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Conserved domains on  [gi|51242966|ref|NP_001003791|]
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erlin-2 isoform 2 [Homo sapiens]

Protein Classification

SPFH domain-containing protein( domain architecture ID 139628)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_like super family cl19107
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 16-141 7.37e-100

core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


The actual alignment was detected with superfamily member cd03406:

Pssm-ID: 473137 [Multi-domain]  Cd Length: 293  Bit Score: 288.43  E-value: 7.37e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966  16 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 95
Cdd:cd03406   1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51242966  96 VPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELF 141
Cdd:cd03406  81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLF 126
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 16-141 7.37e-100

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 288.43  E-value: 7.37e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966  16 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 95
Cdd:cd03406   1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51242966  96 VPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELF 141
Cdd:cd03406  81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLF 126
PHB smart00244
prohibitin homologues; prohibitin homologues
 21-138 6.72e-23

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 88.10  E-value: 6.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966     21 SAVHKIEEGHIGVYYRGGALLTsTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPNAV 100
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA--VVYYRVLDPL 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 51242966    101 YDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYI 138
Cdd:smart00244  78 RAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLT 113
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 25-150 1.18e-19

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 80.44  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966    25 KIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLV-PNAVYDI 103
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDV--TVIYRVnPDDPPKL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 51242966   104 VKNY-TADYDKALIFNKIHHELNQFCSVHTLQEVYIELFGLENDFSQE 150
Cdd:pfam01145  79 VQNVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNA 126
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-139 2.78e-09

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 54.08  E-value: 2.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966   4 LGAVVAVASSFFcasLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVM 83
Cdd:COG0330   5 LLLILLVLVLVL---LFSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51242966  84 IYFDriEVVNFLVPNAvYDIVKNyTADYDKALIfNKIHHELNQFCSVHTLQEVYIE 139
Cdd:COG0330  81 VDVD--AVVQYRITDP-AKFLYN-VENAEEALR-QLAESALREVIGKMTLDEVLST 131
PRK11029 PRK11029
protease modulator HflC;
6-68 4.53e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 36.26  E-value: 4.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51242966    6 AVVAVASSFFCASLFSavhkIEEGHIGVYYRGGALLTSTSG------PGFHLMLPFITSYKSVQTTLQT 68
Cdd:PRK11029   7 AIIIIVLVVLYMSVFV----VKEGERGIVLRFGKVLRDDDNkplvyaPGLHFKIPFIETVKMLDARIQT 71
 
Name Accession Description Interval E-value
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 16-141 7.37e-100

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 288.43  E-value: 7.37e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966  16 CASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFL 95
Cdd:cd03406   1 ALLLFFSIHKIPEGHVGVYYRGGALLNETSEPGYHLMLPFLTTYESVQVTLQTDEVKNVPCGTSGGVMIYFDRIEVVNRL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 51242966  96 VPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELF 141
Cdd:cd03406  81 DKESVYDTVKNYTVDYDKTWIFDKIHHELNQFCSVHTLQEVYIDLF 126
PHB smart00244
prohibitin homologues; prohibitin homologues
 21-138 6.72e-23

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 88.10  E-value: 6.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966     21 SAVHKIEEGHIGVYYRGGALLTsTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLVPNAV 100
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR-VLGPGLHFLIPFIDDVKKVDLRAQTDDVPPQETITKDNVKVSVDA--VVYYRVLDPL 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 51242966    101 YDIVKNYTADYdkALIFNKIHHELNQFCSVHTLQEVYI 138
Cdd:smart00244  78 RAVYRVLDADY--AVIEQLAQTTLRSVIGKRTLDELLT 113
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 25-150 1.18e-19

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 80.44  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966    25 KIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRieVVNFLV-PNAVYDI 103
Cdd:pfam01145   2 IVPPGEVGVVTRFGKL-SRVLEPGLHFIIPFIQRVVTVDVRVQTLEVSVQTVLTKDGVPVNVDV--TVIYRVnPDDPPKL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 51242966   104 VKNY-TADYDKALIFNKIHHELNQFCSVHTLQEVYIELFGLENDFSQE 150
Cdd:pfam01145  79 VQNVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNA 126
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 65-133 5.17e-17

core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 71.63  E-value: 5.17e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51242966  65 TLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTL 133
Cdd:cd02106   1 RPQFDDVRVEPVGTADGVPVAVDLVVQFRITDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTL 69
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 23-137 2.50e-12

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 61.38  E-value: 2.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966  23 VHKIEEGHIGV-YYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKnVPCGTSGGVMIyfdRIEV-VNF-LVPNA 99
Cdd:cd03401   1 FYTVDAGEVGVvFRRGKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREIT-LTVLSKDGQTV---NIDLsVLYrPDPEK 76

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 51242966 100 VYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVY 137
Cdd:cd03401  77 LPELYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELY 114
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 4-139 2.78e-09

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 54.08  E-value: 2.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966   4 LGAVVAVASSFFcasLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVM 83
Cdd:COG0330   5 LLLILLVLVLVL---LFSSVYIVPQGERGVVLRFGKY-VRTLEPGLHFKIPFIDRVRKVDVREQVLDVPPQEVLTKDNNI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51242966  84 IYFDriEVVNFLVPNAvYDIVKNyTADYDKALIfNKIHHELNQFCSVHTLQEVYIE 139
Cdd:COG0330  81 VDVD--AVVQYRITDP-AKFLYN-VENAEEALR-QLAESALREVIGKMTLDEVLST 131
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 4-84 2.33e-04

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 39.80  E-value: 2.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51242966   4 LGAVVAVAssffcASLFSAVHKIEEGHIGVYYRGGALlTSTSGPGFHLMLPF-ITSYKSVQTTlQTDEVKNVPCGTSGGV 82
Cdd:cd03404   1 LILLLLLL-----VWLLSGFYTVDPGERGVVLRFGKY-VRTVGPGLHWKLPFpIEVVEKVNVT-QVRSVEIGFRVPEESL 73


                ..
gi 51242966  83 MI 84
Cdd:cd03404  74 ML 75
PRK11029 PRK11029
protease modulator HflC;
6-68 4.53e-03

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 36.26  E-value: 4.53e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51242966    6 AVVAVASSFFCASLFSavhkIEEGHIGVYYRGGALLTSTSG------PGFHLMLPFITSYKSVQTTLQT 68
Cdd:PRK11029   7 AIIIIVLVVLYMSVFV----VKEGERGIVLRFGKVLRDDDNkplvyaPGLHFKIPFIETVKMLDARIQT 71
 
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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