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Conserved domains on  [gi|568956836|ref|XP_006531081|]
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protein MTSS 2 isoform X10 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
1-177 9.45e-118

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


The actual alignment was detected with superfamily member cd07643:

Pssm-ID: 448379  Cd Length: 231  Bit Score: 351.75  E-value: 9.45e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836   1 MATNTRGATRDIGSALTRMCMRHRSIETKLRQFTNALLESLINPLQERIEDWKKSANQLDKDHAKEYKRARHEIKKKSSD 80
Cdd:cd07643   58 AATNTRGATKEIGSALTRMCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836  81 TLKLQKKARKellGKGDLQPQLDSALQDVNDMYLLLEETEKQAVRRALIEERGRFCTFITFLQPVVNGELTMLGEITHLQ 160
Cdd:cd07643  138 TIRLQKKARK---GKGDLQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQ 214
                        170
                 ....*....|....*..
gi 568956836 161 GIIDDLVVLTADPHKLP 177
Cdd:cd07643  215 TIMEDLASLTADPHKLP 231
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
658-688 2.96e-13

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein 1 (MTSS-1); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in metastasis suppressor protein 1 (MTSS1, also called also known as missing in metastasis or MIM). MTSS1 may be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton. It interacts with actin via its WH2 domain. MTSS1 is a novel potential metastasis suppressor gene in several types of human cancers; its expression is down-regulated in ovarian cancer, colorectal cancer, oesophageal cancer, prostate cancer and breast cancer, whereas it has also been observed to be up-regulated in hepato-cellular carcinoma and breast cancer.


:

Pssm-ID: 409203  Cd Length: 31  Bit Score: 63.96  E-value: 2.96e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568956836 658 SDPPAEDMLVAIRRGVRLRRTVTNDRSAPRI 688
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
 
Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
1-177 9.45e-118

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 351.75  E-value: 9.45e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836   1 MATNTRGATRDIGSALTRMCMRHRSIETKLRQFTNALLESLINPLQERIEDWKKSANQLDKDHAKEYKRARHEIKKKSSD 80
Cdd:cd07643   58 AATNTRGATKEIGSALTRMCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836  81 TLKLQKKARKellGKGDLQPQLDSALQDVNDMYLLLEETEKQAVRRALIEERGRFCTFITFLQPVVNGELTMLGEITHLQ 160
Cdd:cd07643  138 TIRLQKKARK---GKGDLQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQ 214
                        170
                 ....*....|....*..
gi 568956836 161 GIIDDLVVLTADPHKLP 177
Cdd:cd07643  215 TIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
1-176 9.79e-88

IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent.


Pssm-ID: 429972  Cd Length: 218  Bit Score: 273.68  E-value: 9.79e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836    1 MATNTRGaTRDIGSALTRMCMRHRSIETKLRQFTNALLESLINPLQERIEDWKKSANQLDKDHAKEYKRARHEIKKKSSD 80
Cdd:pfam08397  46 MATNSRG-SRELGSALTQMCMRHRSIESKLEQFVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836   81 TLKLQKKARKellGKGDLQPQLDSALQDVNDMYLLLEETEKQAVRRALIEERGRFCTFITFLQPVVNGELTMLGE-ITHL 159
Cdd:pfam08397 125 LLKLQKKADK---GKGDQQPQLDEALQDVNDKYLLLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHL 201
                         170
                  ....*....|....*..
gi 568956836  160 QGIIDDLVVLTADPHKL 176
Cdd:pfam08397 202 QNIVLLWKELTSEPHRL 218
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
658-688 2.96e-13

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein 1 (MTSS-1); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in metastasis suppressor protein 1 (MTSS1, also called also known as missing in metastasis or MIM). MTSS1 may be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton. It interacts with actin via its WH2 domain. MTSS1 is a novel potential metastasis suppressor gene in several types of human cancers; its expression is down-regulated in ovarian cancer, colorectal cancer, oesophageal cancer, prostate cancer and breast cancer, whereas it has also been observed to be up-regulated in hepato-cellular carcinoma and breast cancer.


Pssm-ID: 409203  Cd Length: 31  Bit Score: 63.96  E-value: 2.96e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568956836 658 SDPPAEDMLVAIRRGVRLRRTVTNDRSAPRI 688
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
 
Name Accession Description Interval E-value
I-BAR_IMD_MIM cd07643
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; ...
1-177 9.45e-118

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Missing In Metastasis; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. Members of this subfamily include missing in metastasis (MIM) or metastasis suppressor 1 (MTSS1), metastasis suppressor 1-like (MTSSL) or ABBA (Actin-Bundling protein with BAIAP2 homology), and similar proteins. They contain an N-terminal IMD and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. MIM was originally identified as a missing transcript from metastatic bladder and prostate cancer cells. It is a scaffold protein that functions in a signaling pathway between the PDGF receptor, Src kinases, and actin assembly. It may also function as a cofactor of the Sonic hedgehog (Shh) transcriptional pathway and may participate in tumor development and progression via this pathway. ABBA regulates actin and plasma membrane dynamics to promote the extension of radial glia, which is important in neuronal migration, axon guidance and neurogenesis. The IMD domain of MIM binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153327  Cd Length: 231  Bit Score: 351.75  E-value: 9.45e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836   1 MATNTRGATRDIGSALTRMCMRHRSIETKLRQFTNALLESLINPLQERIEDWKKSANQLDKDHAKEYKRARHEIKKKSSD 80
Cdd:cd07643   58 AATNTRGATKEIGSALTRMCMRHKSIETKLKQFTSALMDCLVNPLQEKIEEWKKVANQLDKDHAKEYKKARQEIKKKSSD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836  81 TLKLQKKARKellGKGDLQPQLDSALQDVNDMYLLLEETEKQAVRRALIEERGRFCTFITFLQPVVNGELTMLGEITHLQ 160
Cdd:cd07643  138 TIRLQKKARK---GKGDLQPQLDSAMQDVNDKYLLLEETEKKAVRNALIEERGRFCTFVSFLKPVLDEEISMLGEVTHLQ 214
                        170
                 ....*....|....*..
gi 568956836 161 GIIDDLVVLTADPHKLP 177
Cdd:cd07643  215 TIMEDLASLTADPHKLP 231
IMD pfam08397
IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor ...
1-176 9.79e-88

IRSp53/MIM homology domain; The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent.


Pssm-ID: 429972  Cd Length: 218  Bit Score: 273.68  E-value: 9.79e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836    1 MATNTRGaTRDIGSALTRMCMRHRSIETKLRQFTNALLESLINPLQERIEDWKKSANQLDKDHAKEYKRARHEIKKKSSD 80
Cdd:pfam08397  46 MATNSRG-SRELGSALTQMCMRHRSIESKLEQFVQAFHGGLLNPLEENTELDKKFANQLDKDYAKEYRHARAELKKCSSE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836   81 TLKLQKKARKellGKGDLQPQLDSALQDVNDMYLLLEETEKQAVRRALIEERGRFCTFITFLQPVVNGELTMLGE-ITHL 159
Cdd:pfam08397 125 LLKLQKKADK---GKGDQQPQLDEALQDVNDKYLLLEETVSQAVRAALIEERRRFCFLIEKLLPVSNTELQMLGEaITHL 201
                         170
                  ....*....|....*..
gi 568956836  160 QGIIDDLVVLTADPHKL 176
Cdd:pfam08397 202 QNIVLLWKELTSEPHRL 218
I-BAR_IMD cd07605
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ...
1-166 5.51e-49

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.


Pssm-ID: 153289 [Multi-domain]  Cd Length: 223  Bit Score: 171.01  E-value: 5.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836   1 MATNTRGaTRDIGSALTRMCMRHRSIETKLRQFTNALLESLINPLQERIEDWKKSANQLDKDHAKEYKRARHEIKKKSSD 80
Cdd:cd07605   56 LASQSRG-SQELGEALKQIVDTHKSIEASLEQVAKAFHGELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKARSE 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836  81 TLKLQKKARKEllGKGDLQPQLDSALQDVNDMYLLLEETEKQAVRRALIEERGRFCTFITFLQPVVNGELTM-LGEITHL 159
Cdd:cd07605  135 LKKLQKKSQKS--GTGKYQEKLDQALEELNDKQKELEAFVSQGLRDALLEERRRYCFLVDKHCSVAKHEIAYhAKAMTLL 212

                 ....*..
gi 568956836 160 QGIIDDL 166
Cdd:cd07605  213 STRLPLW 219
WH2_MTSS1 cd22060
Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein ...
658-688 2.96e-13

Wiskott Aldrich syndrome homology region 2 (WH2 motif) found in Metastasis suppressor protein 1 (MTSS-1); This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in metastasis suppressor protein 1 (MTSS1, also called also known as missing in metastasis or MIM). MTSS1 may be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton. It interacts with actin via its WH2 domain. MTSS1 is a novel potential metastasis suppressor gene in several types of human cancers; its expression is down-regulated in ovarian cancer, colorectal cancer, oesophageal cancer, prostate cancer and breast cancer, whereas it has also been observed to be up-regulated in hepato-cellular carcinoma and breast cancer.


Pssm-ID: 409203  Cd Length: 31  Bit Score: 63.96  E-value: 2.96e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 568956836 658 SDPPAEDMLVAIRRGVRLRRTVTNDRSAPRI 688
Cdd:cd22060    1 DEPQGEDMLSAIRRGVKLRKTVTNDRSAPRI 31
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
15-143 1.11e-09

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 58.22  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836  15 ALTRMCMRHRSIETKLRQFTNALLESLINPLQERIEDWKKSANQLDKDHAKEYKRARHEIKKKSSDTLKLQKKARKEllg 94
Cdd:cd07307   51 DLGEALEKFGKIQKELEEFRDQLEQKLENKVIEPLKEYLKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDS--- 127
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568956836  95 kgDLQPQLDSALQDVNDMYLLLEETEKQAVRRaLIEERGRFC--TFITFLQ 143
Cdd:cd07307  128 --SKLAEAEEELQEAKEKYEELREELIEDLNK-LEEKRKELFlsLLLSFIE 175
I-BAR_IMD_IRSp53 cd07646
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor ...
1-136 1.39e-04

Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), of Insulin Receptor tyrosine kinase Substrate p53; The IMD domain, also called Inverse-Bin/Amphiphysin/Rvs (I-BAR) domain, is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions. IRSp53 (Insulin Receptor tyrosine kinase Substrate p53) is also known as BAIAP2 (Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2). It is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. One variant (T-form) is expressed exclusively in human breast cancer cells. The gene encoding IRSp53 is a putative susceptibility gene for Gilles de la Tourette syndrome. IRSp53 contains an N-terminal IMD, a CRIB (Cdc42 and Rac interactive binding motif), an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus. Its IMD domain binds and bundles actin filaments, binds membranes, and interacts with the small GTPase Rac.


Pssm-ID: 153330  Cd Length: 232  Bit Score: 43.77  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956836   1 MATNTRGaTRDIGSALTRMCMRHRSIETKLRQFTNALLESLINPLQERIEDWKKSANQLDKDHAKEYKRARHEIKKKSSD 80
Cdd:cd07646   58 LASESQG-SKELGDVLFQMAEVHRQIQNQLEEMLKSFHNELLTQLEQKVELDSRYLTAALKKYQTEHRSKGESLEKCQAE 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568956836  81 TLKLQKKARkellGKGDLQPQLDSALQDVNDMYLLLEETEK---QAVRRALIEERGRFC 136
Cdd:cd07646  137 LKKLRKKSQ----GSKNPQKYSDKELQYIEAISNKQGELENyvsDGYKTALTEERRRYC 191
WH2_WAS_WASL cd22064
Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); ...
665-686 3.55e-03

Wiskott Aldrich syndrome homology region 2 (WH2 motif) in WAS/WASL-interacting protein (WIP); This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) found in WAS/WASL-interacting protein family (WIPF, also known as WASP-interacting protein or WIP). Human WIP protein is proline rich and has high sequence similarity to yeast protein verprolin (included in this model). WIP forms complexes with WASP/N-WASP and modulates their function in vivo. It is involved in the regulation of endocytosis and participates in several cellular processes, some of which are relevant in cancer and may be dependent on different oncogenic stimuli. WIP interacts directly with mammalian actin-binding protein-1 (mABP1) via the SH3 domain during platelet-derived growth factor (PDGF)-mediated dorsal ruffle formation. WIP family includes members 1 (WAS/WASL-interacting protein family member 1) or WIPF1), 2 (WIPF2) and 3 (WIPF3). Aberrant expression of WIPF1 contributes to the invasion and metastasis of several malignancies such breast cancer, glioma and colorectal cancer; it has been identified as an oncoprotein in human pancreatic ductal adenocarcinoma (PDAC) and is associated with poor survival. WIPF2 may be an important regulator of the actin cytoskeleton. WIPF2 binds to N-WASP, regulating actin dynamics close to the plasma membrane; N-WASP in turn controls the second phase insulin secretion through the regulation of the Arp2/3 complex. WIPF3, along with LIPA (lysosomal acid lipase A), are expressed in microphages and are involved in pathological abdominal aortic aneurysm (AAA), a serious condition of the aorta. In yeast, verprolin is involved in cytoskeletal organization and cellular growth. It may exert its effects on the cytoskeleton directly, or indirectly via proline-binding proteins, such as profilin, or via proteins possessing SH3 domains.


Pssm-ID: 409207 [Multi-domain]  Cd Length: 29  Bit Score: 35.52  E-value: 3.55e-03
                         10        20
                 ....*....|....*....|..
gi 568956836 665 MLVAIRRGVRLRRTVTNDRSAP 686
Cdd:cd22064    8 LLGDIRKGMKLKKTVTNDRSAP 29
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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