Protein Domain : IPR001452

Type:  Domain Name:  SH3 domain
Description:  SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues [, ]. They are found in a great variety of intracellular or membrane-associated proteins [, , ] for example, in a variety of proteins with enzymatic activity, in adaptor proteins, such as fodrin and yeast actin binding protein ABP-1.The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices. The surface of the SH3-domain bears a flat, hydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions. The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins, altering their subcellular location and mediating the assembly of large multiprotein complexes [].The crystal structure of the SH3 domain of the cytoskeletal protein spectrin, and the solution structures of SH3 domains of phospholipase C (PLC-y) and phosphatidylinositol 3-kinase p85 alpha-subunit, have been determined [, , ]. In spite of relatively limited sequence similarity, their overall structures are similar. The domains belong to the alpha+beta structural class, with 5 to 8 beta-strands forming 2 tightly-packed, anti-parallel beta-sheets arranged in a barrel-like structure, and intervening loops sometimes forming helices. Conserved aliphatic and aromatic residues form a hydrophobic core (A11, L23, A29, V34, W42, L52 and V59 in PLC-y []) and a hydrophobic pocket on the molecular surface (L12, F13, W53 and P55 in PLC-y). The conserved core is believed to stabilise the fold, while the pocket is thought to serve as a binding site for target proteins. Conserved carboxylic amino acids located in the loops, on the periphery of the pocket (D14 and E22), may be involved in protein-protein interactions via proline-rich regions. The N- and C-termini are packed in close proximity, indicating that they are independent structural modules. Short Name:  SH3_domain
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1 Child Features

DB identifier Type Name
IPR029294 Domain Helically-extended SH3 domain

2 Contains

DB identifier Type Name
IPR011511 Domain Variant SH3 domain
IPR013315 Domain Spectrin alpha chain, SH3 domain

6 Cross Referencess

Identifier
PF00018
PF14604
PR00452
PS50002
SM00326
SSF50044

19 Found Ins

DB identifier Type Name
IPR003005 Family Amphiphysin
IPR003017 Family Amphiphysin, isoform 1
IPR003023 Family Amphiphysin 2
IPR016313 Family Disks large 1
IPR016231 Family Mitogen-activated protein (MAP) kinase kinase kinase, MLK1/MLK2/MLK4
IPR016279 Family Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma
IPR017304 Family Cytoplasmic protein NCK
IPR014536 Family Sorting nexin 9 subfamily
IPR014593 Family Uncharacterised conserved protein UCP034961, SH3-2
IPR000919 Family Neutrophil cytosol factor P40
IPR005443 Family Voltage-dependent calcium channel, L-type, beta-1 subunit
IPR005444 Family Voltage-dependent calcium channel, L-type, beta-2 subunit
IPR008079 Family Voltage-dependent calcium channel, L-type, beta-3 subunit
IPR001720 Family PI3 kinase, P85 regulatory subunit
IPR005417 Family Tight junction protein ZO
IPR005420 Family Tight junction protein ZO-3
IPR001655 Family Neutrophil cytosol factor 1
IPR015503 Family Cortactin
IPR015827 Family Alpha-(1,6)-fucosyltransferase, eukaryotic type

1 GO Annotation

GO Term Gene Name
GO:0005515 IPR001452

1 Ontology Annotations

GO Term Gene Name
GO:0005515 IPR001452

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
94776 D8RJB0 PAC:15404199 Selaginella moellendorffii 362  
416473 D8RZE0 PAC:15423192 Selaginella moellendorffii 301  
163731 D8QQ69 PAC:15409871 Selaginella moellendorffii 396  
73493 D8QPC8 PAC:15406961 Selaginella moellendorffii 1058  
164821 D8QRJ8 PAC:15413575 Selaginella moellendorffii 370  
evm.model.supercontig_150.30 PAC:16409484 Carica papaya 400  
evm.model.supercontig_463.4 PAC:16420584 Carica papaya 59  
evm.model.supercontig_8.51 PAC:16426645 Carica papaya 399  
evm.model.supercontig_91.64 PAC:16428521 Carica papaya 1211  
29693.m002083 B9S187 PAC:16806053 Ricinus communis 347  
29827.m002608 B9S1M7 PAC:16810040 Ricinus communis 368  
30018.m000546 B9SAB7 PAC:16815698 Ricinus communis 1201  
30131.m007118 B9RHC4 PAC:16818941 Ricinus communis 371  
Cucsa.109200.1 A0A0A0LPE3 PAC:16959808 Cucumis sativus 375  
Cucsa.357200.1 PAC:16980371 Cucumis sativus 1202  
Cucsa.191610.1 PAC:16967907 Cucumis sativus 382  
Cucsa.212610.1 A0A0A0LUI7 PAC:16969367 Cucumis sativus 348  
orange1.1g042979m A0A067DH54 PAC:18116001 Citrus sinensis 72  
orange1.1g040038m A0A067DI03 PAC:18110872 Citrus sinensis 79  
orange1.1g017467m A0A067GRR0 PAC:18112148 Citrus sinensis 371  
orange1.1g018756m A0A067GH68 PAC:18112149 Citrus sinensis 351  
orange1.1g020634m A0A067GRE1 PAC:18112150 Citrus sinensis 323  
orange1.1g016699m PAC:18110989 Citrus sinensis 384  
orange1.1g018995m PAC:18110991 Citrus sinensis 348  
orange1.1g017347m PAC:18110990 Citrus sinensis 373  
AT4G18060.1 Q8L7W0 PAC:19644168 Arabidopsis thaliana 351  
AT4G34660.2 Q8VWF1 PAC:19646294 Arabidopsis thaliana 345  
AT4G34660.3 Q8VWF1 PAC:19646295 Arabidopsis thaliana 317  
AT4G34660.1 Q8VWF1 PAC:19646293 Arabidopsis thaliana 368  
AT4G39020.1 Q9SVJ1 PAC:19647927 Arabidopsis thaliana 169  

9 Publications

First Author Title Year Journal Volume Pages PubMed ID
            15335710
            7531822
            14731533
            7681365
            7684655
            7953536
            1639195
            1279434
            11256992