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Conserved domains on  [gi|506325748|ref|NP_001265164|]
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LIM and cysteine-rich domains protein 1 isoform 4 [Homo sapiens]

Protein Classification

PET_testin domain-containing protein( domain architecture ID 10177008)

PET_testin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PET_testin cd09829
The PET domain of Testin; The PET domain of Testin: Testin contains a PET domain at the ...
 116-203 1.40e-53

The PET domain of Testin; The PET domain of Testin: Testin contains a PET domain at the N-terminus and three C-terminal LIM domains. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and is involved in cell motility and adhesion events. Knockout mice experiments reveal a tumor repressor function of Testin. The PET domain is a protein-protein interaction domain and is usually found in conjunction with LIM domain, which is also involved in protein-protein interactions. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes.


:

Pssm-ID: 193604  Cd Length: 88  Bit Score: 167.81  E-value: 1.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506325748 116 ITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALG 195
Cdd:cd09829    1 VTYEWAPPGVTQELARYYMELLPKEKQPIAGSEGAQYRKKQLQKQLPLHDQDPSLCHELSENEVKQMEQFVKKYKEEALG 80


                 ....*...
gi 506325748 196 VGEVALPG 203
Cdd:cd09829   81 VGKVIEPG 88
 
Name Accession Description Interval E-value
PET_testin cd09829
The PET domain of Testin; The PET domain of Testin: Testin contains a PET domain at the ...
 116-203 1.40e-53

The PET domain of Testin; The PET domain of Testin: Testin contains a PET domain at the N-terminus and three C-terminal LIM domains. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and is involved in cell motility and adhesion events. Knockout mice experiments reveal a tumor repressor function of Testin. The PET domain is a protein-protein interaction domain and is usually found in conjunction with LIM domain, which is also involved in protein-protein interactions. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 193604  Cd Length: 88  Bit Score: 167.81  E-value: 1.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506325748 116 ITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALG 195
Cdd:cd09829    1 VTYEWAPPGVTQELARYYMELLPKEKQPIAGSEGAQYRKKQLQKQLPLHDQDPSLCHELSENEVKQMEQFVKKYKEEALG 80


                 ....*...
gi 506325748 196 VGEVALPG 203
Cdd:cd09829   81 VGKVIEPG 88
PET pfam06297
PET Domain; This domain is suggested to be involved in protein-protein interactions. The ...
 116-200 3.65e-49

PET Domain; This domain is suggested to be involved in protein-protein interactions. The family is found in conjunction with pfam00412.


Pssm-ID: 461872  Cd Length: 85  Bit Score: 156.25  E-value: 3.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506325748  116 ITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALG 195
Cdd:pfam06297   1 ETYEWVPPGLTPELVHQYMECLPEEKVPVVGSEGAKYRKKQLLKQLPPHDQDPSYCHGLSEEEVKEMEDFVKQRKEEALG 80


                  ....*
gi 506325748  196 VGEVA 200
Cdd:pfam06297  81 VGEVK 85
 
Name Accession Description Interval E-value
PET_testin cd09829
The PET domain of Testin; The PET domain of Testin: Testin contains a PET domain at the ...
 116-203 1.40e-53

The PET domain of Testin; The PET domain of Testin: Testin contains a PET domain at the N-terminus and three C-terminal LIM domains. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell-cell contact areas, and at focal adhesion plaques. Testin interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin and is involved in cell motility and adhesion events. Knockout mice experiments reveal a tumor repressor function of Testin. The PET domain is a protein-protein interaction domain and is usually found in conjunction with LIM domain, which is also involved in protein-protein interactions. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 193604  Cd Length: 88  Bit Score: 167.81  E-value: 1.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506325748 116 ITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALG 195
Cdd:cd09829    1 VTYEWAPPGVTQELARYYMELLPKEKQPIAGSEGAQYRKKQLQKQLPLHDQDPSLCHELSENEVKQMEQFVKKYKEEALG 80


                 ....*...
gi 506325748 196 VGEVALPG 203
Cdd:cd09829   81 VGKVIEPG 88
PET pfam06297
PET Domain; This domain is suggested to be involved in protein-protein interactions. The ...
 116-200 3.65e-49

PET Domain; This domain is suggested to be involved in protein-protein interactions. The family is found in conjunction with pfam00412.


Pssm-ID: 461872  Cd Length: 85  Bit Score: 156.25  E-value: 3.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506325748  116 ITYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALG 195
Cdd:pfam06297   1 ETYEWVPPGLTPELVHQYMECLPEEKVPVVGSEGAKYRKKQLLKQLPPHDQDPSYCHGLSEEEVKEMEDFVKQRKEEALG 80


                  ....*
gi 506325748  196 VGEVA 200
Cdd:pfam06297  81 VGEVK 85
PET cd09027
PET ((Prickle Espinas Testin) domain is involved in protein-protein interactions; PET domain ...
 117-197 1.94e-31

PET ((Prickle Espinas Testin) domain is involved in protein-protein interactions; PET domain is involved in protein-protein interactions and is usually found in conjunction with LIM domain, which is also a protein-protein interaction domain. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes. The PET domain has been found at the N-terminal of four known groups of proteins: prickle, testin, LIMPETin/LIM-9 and overexpressed breast tumor protein (OEBT). Prickle has been implicated in regulation of cell movement through its association with the Dishevelled (Dsh) protein in the planar cell polarity (PCP) pathway. Testin is a cytoskeleton associated focal adhesion protein that localizes along actin stress fibers, at cell contact areas, and at focal adhesion plaques. It interacts with a variety of cytoskeletal proteins, including zyxin, mena, VASP, talin, and actin, and is involved in cell motility and adhesion events. Knockout mice experiments reveal tumor repressor function of Testin. LIMPETin/LIM-9 contains an N-terminal PET domain and 6 LIM domains at the C-terminal. In Schistosoma mansoni, where LIMPETin was first identified, it is down regulated in sexually mature adult females compared to sexually immature adult females and adult males. Its differential expression indicates that it is a transcription regulator. In C. elegans, LIM-9 may play a role in regulating the assembly and maintenance of the muscle A-band by forming a protein complex with SCPL-1 and UNC-89 and other proteins. OEBT displays a PET domain with two LIM domains, and is predicted to be localized in the nucleus with a possible role in cancer differentiation.


Pssm-ID: 193601  Cd Length: 82  Bit Score: 110.97  E-value: 1.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506325748 117 TYEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALGV 196
Cdd:cd09027    2 KYAWVPPGLNASLIEQYFECLPKEKVPRLGSEGAKYRRRQLLYQLPAHDLDPRYCDALSEEERAEFEDFVAARKQEALGV 81


                 .
gi 506325748 197 G 197
Cdd:cd09027   82 G 82
PET_LIMPETin_LIM-9 cd09830
The PET domain of protein LIMPETin and LIM-9; The PET domain of protein LIMPETin and LIM-9: ...
 118-197 1.19e-19

The PET domain of protein LIMPETin and LIM-9; The PET domain of protein LIMPETin and LIM-9: Members of this family contain an N-terminal PETdomain and five to six LIM domains at the C-terminus. Four of the six LIM domains are highly homologous to the four-and-half LIM (FHL) domain family while the other two show sequence similarity to LIM domains of the Testin family. Thus, proteins of this family may be the recombinant product of genes coding testin and FHL proteins. In Schistosoma mansoni, where LIMPETin was first identified, LIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult male. Thus, proteins of this family may be the recombinant product of genes coding Testin and FHL proteins. SmLIMPETin is down regulated in sexually mature adult Schistosoma females compared to sexually immature adult females and adult males. Its differential expression indicates that it is a transcription regulator. In C. elegans, LIM-9 binds to UNC-97 and UNC-96, components of sarcomeric muscle M-lines. LIM-9 also forms a complex with SCPL-1 and UNC-89, whose function is to organize sarcomeric A-bands, especially the M-line of muscle. Thus, it might play a role in regulating the assembly and maintenance of muscle A-band. The PET domain is a protein-protein interaction domain and is usually found in conjunction with LIM domain, which is also involved in protein-protein interactions. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 193605  Cd Length: 83  Bit Score: 80.44  E-value: 1.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506325748 118 YEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIydQDPSR--CRGLLENELKLMEEFVKQYKSEALG 195
Cdd:cd09830    3 YTWVPPGLSSTKIDDYMSSLPNEKVPKLGSPGERYREKQLILQLPK--QDLSLayCKHLEEDEKRSFEDFVNARNEIALG 80


                 ..
gi 506325748 196 VG 197
Cdd:cd09830   81 IG 82
PET_Prickle cd09827
The PET domain of Prickle; The PET domain of Prickle: Prickle contains an N-terminal PET ...
 118-199 1.46e-18

The PET domain of Prickle; The PET domain of Prickle: Prickle contains an N-terminal PET domain and three C-terminal LIM domains. Prickle has been implicated in regulation of cell movement in the planar cell polarity (PCP) pathway which requires the conserved Frizzled/Dishevelled (Dsh); Prickle interacts with Dishevelled, thereby modulating the activity of Frizzled/Dishevelled and the PCP signaling. Two forms of Prickle have been identified, namely Prickle 1 and Prickle 2. These are differentially expressed; Prickle 1 is found in fetal heart and hematological malignancies, while Prickle 2 is expressed in fetal brain, adult cartilage, pancreatic islet, and some types of timorous cells. The PET domain is a protein-protein interaction domain, usually found in conjunction with the LIM domain, which is also involved in protein-protein interactions. The PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 193602  Cd Length: 97  Bit Score: 77.78  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506325748 118 YEWAPPGVTQKLGLQYMELIPKEKQPVTGTEGAFYRRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALGVG 197
Cdd:cd09827   12 YAWVPPGLKPEQVHAYFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDNEVRYCNSLSEEEKRELRLFSAQRKREALGRG 91


                 ..
gi 506325748 198 EV 199
Cdd:cd09827   92 IV 93
PET_OEBT cd09828
The PET domain of overexpressed breast tumor protein (OEBT); The PET domain of overexpressed ...
 153-202 2.22e-03

The PET domain of overexpressed breast tumor protein (OEBT); The PET domain of overexpressed breast tumor protein (OEBT): OEBT contains an N-terminal PET domain and two C-terminal LIM domains, and is predicted to be localized in the nucleus. The expression pattern of OEBT in malignant tissues indicates a possible role of OEBT in cancer differentiation. The PET domain is a protein-protein interaction domain and is usually found in conjunction with LIM domain, which is also involved in protein-protein interactions. PET containing proteins serve as adaptors or scaffolds to support the assembly of multimeric protein complexes.


Pssm-ID: 193603  Cd Length: 116  Bit Score: 36.84  E-value: 2.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 506325748 153 RRRQLMHQLPIYDQDPSRCRGLLENELKLMEEFVKQYKSEALGVGeVALP 202
Cdd:cd09828   66 GLRTLLQQLPPQDSDERYCLALAEEERAQLRLFCARRKQEALGQG-VARP 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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