
RN   [6]
RP   TALIN INTERACTION DOMAIN.
RX   PubMed=2512301; DOI=10.1083/jcb.109.6.2917;
RA   Jones P., Jackson P., Price G.J., Patel B., Ohanion V., Lear A.L.,
RA   Critchley D.R.;
RT   "Identification of a talin binding site in the cytoskeletal protein
RT   vinculin.";
RL   J. Cell Biol. 109:2917-2927(1989).
RN   [7]
RP   INTERACTION WITH NRAP.
RX   PubMed=10320340; DOI=10.1021/bi982395t;
RA   Luo G., Herrera A.H., Horowits R.;
RT   "Molecular interactions of N-RAP, a nebulin-related protein of striated
RT   muscle myotendon junctions and intercalated disks.";
RL   Biochemistry 38:6135-6143(1999).
RN   [8]
RP   PHOSPHORYLATION AT TYR-100 AND TYR-1134, FUNCTION, AND MUTAGENESIS OF
RP   TYR-100; TYR-160; TYR-537; TYR-692; TYR-822 AND TYR-1134.
RX   PubMed=15229287; DOI=10.1091/mbc.e04-03-0264;
RA   Zhang Z., Izaguirre G., Lin S.-Y., Lee H.Y., Schaefer E., Haimovich B.;
RT   "The phosphorylation of vinculin on tyrosine residues 100 and 1065,
RT   mediated by SRC kinases, affects cell spreading.";
RL   Mol. Biol. Cell 15:4234-4247(2004).
RN   [9]
RP   INTERACTION WITH TLN1.
RX   PubMed=20610383; DOI=10.1074/jbc.m109.095455;
RA   Gingras A.R., Bate N., Goult B.T., Patel B., Kopp P.M., Emsley J.,
RA   Barsukov I.L., Roberts G.C., Critchley D.R.;
RT   "Central region of talin has a unique fold that binds vinculin and actin.";
RL   J. Biol. Chem. 285:29577-29587(2010).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20584916; DOI=10.1083/jcb.201001149;
RA   le Duc Q., Shi Q., Blonk I., Sonnenberg A., Wang N., Leckband D.,
RA   de Rooij J.;
RT   "Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-
RT   anchored sites within adherens junctions in a myosin II-dependent manner.";
RL   J. Cell Biol. 189:1107-1115(2010).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNB1.
RX   PubMed=20086044; DOI=10.1242/jcs.056432;
RA   Peng X., Cuff L.E., Lawton C.D., DeMali K.A.;
RT   "Vinculin regulates cell-surface E-cadherin expression by binding to beta-
RT   catenin.";
RL   J. Cell Sci. 123:567-577(2010).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 881-1135 OF ISOFORM 1.
RX   PubMed=10612396; DOI=10.1016/s0092-8674(00)81549-4;
RA   Bakolitsa C., de Pereda J.M., Bagshaw C.R., Critchley D.R.,
RA   Liddington R.C.;
RT   "Crystal structure of the vinculin tail suggests a pathway for
RT   activation.";
RL   Cell 99:603-613(1999).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-259 IN COMPLEX WITH APBB1IP, AND
RP   INTERACTION WITH TLN1 AND APBB1IP.
RX   PubMed=23389036; DOI=10.1074/jbc.m112.438119;
RA   Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R.,
RA   Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R., Barsukov I.L.;
RT   "RIAM and vinculin binding to talin are mutually exclusive and regulate
RT   adhesion assembly and turnover.";
RL   J. Biol. Chem. 288:8238-8249(2013).
CC   -!- FUNCTION: Actin filament (F-actin)-binding protein involved in cell-
CC       matrix adhesion and cell-cell adhesion. Regulates cell-surface E-
CC       cadherin expression and potentiates mechanosensing by the E-cadherin
CC       complex. May also play important roles in cell morphology and
CC       locomotion. {ECO:0000269|PubMed:15229287, ECO:0000269|PubMed:20086044,
CC       ECO:0000269|PubMed:20584916}.
CC   -!- SUBUNIT: Exhibits self-association properties. Interacts with APBB1IP,
CC       NRAP and TLN1. Interacts with CTNNB1 and this interaction is necessary
CC       for its localization to the cell-cell junctions and for its function in
CC       regulating cell surface expression of E-cadherin.
CC       {ECO:0000269|PubMed:10320340, ECO:0000269|PubMed:20086044,
CC       ECO:0000269|PubMed:20610383, ECO:0000269|PubMed:23389036}.
CC   -!- INTERACTION:
CC       P12003; P05094-2: ACTN1; NbExp=5; IntAct=EBI-1039563, EBI-6049246;
CC       P12003; P49024: PXN; NbExp=5; IntAct=EBI-1039563, EBI-2896280;
CC       P12003; P26039: Tln1; Xeno; NbExp=5; IntAct=EBI-1039563, EBI-1039593;
CC       P12003; P50552: VASP; Xeno; NbExp=2; IntAct=EBI-1039563, EBI-748201;
CC       P12003-1; P49024: PXN; NbExp=2; IntAct=EBI-6138078, EBI-2896280;
CC       P12003-1; P68135: ACTA1; Xeno; NbExp=2; IntAct=EBI-6138078, EBI-367540;
CC       P12003-2; P49024: PXN; NbExp=2; IntAct=EBI-6138096, EBI-2896280;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20584916};
CC       Peripheral membrane protein {ECO:0000305|PubMed:20584916}; Cytoplasmic
CC       side {ECO:0000305|PubMed:20584916}. Cell junction, adherens junction
CC       {ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20584916}. Cell
CC       junction, focal adhesion {ECO:0000269|PubMed:20086044}. Cytoplasm,
CC       cytoskeleton {ECO:0000250|UniProtKB:P85972}. Cell membrane, sarcolemma
CC       {ECO:0000250|UniProtKB:Q64727}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q64727}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q64727}. Cell projection, podosome
CC       {ECO:0000250|UniProtKB:Q64727}. Note=Recruitment to cell-cell junctions
CC       occurs in a myosin II-dependent manner (PubMed:20584916). Interaction
CC       with CTNNB1 is necessary for its localization to the cell-cell
CC       junctions (PubMed:20086044). {ECO:0000269|PubMed:20086044,
CC       ECO:0000269|PubMed:20584916}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=Metavinculin;
CC         IsoId=P12003-2; Sequence=Displayed;
CC       Name=1; Synonyms=Vinculin;
CC         IsoId=P12003-1; Sequence=VSP_010772;
CC   -!- TISSUE SPECIFICITY: Isoform Metavinculin is muscle-specific.
CC   -!- DOMAIN: Exists in at least two conformations. When in the closed,
CC       'inactive' conformation, extensive interactions between the head and
CC       tail domains prevent detectable binding to most of its ligands. It
CC       takes on an 'active' conformation after cooperative and simultaneous
CC       binding of two different ligands. This activation involves displacement
CC       of the head-tail interactions and leads to a significant accumulation
CC       of ternary complexes. The active form then binds a number of proteins
CC       that have both signaling and structural roles that are essential for
CC       cell adhesion. {ECO:0000250|UniProtKB:P18206}.
CC   -!- DOMAIN: The N-terminal globular head (Vh) comprises of subdomains D1-
CC       D4. The C-terminal tail (Vt) binds F-actin and cross-links actin
CC       filaments into bundles. An intramolecular interaction between Vh and Vt
CC       masks the F-actin-binding domain located in Vt. The binding of talin
CC       and alpha-actinin to the D1 subdomain of vinculin induces a helical
CC       bundle conversion of this subdomain, leading to the disruption of the
CC       intramolecular interaction and the exposure of the cryptic F-actin-
CC       binding domain of Vt. Vt inhibits actin filament barbed end elongation
CC       without affecting the critical concentration of actin assembly.
CC       {ECO:0000250|UniProtKB:P18206}.
CC   -!- PTM: Phosphorylated; on serines, threonines and tyrosines.
CC       Phosphorylation on Tyr-1134 in activated platelets affects head-tail
CC       interactions and cell spreading but has no effect on actin binding nor
CC       on localization to focal adhesion plaques.
CC       {ECO:0000269|PubMed:15229287}.
CC   -!- PTM: Acetylated; mainly by myristic acid but also by a small amount of
CC       palmitic acid. {ECO:0000269|PubMed:3030822}.
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC       {ECO:0000305}.
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DR   EMBL; J04126; AAA49136.1; -; mRNA.
DR   EMBL; M87837; AAA49135.1; -; Genomic_DNA.
DR   EMBL; Y00312; CAA68412.1; -; mRNA.
DR   PIR; A31346; A29997.
DR   RefSeq; NP_990772.1; NM_205441.1. [P12003-1]
DR   RefSeq; XP_015143689.1; XM_015288203.1. [P12003-2]
DR   PDB; 1QKR; X-ray; 1.80 A; A/B=879-1135.
DR   PDB; 1ST6; X-ray; 3.10 A; A=1-1135.
DR   PDB; 1T01; X-ray; 2.06 A; A=1-254.
DR   PDB; 1U6H; X-ray; 2.38 A; A=1-259.
DR   PDB; 1XWJ; X-ray; 2.60 A; A=2-259.
DR   PDB; 1ZVZ; X-ray; 1.80 A; A=2-259.
DR   PDB; 1ZW2; X-ray; 2.10 A; A=2-259.
DR   PDB; 1ZW3; X-ray; 3.30 A; A=2-259.
DR   PDB; 2GDC; X-ray; 2.74 A; A=1-266.
DR   PDB; 3JBI; EM; 8.50 A; V=879-1130.
DR   PDB; 3ZDL; X-ray; 2.30 A; A=1-259.
DR   PDB; 4E17; X-ray; 2.30 A; A=1-259.
DR   PDB; 4E18; X-ray; 2.40 A; A=1-259.
DR   PDB; 6FQ4; X-ray; 2.89 A; A=1-259.
DR   PDB; 6NR7; X-ray; 3.00 A; A=1-1135.
DR   PDBsum; 1QKR; -.
DR   PDBsum; 1ST6; -.
DR   PDBsum; 1T01; -.
DR   PDBsum; 1U6H; -.
DR   PDBsum; 1XWJ; -.
DR   PDBsum; 1ZVZ; -.
DR   PDBsum; 1ZW2; -.
DR   PDBsum; 1ZW3; -.
DR   PDBsum; 2GDC; -.
DR   PDBsum; 3JBI; -.
DR   PDBsum; 3ZDL; -.
DR   PDBsum; 4E17; -.
DR   PDBsum; 4E18; -.
DR   PDBsum; 6FQ4; -.
DR   PDBsum; 6NR7; -.
DR   AlphaFoldDB; P12003; -.
DR   EMDB; EMD-6446; -.
DR   EMDB; EMD-6449; -.
DR   EMDB; EMD-6450; -.
DR   EMDB; EMD-6451; -.
DR   SMR; P12003; -.
DR   BioGRID; 676671; 2.
DR   DIP; DIP-35191N; -.
DR   ELM; P12003; -.
DR   IntAct; P12003; 16.
DR   MINT; P12003; -.
DR   STRING; 9031.ENSGALP00000008131; -.
DR   iPTMnet; P12003; -.
DR   PaxDb; 9031-ENSGALP00000008131; -.
DR   DNASU; 396422; -.
DR   Ensembl; ENSGALT00000008145; ENSGALP00000008131; ENSGALG00000005079. [P12003-2]
DR   Ensembl; ENSGALT00010054688.1; ENSGALP00010033042.1; ENSGALG00010022474.1. [P12003-2]
DR   Ensembl; ENSGALT00015023046; ENSGALP00015013321; ENSGALG00015009482. [P12003-2]
DR   GeneID; 396422; -.
DR   KEGG; gga:396422; -.
DR   CTD; 7414; -.
DR   VEuPathDB; HostDB:geneid_396422; -.
DR   eggNOG; KOG3681; Eukaryota.
DR   GeneTree; ENSGT01030000234543; -.
DR   HOGENOM; CLU_012338_0_0_1; -.
DR   InParanoid; P12003; -.
DR   PhylomeDB; P12003; -.
DR   Reactome; R-GGA-114608; Platelet degranulation.
DR   Reactome; R-GGA-445355; Smooth Muscle Contraction.
DR   Reactome; R-GGA-5674135; MAP2K and MAPK activation.
DR   Reactome; R-GGA-6798695; Neutrophil degranulation.
DR   SABIO-RK; P12003; -.
DR   EvolutionaryTrace; P12003; -.
DR   PRO; PR:P12003; -.
DR   Proteomes; UP000000539; Chromosome 6.
DR   Bgee; ENSGALG00000005079; Expressed in colon and 14 other cell types or tissues.
DR   ExpressionAtlas; P12003; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:AgBase.
DR   GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR   GO; GO:0005903; C:brush border; IDA:AgBase.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0044291; C:cell-cell contact zone; IBA:GO_Central.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0043034; C:costamere; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IDA:AgBase.
DR   GO; GO:0090637; C:inner dense plaque of desmosome; IDA:AgBase.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005927; C:muscle tendon junction; IDA:AgBase.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:AgBase.
DR   GO; GO:0090636; C:outer dense plaque of desmosome; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR   GO; GO:0061826; C:podosome ring; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0042383; C:sarcolemma; IDA:AgBase.
DR   GO; GO:0098723; C:skeletal muscle myofibril; IDA:AgBase.
DR   GO; GO:0001725; C:stress fiber; IDA:AgBase.
DR   GO; GO:1990357; C:terminal web; IDA:AgBase.
DR   GO; GO:0030018; C:Z disc; IDA:AgBase.
DR   GO; GO:0005915; C:zonula adherens; IDA:AgBase.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0051393; F:alpha-actinin binding; IDA:AgBase.
DR   GO; GO:0045294; F:alpha-catenin binding; IDA:BHF-UCL.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR   GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL.
DR   GO; GO:0002162; F:dystroglycan binding; IEA:Ensembl.
DR   GO; GO:0051371; F:muscle alpha-actinin binding; IMP:AgBase.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:AgBase.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0017166; F:vinculin binding; IDA:AgBase.
DR   GO; GO:0034333; P:adherens junction assembly; IDA:BHF-UCL.
DR   GO; GO:0043297; P:apical junction assembly; IEA:Ensembl.
DR   GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IDA:BHF-UCL.
DR   GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR   GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
DR   GO; GO:0051893; P:regulation of focal adhesion assembly; IEA:Ensembl.
DR   GO; GO:1904702; P:regulation of protein localization to adherens junction; IEA:Ensembl.
DR   Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 3.
DR   Gene3D; 1.20.120.810; Vinculin, Vh2 four-helix bundle; 3.
DR   InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR   InterPro; IPR017997; Vinculin.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   InterPro; IPR000633; Vinculin_CS.
DR   PANTHER; PTHR46180; VINCULIN; 1.
DR   PANTHER; PTHR46180:SF1; VINCULIN; 1.
DR   Pfam; PF01044; Vinculin; 1.
DR   PRINTS; PR00806; VINCULIN.
DR   SUPFAM; SSF47220; alpha-catenin/vinculin-like; 8.
DR   PROSITE; PS00663; VINCULIN_1; 1.
DR   PROSITE; PS00664; VINCULIN_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cell adhesion;
KW   Cell junction; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW   Lipoprotein; Membrane; Myristate; Palmitate; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P26234"
FT   CHAIN           2..1135
FT                   /note="Vinculin"
FT                   /id="PRO_0000064255"
FT   REPEAT          259..369
FT                   /note="1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          370..479
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          480..589
FT                   /note="3"
FT                   /evidence="ECO:0000255"
FT   REGION          2..835
FT                   /note="N-terminal globular head"
FT                   /evidence="ECO:0000250|UniProtKB:P18206"
FT   REGION          168..208
FT                   /note="Talin-interaction"
FT                   /evidence="ECO:0000269|PubMed:2512301"
FT   REGION          259..589
FT                   /note="3 X 112 AA tandem repeats"
FT                   /evidence="ECO:0000255"
FT   REGION          836..878
FT                   /note="Linker (Pro-rich)"
FT                   /evidence="ECO:0000250|UniProtKB:P18206"
FT   REGION          837..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..1135
FT                   /note="C-terminal tail"
FT                   /evidence="ECO:0000250|UniProtKB:P18206"
FT   REGION          1004..1047
FT                   /note="Facilitates phospholipid membrane insertion"
FT                   /evidence="ECO:0000250|UniProtKB:Q64727"
FT   REGION          1121..1135
FT                   /note="Facilitates phospholipid membrane insertion"
FT                   /evidence="ECO:0000250|UniProtKB:Q64727"
FT   COMPBIAS        859..873
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..888
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         100
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:15229287"
FT   MOD_RES         537
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         822
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P18206"
FT   MOD_RES         1134
FT                   /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT                   /evidence="ECO:0000269|PubMed:15229287"
FT   VAR_SEQ         916..984
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:2497736,
FT                   ECO:0000303|PubMed:3141928"
FT                   /id="VSP_010772"
FT   MUTAGEN         100
FT                   /note="Y->F: Some reduction of phosphorylation levels in
FT                   platelets. Little change in cell spreading. Complete loss
FT                   of phosphorylation. No change in subcellular location nor
FT                   on in vitro actin binding. 40% decrease in cell spreading;
FT                   when associated with F-1134."
FT                   /evidence="ECO:0000269|PubMed:15229287"
FT   MUTAGEN         160
FT                   /note="Y->F: No change of phosphorylation levels in
FT                   platelets."
FT                   /evidence="ECO:0000269|PubMed:15229287"
FT   MUTAGEN         537
FT                   /note="Y->F: No change of phosphorylation levels in
FT                   platelets."
FT                   /evidence="ECO:0000269|PubMed:15229287"
FT   MUTAGEN         692
FT                   /note="Y->F: No change of phosphorylation levels in
FT                   platelets."
FT                   /evidence="ECO:0000269|PubMed:15229287"
FT   MUTAGEN         822
FT                   /note="Y->F: No change of phosphorylation levels in
FT                   platelets."
FT                   /evidence="ECO:0000269|PubMed:15229287"
FT   MUTAGEN         1134
FT                   /note="Y->F: Greatly reduced phosphorylation levels in
FT                   platelets. Little change in cell spreading. Complete loss
FT                   of phosphorylation. No change in subcellular location nor
FT                   on in vitro actin binding. 40% decrease in cell spreading;
FT                   when associated with F-100."
FT                   /evidence="ECO:0000269|PubMed:15229287"
FT   CONFLICT        442..447
FT                   /note="TAKLSD -> QLSCQI (in Ref. 2 and 4; CAA68412)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        701
FT                   /note="Q -> H (in Ref. 2 and 4; CAA68412)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        880
FT                   /note="E -> K (in Ref. 4; CAA68412)"
FT                   /evidence="ECO:0000305"
FT   HELIX           7..28
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   TURN            29..32
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   HELIX           41..63
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   HELIX           68..73
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   HELIX           75..97
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   HELIX           102..146
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:3ZDL"
FT   HELIX           154..181
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   HELIX           185..215
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   STRAND          218..221
FT                   /evidence="ECO:0007829|PDB:1T01"
FT   HELIX           222..249
FT                   /evidence="ECO:0007829|PDB:1ZVZ"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:3ZDL"
FT   HELIX           258..276
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           278..280
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           282..285
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   STRAND          292..296
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           297..311
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           316..340
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           347..396
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   TURN            403..405
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           406..420
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           425..450
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   TURN            451..454
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   TURN            457..460
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           461..482
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           493..501
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   TURN            509..513
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           514..530
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           535..560
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           566..569
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           572..598
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           604..614
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           622..650
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           655..684
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           690..714
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           719..741
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   TURN            742..744
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           747..751
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   STRAND          752..754
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           755..773
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           777..791
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           795..797
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   TURN            799..804
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           811..814
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           817..835
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   STRAND          864..866
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   STRAND          887..890
FT                   /evidence="ECO:0007829|PDB:1ST6"
FT   STRAND          892..894
FT                   /evidence="ECO:0007829|PDB:1ST6"
FT   HELIX           896..910
FT                   /evidence="ECO:0007829|PDB:6NR7"
FT   HELIX           961..964
FT                   /evidence="ECO:0007829|PDB:1QKR"
FT   HELIX           966..978
FT                   /evidence="ECO:0007829|PDB:1QKR"
FT   HELIX           987..1005
FT                   /evidence="ECO:0007829|PDB:1QKR"
FT   HELIX           1010..1012
FT                   /evidence="ECO:0007829|PDB:1QKR"
FT   HELIX           1013..1040
FT                   /evidence="ECO:0007829|PDB:1QKR"
FT   HELIX           1044..1054
FT                   /evidence="ECO:0007829|PDB:1QKR"
FT   HELIX           1057..1074
FT                   /evidence="ECO:0007829|PDB:1QKR"
FT   STRAND          1075..1077
FT                   /evidence="ECO:0007829|PDB:1ST6"
FT   HELIX           1082..1113
FT                   /evidence="ECO:0007829|PDB:1QKR"
FT   HELIX           1121..1123
FT                   /evidence="ECO:0007829|PDB:1QKR"
SQ   SEQUENCE   1135 AA;  124560 MW;  28CC2699C9511058 CRC64;
     MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA VSNLVRVGKE
     TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY SVPARDYLID GSRGILSGTS
     DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ
     ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE
     INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR
     QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM QKAQQVSQGL
     DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG GSEGEEHIRG IMSEARKVAE
     LCEEPKERDD ILRSLGEISA LTAKLSDLRR HGKGDSPEAR ALAKQIATSL QNLQSKTNRA
     VANTRPVKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD
     LLAKCDRVDQ LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS
     DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV GTANKTTVEG
     IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK
     SLLDASEEAI KKDLDKCKVA MANMQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
     EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP
     DFPPPPPDLE HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM
     AARQLHDEAR KWSSKPVTVI NEAAEAGVDI DEEDDADVEF SLPSDIEDDY EPELLLMPTN
     QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA EMSRLVRGGS GNKRALIQCA
     KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL LQVCERIPTI STQLKILSTV KATMLGRTNI
     SDEESEQATE MLVHNAQNLM QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ
//