BTB/POZ domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130399    97 RITMLVDGVRFTVEQSLLTAHPTTMLGTMFGSGFQFAHT--NERGEYDVADGISHLVFRAILEYYKSGVIRCPPTVSVPE 174
Cdd:pfam16017   1 RLTLVVDGTRFVVDPSLFTAHPDTMLGRMFGSSMERNFTrpNEKGEYEIAEGISSTVFRAILDYYKTGVIRCPPSVSIPE 80

                          90       100
                  ....*....|....*....|....*.
gi 20130399   175 LKEACDYLLIPFDATTVRCQNLRGLL 200
Cdd:pfam16017  81 LREACDYLLIPFDATTIKCQNLRALL 106

BTB/POZ domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130399    97 RITMLVDGVRFTVEQSLLTAHPTTMLGTMFGSGFQFAHT--NERGEYDVADGISHLVFRAILEYYKSGVIRCPPTVSVPE 174
Cdd:pfam16017   1 RLTLVVDGTRFVVDPSLFTAHPDTMLGRMFGSSMERNFTrpNEKGEYEIAEGISSTVFRAILDYYKTGVIRCPPSVSIPE 80

                          90       100
                  ....*....|....*....|....*.
gi 20130399   175 LKEACDYLLIPFDATTVRCQNLRGLL 200
Cdd:pfam16017  81 LREACDYLLIPFDATTIKCQNLRALL 106

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130399     98 ITMLVDGVRFTVEQSLLTAHPTTMLGtMFGSgfQFAHTNERGEYdvADGISHLVFRAILEYYKSGVIRCPPtVSVPELKE 177
Cdd:smart00225   2 VTLVVGGKKFHAHKAVLAAHSPYFKA-LFSS--DFKESDKSEIY--LDDVSPEDFRALLNFLYTGKLDLPE-ENVEELLE 75

                           90       100
                   ....*....|....*....|..
gi 20130399    178 ACDYLLIPFDATTVRCQNLRGL 199
Cdd:smart00225  76 LADYLQIPGLVELCEEFLLKLL 97

BTB/POZ domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130399    97 RITMLVDGVRFTVEQSLLTAHPTTMLGTMFGSGFQFAHT--NERGEYDVADGISHLVFRAILEYYKSGVIRCPPTVSVPE 174
Cdd:pfam16017   1 RLTLVVDGTRFVVDPSLFTAHPDTMLGRMFGSSMERNFTrpNEKGEYEIAEGISSTVFRAILDYYKTGVIRCPPSVSIPE 80

                          90       100
                  ....*....|....*....|....*.
gi 20130399   175 LKEACDYLLIPFDATTVRCQNLRGLL 200
Cdd:pfam16017  81 LREACDYLLIPFDATTIKCQNLRALL 106

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 20 (KCTD20); KCTD20, also called potassium channel tetramerization domain containing 20, is a positive regulator of Akt signaling. It may play an important role in regulating the death and growth of some non-nervous and nervous cells. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130399  95 PERITMLVDGVRFTVEQSLLTAHPTTMLGTMFGSG--FQFAHTNERGEYDVADGISHLVFRAILEYYKSGVIRCPPTVSV 172
Cdd:cd18386   2 PEKVTLIVDGTRFVVNPQIFTAHPDTMLGRMFGPGreYNFTRPNEKGEYEIAEGISCTVFRTVLDYYKTGIINCPDGISI 81

                        90       100
                ....*....|....*....|...
gi 20130399 173 PELKEACDYLLIPFDATTVRCQN 195
Cdd:cd18386  82 PDLRDTCDYLCINFDFNTIKCQD 104

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins; This family includes two protein groups: voltage-gated potassium (Kv) channels and potassium channel tetramerization domain-containing (KCTD) proteins. Kv channels are membrane proteins with fundamental physiological roles. They are responsible for a variety of electrical phenomena, such as the repolarization of the action potential, spike frequency adaptation, synaptic repolarization, and smooth muscle contraction. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels, and others. All family members contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130399  98 ITMLVDGVRFTVEQSLLTAHPTTMLGTMFGSGFQFAHTNERGEYDVADgiSHLVFRAILEYYKSGVIRCPPTVSVPELKE 177
Cdd:cd18187   1 VVLNVSGTRFVTNRQTLTRHPDTLLGRMFKPGREFTFPNETGEYFIDR--DPTVFRTILNYYRTGKLNCPDGISIPDLRE 78

                ....*
gi 20130399 178 ACDYL 182
Cdd:cd18187  79 ECDFY 83

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 7 (KCTD7); KCTD7 is a BTB/POZ domain-containing protein that has an impact on K+ fluxes, neurotransmitter synthesis, and neuronal function. It functions as a regulator of potassium conductance in neurons, and is involved in the control of excitability of cortical neurons. Mutations in KCTD7 may cause progressive myoclonus epilepsy (PME). The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130399  95 PERITMLVDGVRFTVEQSLLTAHPTTMLGTMFgSGFQFAHTNERGEYDV-ADGIShlvFRAILEYYKSGVIRcPPTVSVP 173
Cdd:cd18366   3 PEVVPLNVGGMHFTTRLSTLRKYEDSMLAAMF-SGRHHIPKDSEGRYFIdRDGSY---FGYILNFLRDGDLP-PRERARA 77

                        90
                ....*....|...
gi 20130399 174 ELKEACDYLLIPF 186
Cdd:cd18366  78 VYKEAQYYGIGPL 90

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing proteins; The potassium channel tetramerization domain (KCTD) family proteins contain the BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD proteins play crucial roles in a variety of fundamental biological processes, such as protein ubiquitination and degradation, suppression of proliferation or transcription, cytoskeleton regulation, tetramerization and gating of ion channels and others. Some KCTD proteins are involved in protein ubiquitination as part of the CRL (Cullin RING Ligase) E3 ligases. Some others show Cullin-independent functions including binding and regulation of GABA (gamma-aminobutyric acid) receptors (KCTD8, KCTD12 and KCTD16) and inhibition of AP-2 function (KCTD15). KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130399 102 VDGVRFTVEQSLLTAHPTTMLGTMFGSGFqFAHTNERGEYDV-ADGIshlVFRAILEYYKSGVIRCPPT-VSVPELKEAC 179
Cdd:cd18316   5 VGGTLFTTSRSTLLKDPDSLLAALFSGRW-PLPRDEDGSIFIdRDPE---LFRHILNFLRTGKLPLPSDfVELEELLAEA 80

                ...
gi 20130399 180 DYL 182
Cdd:cd18316  81 EFY 83

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCND/Kv4 subfamily of Shal-type voltage-dependent potassium channels; Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv4, also known as subfamily D, contains three alpha subunit members, Kv4.1 (KCND1), Kv4.2 (KCND2), and Kv4.3 (KCND3), which are orthologs of the Shal gene in Drosophila. They are A-type potassium channels that mediate the native, fast inactivating (A-type) K+ current (IA) described both in the nervous system (A currents) and the heart (transient outward current). Kv4/KCND subfamily alpha subunits form functional homo- or hetero-tetrameric channels through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif. They are modulated by cytoplasmic KChIPs/KCNIPs (Kv-channel interacting proteins), which are small calcium binding proteins with EF-hand-like domains.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20130399  97 RITMLVDGVRFTVEQSLLTAHPTTMLGtmfGSGFQFAHTNERGEY--DvADGIshlVFRAILEYYKSGVIRCP 167
Cdd:cd18380   1 RIVINVSGRRFETWKNTLEKYPDTLLG---STEKEFFYDDDTKEYffD-RDPE---IFRHILNFYRTGKLHYP 66

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in KCNC/Kv3 subfamily of Shaw-type voltage-dependent potassium channels; Voltage-gated potassium (Kv) channels are composed of alpha subunits, which form the actual conductance pore, and cytoplasmic beta subunits, which are auxiliary proteins that associate with alpha subunits to modulate the activity of the Kv channel. The potassium voltage-gated channel subfamily Kv3, also known as subfamily C, contains four alpha subunit members, Kv3.1 (KCNC1), Kv3.2 (KCNC2), Kv3.3 (KCNC3), and Kv3.4 (KCNC4), which are orthologs of the Shaw gene in Drosophila. Unlike other Kv subfamilies, Kv3 channels typically open only at positive potentials and both, activation and deactivation, in response to changes in voltage are very rapid. They are uniquely associated with the ability of certain neurons to fire action potentials and to release neurotransmitter at high rates of up to 1,000 Hz. Kv3/KCNC subfamily alpha subunits form functional homo- or hetero-tetrameric channels (with other alpha subunits) through their BTB/POZ domain, also known as tetramerization (T1) domain, which is a versatile protein-protein interaction motif.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130399  98 ITMLVDGVRFTVEQSLLTAHPTTMLGTMFGSGFQ-FAHTNERGEY--DVADGishlVFRAILEYYKSGVIRCPPTVSVPE 174
Cdd:cd18379   1 IVINVGGVRHETYKSTLRNLPDTRLAWLTETEASaFDYDPVTGEFffDRHPG----VFAQILNYYRTGKLHCPADVCGPL 76

                ...
gi 20130399 175 LKE 177
Cdd:cd18379  77 FEE 79

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein KCTD11; KCTD11 may function as an antagonist of the Hedgehog pathway of cell proliferation and differentiation by affecting the nuclear transfer of transcription factor GLI1, thus maintaining cerebellar granule cells in the undifferentiated state. It is a probable substrate-specific adapter for a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex towards HDAC1. It contains a BTB/POZ domain; in some cases the domain may be truncated. The BTB/POZ domain, also known as tetramerization (T1) domain, is a versatile protein-protein interaction motif that facilitates homodimerization or heterodimerization. KCTD family BTB domains can adopt a wide range of oligomerization geometries, including homodimerization, tetramerization, and pentamerization. Variants of the human/mouse KCTD11 appear to contain truncated BTB/POZ domains.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20130399  98 ITMLVDGVRFTVEQSLLTAHPTTMLGTMFGSG---FQFAHTNERGEYDV-ADGIShlvFRAILEYYKSGVIRCP 167
Cdd:cd18370   1 VTLNVGGTLYSTTLETLTRFPDSMLGAMFRAGtpiPPNLNMQGGGHYFIdRDGKA---FRHILNFLRLGRLDLP 71