DP00167: Ras-related protein Rap-2aFASTA viewXML view

General information
DisProt:DP00167
Name:Ras-related protein Rap-2a
Synonym(s):RAP2A_HUMAN
RbBP-30
RAP2A
First appeared in release:Release 2.1 (03/14/2005)
UniProt:P10114
UniGene:Hs.508480
SwissProt: RAP2A_HUMAN
TrEMBL:  
NCBI (GI): 131852
Source organism:Homo sapiens (Human)
Sequence length:183
Percent disordered:13%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG - 60
TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYEKVP VILVGNKVDL - 120
ESEREVSSSE GRALAEEWGC PFMETSAKSK TMVDELFAEI VRQMNYAAQP DKDDPCCSAC - 180
NIQ



Functional narrative    

Rap2A is a member the small GTPase super family and the Ras family. Rap2A is involved with multiple signal transduction cascades that regulate cell growth and differentiation. Rap2A cycles between the binding partners GDP and GTP with the assistance of guanine nucleotide exchange factors and GTPase activating proteins. Switches I and II in this protein undergo conformational changes depending upon the partner bound. L3, a loop located between two beta sheets is consistently disordered and functions as a linker or hinge region to assist in binding and overall flexibility of this protein.

Region 1: 32-36 Region 2: 45-55 Region 3: 60-63 Region 4: 62-63 Region 5: 62-66

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.


Region 1
Type:Disordered - Extended
Name:Switch I
Location:32 - 36
Length:5
Region sequence:

YDPTI

Modification type: Complex
Fragment
PDB: 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (pH: 7.5; protein (per mL) 10 mg; PEG 4000 19 %; magnesium chloride 100 mM; Tris 100 mM)

References:
  1. Cherfils J, Menetrey J, Le Bras G, Janoueix-Lerosey I, de Gunzburg J, Garel JR, Auzat I. "Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgammaS." EMBO J. 1997; 16(18): 5582-91. PubMed: 9312017

Comments:
 



Region 2
Type:Disordered - Extended
Name:L3 Loop
Location:45 - 55
Length:11
Region sequence:

EVDSSPSVLEI

Modification type: Complex
Fragment
Native
PDB: 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S
Structural/functional type: Function arises from the disordered state
Functional classes: Entropic chain
Functional subclasses: Flexible linkers/spacers
Detection methods:
  1. X-ray crystallography (pH: 8; LiSO4 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)

  2. X-ray crystallography (pH: 8; MgCl2 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)

References:
  1. Menetrey J, Cherfils J. "Structure of the small G protein Rap2 in a non-catalytic complex with GTP." Proteins. 1999; 37(3): 465-473. PubMed: 10591105

Comments:
 



Region 3
Type:Disordered - Extended
Name:Switch II
Location:60 - 63
Length:4
Region sequence:

GTEQ

Modification type: Complex
Fragment
PDB: 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (pH: 7.5; magnesium chloride 100 mM; PEG 4000 19 %; protein (per mL) 10 mg; Tris 100 mM)

References:
  1. Cherfils J, Menetrey J, Le Bras G, Janoueix-Lerosey I, de Gunzburg J, Garel JR, Auzat I. "Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgammaS." EMBO J. 1997; 16(18): 5582-91. PubMed: 9312017

Comments:
 



Region 4
Type:Disordered - Extended
Name:Switch II
Location:62 - 63
Length:2
Region sequence:

EQ

Modification type: Complex
Fragment
Native
PDB: 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (pH: 8; LiSO4 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)

  2. X-ray crystallography (pH: 8; MgCl2 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)

References:
  1. Menetrey J, Cherfils J. "Structure of the small G protein Rap2 in a non-catalytic complex with GTP." Proteins. 1999; 37(3): 465-473. PubMed: 10591105

Comments:
 



Region 5
Type:Disordered - Extended
Name:Switch II
Location:62 - 66
Length:5
Region sequence:

EQFAS

Modification type: Complex
Fragment
Native
PDB: 1KAO:A, 2RAP:A, 3RAP:R, 3RAP:S
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (pH: 8; LiSO4 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)

  2. X-ray crystallography (pH: 8; MgCl2 100 mM; PEG 8000 (20-25%); Tris/HCl 100 mM)

References:
  1. Menetrey J, Cherfils J. "Structure of the small G protein Rap2 in a non-catalytic complex with GTP." Proteins. 1999; 37(3): 465-473. PubMed: 10591105

Comments:
 


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