| General information | | DisProt: | DP00634 | | Name: | Actin-binding protein | | Synonym(s): | ABP1_YEAST
| | First appeared in release: | Release 5.5 (11/17/2010) | | UniProt: | P15891 | | UniGene: | | | SwissProt: | ABP1_YEAST | | TrEMBL: | | | NCBI (GI): | 113000 | | Source organism: | Saccharomyces cerevisiae (Baker's yeast) | | Sequence length: | 592 | | Percent disordered: | 5% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MALEPIDYTT HSREIDAEYL KIVRGSDPDT TWLIISPNAK KEYEPESTGS SFHDFLQLFD - 60
ETKVQYGLAR VSPPGSDVEK IIIIGWCPDS APLKTRASFA ANFAAVANNL FKGYHVQVTA - 120
RDEDDLDENE LLMKISNAAG ARYSIQTSSK QQGKASTPPV KKSFTPSKSP APVSKKEPVK - 180
TPSPAPAAKI SSRVNDNNDD DDWNEPELKE RDFDQAPLKP NQSSYKPIGK IDLQKVIAEE - 240
KAKEDPRLVQ KPTAAGSKID PSSDIANLKN ESKLKRDSEF NSFLGTTKPP SMTESSLKND - 300
DDKVIKGFRN EKSPAQLWAE RKAKQNSGNA ETKAEAPKPE VPEDEPEGEP DVKDLKSKFE - 360
GLAASEKEEE EMENKFAPPP KKSEPTIISP KPFSKPQEPV KAEEAEQPKT DYKKIGNPLP - 420
GMHIEADNEE EPEENDDDWD DDEDEAAQPP LPSRNVASGA PVQKEEPEQE EIAPSLPSRN - 480
SIPAPKQEEA PEQAPEEEIE EEAEEAAPQL PSRSSAAPPP PPRRATPEKK PKENPWATAE - 540
YDYDAAEDNE LTFVENDKII NIEFVDDDWW LGELEKDGSK GLFPSNYVSL GN
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| Functional narrative |
Regulates ARP2/3 complex-mediated actin assembly. Recruits ARP2/3 complex to sides of preexisting actin filaments, which may promote nucleation or stabilization of filament branches. Binds to actin filaments, but not actin monomers. Actin binding is required for ARP2/3 complex activation. May also have a role in linking the actin cytoskeleton to endocytosis. Recruites components of the endocytotic machinery to cortical actin patches, known sites of endocytosis. (UniProt).
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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 - Extended | | Name: | RT loop of SH3 domain | | Location: | 542 - 556 | | Length: | 15 | | Region sequence: |
DYDAAEDNELTFVEN | | Modification type: | Complex
Fragment
| | PDB: | 1JO8:A, 2RPN:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (283 K; pH: 7; AbpSH3 (15N,13C-labeled, 1:1 with peptide); ArkA (15N,13C-labeled peptide); Na2HPO4 (buffer) 50 mM; NaCl (buffer) 100 mM; EDTA (buffer) 1 mM; NaN3 (buffer) 0.05 %; D2O (buffer) 10 %)
- X-ray crystallography (298 K; pH: 8; Ammonium sulfate; bis-tris-propane)
| References:
- Beltrao P, Serrano L. "Comparative genomics and disorder prediction identify biologically relevant SH3 protein interactions." PLoS Comput. Biol.. 2005; 1(3): e26. PubMed: 16110343
- Fazi B, Cope MJ, Douangamath A, Ferracuti S, Schirwitz K, Zucconi A, Drubin DG, Wilmanns M, Cesareni G, Castagnoli L. "Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis." J. Biol. Chem.. 2001; 277(7): 5290-8. PubMed: 11668184
- Stollar EJ, Garcia B, Chong PA, Rath A, Lin H, Forman-Kay JD, Davidson AR. "Structural, functional, and bioinformatic studies demonstrate the crucial role of an extended peptide binding site for the SH3 domain of yeast Abp1p." J. Biol. Chem.. 2009; 284(39): 26918-27. PubMed: 19590096
| Comments:PDB structure 2RPN is from Stollar, et al. (2009) using solution NMR.
PDB structure 1JO8 from Fazi, et al. (2002) using x-ray crystallography.
Discussion of protein disorder is from Beltrao and Serrano (2005).
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| Region 2 | | Type: | Disordered - Extended | | Name: | N-Src loop of SH3 domain | | Location: | 564 - 569 | | Length: | 6 | | Region sequence: |
FVDDDW | | Modification type: | Complex
Fragment
| | PDB: | 1JO8:A, 2RPN:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (283 K; pH: 7; AbpSH3 (15N,13C-labeled, 1:1 with peptide); ArkA (15N,13C-labeled peptide); D2O (buffer) 10 %; EDTA (buffer) 1 mM; Na2HPO4 (buffer) 50 mM; NaCl (buffer) 100 %; NaN3 (buffer) 0.05 mM)
- X-ray crystallography (298 K; pH: 8; Ammonium sulfate; bis-tris-propane)
| References:
- Beltrao P, Serrano L. "Comparative genomics and disorder prediction identify biologically relevant SH3 protein interactions." PLoS Comput. Biol.. 2005; 1(3): e26. PubMed: 16110343
- Fazi B, Cope MJ, Douangamath A, Ferracuti S, Schirwitz K, Zucconi A, Drubin DG, Wilmanns M, Cesareni G, Castagnoli L. "Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis." J. Biol. Chem.. 2001; 277(7): 5290-8. PubMed: 11668184
- Stollar EJ, Garcia B, Chong PA, Rath A, Lin H, Forman-Kay JD, Davidson AR. "Structural, functional, and bioinformatic studies demonstrate the crucial role of an extended peptide binding site for the SH3 domain of yeast Abp1p." J. Biol. Chem.. 2009; 284(39): 26918-27. PubMed: 19590096
| Comments:PDB structure 2RPN is from Stollar, et al. (2009) using solution NMR.
PDB structure 1JO8 from Fazi, et al. (2002) using x-ray crystallography.
Discussion of protein disorder is from Beltrao and Serrano (2005).
|
| Region 3 | | Type: | Disordered | | Name: | Distal loop of SH3 domain | | Location: | 574 - 580 | | Length: | 7 | | Region sequence: |
LEKDGSK | | Modification type: | Complex
Fragment
| | PDB: | 1JO8:A, 2RPN:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (283 K; pH: 7; AbpSH3 (15N,13C-labeled, 1:1 with peptide); ArkA (15N,13C-labeled peptide); D2O (buffer) 10 %; EDTA (buffer) 1 mM; Na2HPO4 (buffer) 50 mM; NaCl (buffer) 100 mM; NaN3 (buffer) 0.05 %)
- X-ray crystallography (298 K; pH: 8; Ammonium sulfate; bis-tris-propane)
| References:
- Beltrao P, Serrano L. "Comparative genomics and disorder prediction identify biologically relevant SH3 protein interactions." PLoS Comput. Biol.. 2005; 1(3): e26. PubMed: 16110343
- Fazi B, Cope MJ, Douangamath A, Ferracuti S, Schirwitz K, Zucconi A, Drubin DG, Wilmanns M, Cesareni G, Castagnoli L. "Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis." J. Biol. Chem.. 2001; 277(7): 5290-8. PubMed: 11668184
- Stollar EJ, Garcia B, Chong PA, Rath A, Lin H, Forman-Kay JD, Davidson AR. "Structural, functional, and bioinformatic studies demonstrate the crucial role of an extended peptide binding site for the SH3 domain of yeast Abp1p." J. Biol. Chem.. 2009; 284(39): 26918-27. PubMed: 19590096
| Comments:PDB structure 2RPN is from Stollar, et al. (2009) using solution NMR.
PDB structure 1JO8 from Fazi, et al. (2002) using x-ray crystallography.
Discussion of protein disorder is from Beltrao and Serrano (2005).
|
| References |
- Fazi B, Cope MJ, Douangamath A, Ferracuti S, Schirwitz K, Zucconi A, Drubin DG, Wilmanns M, Cesareni G, Castagnoli L. "Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis." J. Biol. Chem.. 2001; 277(7): 5290-8. PubMed: 11668184
- Stollar EJ, Garcia B, Chong PA, Rath A, Lin H, Forman-Kay JD, Davidson AR. "Structural, functional, and bioinformatic studies demonstrate the crucial role of an extended peptide binding site for the SH3 domain of yeast Abp1p." J. Biol. Chem.. 2009; 284(39): 26918-27. PubMed: 19590096
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| Comments |
Sent for AV 10-26-2010 (PubMed: 19590096)
[CorrAU for 19590096 considers DP00634 fully-structured. ~CMM]
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