leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding protein, and similar proteins; The family includes TGF-beta-stimulated clone-22 domain (TSC22D) leucine zipper transcription factors, TSC22D1-4, as well as c-Myc-binding protein (MycBP). TSC22D proteins have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. Members of this family contain a conserved leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 61557172 150 RKFLESGG---KDVET-RKQIAGMQKRIQDLETENMELKNKVQDLE 191
Cdd:cd21937   8 KQHLGAPGpedADVEAlRLENEELKQKNEELEEENKELKAKLQQYE 53

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172     27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFArhiKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:smart00462   6 FRVKYLGSVEVPEARGLQVVQEAIRKLRAA---QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPD 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 61557172    107 DKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRKFL 153
Cdd:smart00462  83 DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKL 129

leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. This model corresponds to the conserved region that shows high sequence similarity with the leucine zipper (ZIP) domain located at the C-terminus of TGF-beta-stimulated clone-22 domain (TSC22D) family transcription factors. The first helix of ZIP is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 61557172 150 RKFLESGG---KDVET-RKQIAGMQKRIQDLETENMELKNKVQDLE 191
Cdd:cd21937   8 KQHLGAPGpedADVEAlRLENEELKQKNEELEEENKELKAKLQQYE 53

Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain; PTB/PI domain structure similar to those of pleckstrin homology (PH) and IRS-1-like PTB domains.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172     27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFArhiKKSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:smart00462   6 FRVKYLGSVEVPEARGLQVVQEAIRKLRAA---QGSEKKEPQKVILSISSRGVKLIDEDTKAVLHEHPLRRISFCAVGPD 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 61557172    107 DKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRKFL 153
Cdd:smart00462  83 DLDVFGYIARDPGSSRFACHVFRCEKAAEDIALAIGQAFQLAYELKL 129

Ankyrin repeat and sterile alpha motif (SAM) domain-containing (Anks) protein family Phosphotyrosine-binding (PTB) domain; Both AIDA-1b (AbetaPP intracellular domain-associated protein 1b) and Odin (also known as ankyrin repeat and sterile alpha motif domain-containing 1A; ANKS1A) belong to the Anks protein family. Both of these family members interacts with the EphA8 receptor. Ank members consists of ankyrin repeats, a SAM domain and a C-terminal PTB domain which is crucial for interaction with the juxtamembrane (JM) region of EphA8. PTB domains are classified into three groups, namely, phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains of which the Anks PTB is a member. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  13 WMHMPEALSKHYVPYNAKFLGSTEVEQPKGTEVVRDAVRKLKfarhIKKSEGQKIPKVELQISIYGVKILEPKTKEVQHN 92
Cdd:cd01274   3 WRHSPEKLITGSVNYEAHYLGSTEIKELRGTESTKKAIQKLK----KSTREMKKIPTIILSISYKGVKFIDATTKNLICE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61557172  93 CQLHRISFCADDKTDKRIFTFICKDSESNKHLCFVFDSEKC--AEEITLTIGQAFDLAYRKFLESGGK 158
Cdd:cd01274  79 HEIRNISCACQDPEDLNTFAYITKDLKTDHHYCHVFCVLTVdlATEIILTLGQAFEVAYQLALRAQKS 146

Tyrosine-specific kinase/HM-motif TK (TM/HMTK) Phosphotyrosine-binding (PTB) PH-like fold; TK kinases catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. TK kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases. In HMTK the conserved His-Arg-Asp sequence within the catalytic loop is replaced by a His-Met sequence. TM/HMTK have are 2-3 N-terminal PTB domains. PTB domains in TKs are thought to function analogously to the membrane targeting (PH, myristoylation) and pTyr binding (SH2) domains of Src subgroup kinases. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKfarhikkSEGQKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:cd13161   4 FEAKYLGSVPVKEPKGNDVVMAAVKRLK-------DLKLKPKPVVLVVSSEGIRVVERLTGEVLTNVPIKDISFVTVDPK 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 61557172 107 DKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYR 150
Cdd:cd13161  77 DKKLFAFISHDPRLGRITCHVFRCKRGAQEICDTIAEAFKAAAE 120

Numb Phosphotyrosine-binding (PTB) domain; Numb is a membrane associated adaptor protein which plays critical roles in cell fate determination. Numb proteins are involved in control of asymmetric cell division and cell fate choice, endocytosis, cell adhesion, cell migration, ubiquitination of specific substrates and a number of signaling pathways (Notch, Hedgehog, p53). Mutations in Numb plays a critical role in disease (cancer). Numb has an N-terminal PTB domain and a C-terminal NumbF domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHikksegqKIPKVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:cd01268  17 FPVKYLGCVEVGESRGMQVCEEALKKLKASRK-------KPVRAVLWVSGDGLRVVDEKTKGLIVDQTIEKVSFCAPDRN 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 61557172 107 DKRIFTFICKDSESNKHLCFVFDSEK-CAEEITLTIGQAFDLAYRK 151
Cdd:cd01268  90 HERAFSYICRDGTTRRWMCHCFLAVKdSGERLSHAVGCAFAACLER 135

Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein (CAPON) Phosphotyrosine-binding (PTB) domain; CAPON (also known as Nitric oxide synthase 1 adaptor protein, NOS1AP, encodes a cytosolic protein that binds to the signaling molecule, neuronal NOS (nNOS). It contains a N-terminal PTB domain that binds to the small monomeric G protein, Dexras1 and a C-terminal PDZ-binding domain that mediates interactions with nNOS. Included in this cd are C. elegan proteins dystrobrevin, DYB-1, which controls neurotransmitter release and muscle Ca(2+) transients by localizing BK channels and DYstrophin-like phenotype and CAPON related,DYC-1, which is functionally related to dystrophin homolog, DYS-1. Mutations in the dystrophin gene causes Duchenne muscular dystrophy. DYS-1 shares sequence similarity, including key motifs, with their mammalian counterparts. These CAPON-like proteins all have a single PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  14 MHMPEALsKHYVPYNAKFLGSTEVEQPKG-TEVVRdAVRKLKF---ARHIKKSegqkipKVELQISIYGVK-ILEPKTKE 88
Cdd:cd01270  19 LHNEEAF-QHGITFQAKYIGSLEVPRPSSrVEIVA-AMRRIRYefkAKNIKKK------KVTITVSVDGVKvVLRKKKKK 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  89 VQH----------NCQLHRISFCADDKTDKRIFTFICKDSESNKHLCFVFDSEK--CAEEITLTIGQAFDLAYRKFLESG 156
Cdd:cd01270  91 KGWtwdesklllmQHPIYRIFYVSHDSQDLKIFSYIARDGSSNVFKCNVFKSKKksQAMRIVRTIGQAFEVCHKLSLQHM 170

                ....*
gi 61557172 157 GKDVE 161
Cdd:cd01270 171 QGNAD 175

JNK-interacting protein-like (JIP) Phosphotyrosine-binding (PTB) domain; JIP is a mitogen-activated protein kinase scaffold protein. JIP consists of a C-terminal SH3 domain, followed by a PTB domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFARhikKSEGQKIPK--VELQISIYGVKI------LEPKTKEVQHNCQ-LHR 97
Cdd:cd01212   5 FLLGFLGSVEVPYHKGNDVLCQAMQKIATAR---RLTVHLRPPqsCILEISDRGLKMvdrskpNKKDGKPCIHYFYsLKN 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 61557172  98 ISFCADDKTDKRIFTFICKDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRKFLE 154
Cdd:cd01212  82 ISFCGFHPRNSRYFGFITKHPLLQRFACHVFVSQESTRPVAESVGRAFQRFYQEFIE 138

Shc-like phosphotyrosine-binding (PTB) domain; Shc is a substrate for receptor tyrosine kinases, which can interact with phosphoproteins at NPXY motifs. Shc contains an PTB domain followed by an SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Shc-like subgroup.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  13 WMHMPEALSKH-YVPYNAKFLGSTEVEQ-------PKGTEVVRDAVRKL----KFARHIKKSEGQKI---------PK-- 69
Cdd:cd01209   2 GWLHPDQLGMGpGVSYPVRYVGCIEVLQsmrsldfNTRTQVTREAINRVceavGGAKGAKRKRKSKAlssilgksnLQfa 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  70 ---VELQISIYGVKILEPKTKEVQHNCQLHRISF--CADDKTDKRIfTFICKDsESNKHLCFVFD-SEKCAEEITLTIGQ 143
Cdd:cd01209  82 gmnISLTISTDGLNLVTPDTGQIIANHHMQSISFasGGDPDTYDYV-AYVAKD-PVNQRACHVLEcGDGLAQDVIATIGQ 159

                       170
                ....*....|
gi 61557172 144 AFDLAYRKFL 153
Cdd:cd01209 160 AFELRFKQYL 169

Tensin-related Phosphotyrosine-binding (PTB) domain; Tensin plays critical roles in renal function, muscle regeneration, and cell migration. It binds to actin filaments and interacts with the cytoplasmic tails of beta-integrin via its PTB domain, allowing tensin to link actin filaments to integrin receptors. Tensin functions as a platform for assembly and disassembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules, and also by providing interaction sites for other proteins. In addition to its PTB domain, it contains a C-terminal SH2 domain. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  25 VPYNAKFLGSTEVEQPKGTEVVrDAVRKLKFArhIKKSEGQKIPkVELQISIYGVKILEPKTKEVQHNCQLHRISFCADD 104
Cdd:cd13157   2 VSRNAQYIGSFPVSGLDVADRA-DSVRKQLES--LKESGSRGRP-VILSVSLSGIKICSEDGKVVLMAHALRRVSYSTCR 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 61557172 105 KTDKRiFTFICKD--SESNKHLCFVF--DSEKCAEEITLTIGQAFDLAYRK 151
Cdd:cd13157  78 PAHAQ-FAFVARNpgGPTNRQYCHVFvtRSPREAQELNLLLCRAFQLAYLK 127

Phosphotyrosine-binding domain; The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). Human tensin has actin-binding sites, an SH2 (pfam00017) domain and a region similar to the tumour suppressor PTEN. The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172    27 YNAKFLGSTEVEQPKGTEVVRDAVRKLKFARHIKKSEGQKipkVELQISIYGVKILEPKTKEVQHNCQLHRISFCADDKT 106
Cdd:pfam08416   2 YRVEHLTTFELDSLTGLQAVEDAIRKLQLLDAQGRVWTQE---MLLQVSDQGITLTDNETKEELESYPLDSISHCQAVLN 78

                          90       100
                  ....*....|....*....|....*
gi 61557172   107 DKR---IFTFICKDSESNKHLCFVF 128
Cdd:pfam08416  79 DGRynsILALVCQEPGQSKPDVHLF 103

Fe65 C-terminal Phosphotyrosine-binding (PTB) domain; The neuronal adaptor protein Fe65 is involved in brain development, Alzheimer disease amyloid precursor protein (APP) signaling, and proteolytic processing of APP. It contains three protein-protein interaction domains, one WW domain, and a unique tandem array of phosphotyrosine-binding (PTB) domains. The C-terminal PTB domain is responsible for APP binding. PTB domains have a common PH-like fold and are found in various eukaryotic signaling molecules. This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This cd is part of the Dab-like subgroup.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61557172  27 YNAKFLGSTEVEQPKGTEVVRDAVRKLkfARHIKKSegQKIPkVELQISIYGVKIL-EPKTKEVQHNCQLHRISFCADDK 105
Cdd:cd01271   9 LKALYLGSTPVSKPTGMDVLNEAIDTL--LSSVPKE--QWTP-VNVSVAPSTVTILsQKDEEEVLVECRVRFLSFMGIGK 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 61557172 106 TDKRiFTFICkDSESNKHLCFVFDSEKCAEEITLTIGQAFDLAYRK 151
Cdd:cd01271  84 DVHT-FAFIM-DTGPQLFQCHVFWCEPNAGALSEAVQAACMLRYQK 127

leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. This model corresponds to the conserved region that shows high sequence similarity with the leucine zipper (ZIP) domain located at the C-terminus of TGF-beta-stimulated clone-22 domain (TSC22D) family transcription factors. The first helix of ZIP is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 61557172 150 RKFLESGG---KDVET-RKQIAGMQKRIQDLETENMELKNKVQDLE 191
Cdd:cd21937   8 KQHLGAPGpedADVEAlRLENEELKQKNEELEEENKELKAKLQQYE 53

Basic leucine zipper (bZIP) domain of Cyclic AMP-responsive element-binding protein 3 (CREB3) and similar proteins: a DNA-binding and dimerization domain; This subfamily is composed of CREB3 (also called LZIP or Luman), and the CREB3-like proteins CREB3L1 (or OASIS), CREB3L2, CREB3L3 (or CREBH), and CREB3L4 (or AIbZIP). They are type II membrane-associated members of the Basic leucine zipper (bZIP) family of transcription factors, with their N-termini facing the cytoplasm and their C-termini penetrating through the ER membrane. They contain an N-terminal transcriptional activation domain followed bZIP and transmembrane domains, and a C-terminal tail. They play important roles in ER stress and the unfolded protein response (UPR), as well as in many other biological processes such as cell secretion, bone and cartilage formation, and carcinogenesis. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 61557172 163 RKQ--IAGMQKRIQDLETENMELKNKVQDLENRLRT 196
Cdd:cd14689  20 RKKeyIDGLESRVAACTAENQELKKKVEELEKQNRS 55

Basic leucine zipper (bZIP) domain of Activating Transcription Factor-2 (ATF-2) and similar proteins: a DNA-binding and dimerization domain; ATF-2 is a sequence-specific DNA-binding protein that belongs to the Basic leucine zipper (bZIP) family of transcription factors. In response to stress, it activates a variety of genes including cyclin A, cyclin D, and c-Jun. ATF-2 also plays a role in the DNA damage response that is independent of its transcriptional activity. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.

                        10        20        30
                ....*....|....*....|....*....|..
gi 61557172 163 RK--QIAGMQKRIQDLETENMELKNKVQDLEN 192
Cdd:cd14687  19 RKkqWVQQLEEKVRKLESENKALKAEVDKLRE 50