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Conserved domains on  [gi|1907132138|ref|XP_036017414|]
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sorting nexin-32 isoform X2 [Mus musculus]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 36833)

PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to sorting nexins that are involved in regulating membrane traffic and protein sorting in the endosomal system

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 ...
 62-186 8.13e-66

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 cd07621:

Pssm-ID: 472257  Cd Length: 219  Bit Score: 206.80  E-value: 8.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  62 GLLRSIVRSADEVLItgISGLKEVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQEVNQ 141
Cdd:cd07621     1 GFLKSISKSADEELL--LSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQLATSEPTP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907132138 142 LKRSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAK 186
Cdd:cd07621    79 LDKFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAK 123
PX_domain super family cl02563
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 1-45 3.21e-22

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


The actual alignment was detected with superfamily member cd07291:

Pssm-ID: 470617  Cd Length: 141  Bit Score: 90.89  E-value: 3.21e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907132138   1 MKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFSVFLEY 45
Cdd:cd07291    96 MKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEY 140
 
Name Accession Description Interval E-value
BAR_SNX5_6 cd07621
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, ...
 62-186 8.13e-66

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Members of this subfamily include SNX5, SNX6, the mammalian SNX32, and similar proteins. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. The function of SNX32 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153305  Cd Length: 219  Bit Score: 206.80  E-value: 8.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  62 GLLRSIVRSADEVLItgISGLKEVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQEVNQ 141
Cdd:cd07621     1 GFLKSISKSADEELL--LSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQLATSEPTP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907132138 142 LKRSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAK 186
Cdd:cd07621    79 LDKFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAK 123
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 1-45 3.21e-22

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 90.89  E-value: 3.21e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907132138   1 MKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFSVFLEY 45
Cdd:cd07291    96 MKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEY 140
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 14-46 1.42e-04

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 39.92  E-value: 1.42e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907132138  14 KKTVAMHEVFLQRLAAHPTLRRDHNFSVFLEYS 46
Cdd:pfam00787  52 EKRRKGLEQYLQRLLQHPELRNSEVLLEFLESD 84
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 83-186 8.89e-04

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 40.34  E-value: 8.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  83 KEVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQEVNQ-LKRSFLKLAELFERLRKLEG 161
Cdd:pfam09325  20 NEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTgLSRALSQLAEVEERIKELLE 99

                          90       100
                  ....*....|....*....|....*
gi 1907132138 162 RVASDEDLKLSDMLRYYMRDSQAAK 186
Cdd:pfam09325 100 RQALQDVLTLGETIDEYLRLIGSVK 124
 
Name Accession Description Interval E-value
BAR_SNX5_6 cd07621
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, ...
 62-186 8.13e-66

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 5 and 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. Members of this subfamily include SNX5, SNX6, the mammalian SNX32, and similar proteins. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. The function of SNX32 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153305  Cd Length: 219  Bit Score: 206.80  E-value: 8.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  62 GLLRSIVRSADEVLItgISGLKEVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQEVNQ 141
Cdd:cd07621     1 GFLKSISKSADEELL--LSGQKDVDEFFEQEKNFLVEYHNRIKDATAKADKMTRKHKDVADSYIKISAALTQLATSEPTP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907132138 142 LKRSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAK 186
Cdd:cd07621    79 LDKFLLKVAETFEKLRKLEGRVASDEDLKLSDTLRYYMRDTQAAK 123
BAR_SNX5 cd07663
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid ...
 62-186 8.97e-54

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 5; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153347  Cd Length: 218  Bit Score: 175.90  E-value: 8.97e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  62 GLLRSIVRSADEVLITGIsglKEVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQEVNQ 141
Cdd:cd07663     1 GFFKNMVKSADEVLFSGV---KEVDEFFEQEKTFLVNYYNRIKDSCAKADKMTRSHKNVADDYIHISAALNSVAAEEPTV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907132138 142 LKRSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAK 186
Cdd:cd07663    78 IKKYLLKVAELFEKLRKVEDRVASDQDLKLTELLRYYMLNIEAAK 122
BAR_SNX6 cd07662
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid ...
 63-186 8.92e-47

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 6; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153346  Cd Length: 218  Bit Score: 157.90  E-value: 8.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  63 LLRSIVRSADEVLItgiSGLKEVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQEVNQL 142
Cdd:cd07662     2 FFKNVVKSADGVIV---SGVKDVDDFFEHERTFLLEYHNRVKDSSAKSDRMTRSHKSAADDYNRIGSSLYTLGTQDSTDI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907132138 143 KRSFLKLAELFERLRKLEGRVASDEDLKLSDMLRYYMRDSQAAK 186
Cdd:cd07662    79 CKFFLKVSELFDKTRKIEARVAADEDLKLSDLLKYYLRESQAAK 122
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 1-45 3.21e-22

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 90.89  E-value: 3.21e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907132138   1 MKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFSVFLEY 45
Cdd:cd07291    96 MKQELEAEYLAVFKKTVQVHEVFLQRLSSHPSLSKDRNFHIFLEY 140
PX_SNX5_like cd06892
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is ...
 1-45 3.18e-21

The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Members of this subfamily include SNX5, SNX6, and similar proteins. They contain a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p.


Pssm-ID: 132802  Cd Length: 141  Bit Score: 88.26  E-value: 3.18e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907132138   1 MKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFSVFLEY 45
Cdd:cd06892    96 MKQELEAEYLAIFKKTVAMHEVFLRRLASHPVLRNDANFRVFLEY 140
PX_SNX6 cd07292
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a ...
 1-46 1.34e-20

The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs.


Pssm-ID: 132825  Cd Length: 141  Bit Score: 86.69  E-value: 1.34e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907132138   1 MKQELEAEYLAIFKKTVAMHEVFLQRLAAHPTLRRDHNFSVFLEYS 46
Cdd:cd07292    96 MKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRKDLNFHVFLEYN 141
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 84-186 3.02e-09

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 56.21  E-value: 3.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  84 EVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQEVNQ---LKRSFLKLAELFERLRKLE 160
Cdd:cd07596     1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEVggeLGEALSKLGKAAEELSSLS 80

                          90       100
                  ....*....|....*....|....*.
gi 1907132138 161 GRVASDEDLKLSDMLRYYMRDSQAAK 186
Cdd:cd07596    81 EAQANQELVKLLEPLKEYLRYCQAVK 106
BAR_SNX_like cd07630
The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are ...
 84-197 5.02e-06

The Bin/Amphiphysin/Rvs (BAR) domain of uncharacterized Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of uncharacterized proteins with similarity to sorting nexins (SNXs), which are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153314  Cd Length: 198  Bit Score: 46.73  E-value: 5.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  84 EVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQE---VNQLKRSFLKLAELFERLRKLE 160
Cdd:cd07630     1 DVDEFFQKERDMNTKLSANMKEAAEKFLKIVNTEQRLANALGHLSSSLQLCVGLDeasVVALNRLCTKLSEALEEAKENI 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907132138 161 GRVASDEDLKLSDMLRYYMRDSQAAKpscaaDGL--RTC 197
Cdd:cd07630    81 EVVAGNNENTLGLTLDLYSRYSESEK-----DMLfrRTC 114
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 21-44 1.21e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 41.03  E-value: 1.21e-04
                          10        20
                  ....*....|....*....|....
gi 1907132138  21 EVFLQRLAAHPTLRRDHNFSVFLE 44
Cdd:cd06859    89 ERFLRRIAAHPVLRKDPDFRLFLE 112
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 14-46 1.42e-04

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 39.92  E-value: 1.42e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907132138  14 KKTVAMHEVFLQRLAAHPTLRRDHNFSVFLEYS 46
Cdd:pfam00787  52 EKRRKGLEQYLQRLLQHPELRNSEVLLEFLESD 84
Vps5 pfam09325
Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is ...
 83-186 8.89e-04

Vps5 C terminal like; Vps5 is a sorting nexin that functions in membrane trafficking. This is the C terminal dimerization domain.


Pssm-ID: 430527 [Multi-domain]  Cd Length: 236  Bit Score: 40.34  E-value: 8.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  83 KEVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQEVNQ-LKRSFLKLAELFERLRKLEG 161
Cdd:pfam09325  20 NEPDEWFIDKKQYIDSLESQLKKLYKALELLVSQRKELASATGEFAKSLASLASLELSTgLSRALSQLAEVEERIKELLE 99

                          90       100
                  ....*....|....*....|....*
gi 1907132138 162 RVASDEDLKLSDMLRYYMRDSQAAK 186
Cdd:pfam09325 100 RQALQDVLTLGETIDEYLRLIGSVK 124
BAR_SNX1 cd07665
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid ...
 82-180 1.58e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 1; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153349 [Multi-domain]  Cd Length: 234  Bit Score: 39.67  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132138  82 LKEVDDFFEHERTFLVEYHTRIRDTCQRADRVMHSHKCLADNYIPISAALSSLGTQEVNQ-LKRSFLKLAELFERLRKLE 160
Cdd:cd07665    17 MNESDVWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTALFAKSLAMLGSSEDNTaLSRALSQLAEVEEKIEQLH 96

                          90       100
                  ....*....|....*....|
gi 1907132138 161 GRVASDEDLKLSDMLRYYMR 180
Cdd:cd07665    97 QEQANNDFFLLAELLADYIR 116
 
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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