| General information | | DisProt: | DP00556 | | Name: | Vinculin [Isoform 1] | | Synonym(s): | VINC_CHICK
Metavinculin [Isoform 2]
| | First appeared in release: | Release 4.0 (06/23/2008) | | UniProt: | P12003-1 | | UniGene: | Gga.698 | | SwissProt: | VINC_CHICK | | TrEMBL: | | | NCBI (GI): | 50403716 | | Source organism: | Gallus gallus (Chicken) | | Sequence length: | 1066 | | Percent disordered: | 13% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA VSNLVRVGKE - 60
TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY SVPARDYLID GSRGILSGTS - 120
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ - 180
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE - 240
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR - 300
QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM QKAQQVSQGL - 360
DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG GSEGEEHIRG IMSEARKVAE - 420
LCEEPKERDD ILRSLGEISA LTAKLSDLRR HGKGDSPEAR ALAKQIATSL QNLQSKTNRA - 480
VANTRPVKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD - 540
LLAKCDRVDQ LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS - 600
DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV GTANKTTVEG - 660
IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK - 720
SLLDASEEAI KKDLDKCKVA MANMQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR - 780
EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP - 840
DFPPPPPDLE HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM - 900
AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGNKRALIQC AKDIAKASDE - 960
VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISDEESEQAT - 1020
EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLRWVR KTPWYQ
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| Functional narrative |
Cytoskeleton protein, which is involved in the activation and attachment of integrins to the actin cytoskeleton. Vinculin binds beta-integrins through viniculin binding sites (VBS's) located on a talin rod, which is located within the hydrophobic core of the protein. Binding of beta-integrins requires a large structural change at helix 2, which unfolds to a random coil (755-789) upon binding with a vinculin head (Vh'). Involved in cell adhesion. May be involved in the attachment of the actin-based microfilaments to the plasma membrane. May also play important roles in cell morphology and locomotion.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Helix 2 | | Location: | 755 - 889 | | Length: | 135 | | Region sequence: |
SIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQ
KSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEHLHLTDELAPPKPPLPEGEVPPPR
PPPPEEKDEEFPEQK | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via an order to disorder transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Apoptosis Regulation
Substrate/ligand binding
| Detection methods:
| References:
- Fillingham I, Gingras AR, Papagrigoriou E, Patel B, Emsley J, Critchley DR, Roberts GC, Barsukov IL. "A Vinculin Binding Domain from the Talin Rod Unfolds to Form a Complex with the Vinculin Head." Structure. 2005; 13(1): 65-74. PubMed: 15642262
| Comments:
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| References |
- Borgon RA, Vonrhein C, Bricogne G, Bois PR, Izard T. "Crystal structure of human vinculin." Structure. 2004; 12(7): 1189-97. PubMed: 15242595
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