C-terminal SARAH domain of mammalian STE20-like protein kinase 1 (MST1); MST1, also called serine/threonine-protein kinase 4, MST-1, STE20-like kinase MST1, or serine/threonine-protein kinase (STK) Krs-2, is a STE20 family stress-activated, pro-apoptotic STK which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. It is a key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain, which mediates homodimerization of MST1. The MST1 SARAH domain also interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
5XCV_E      117 DYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQCKRQPILDAIEAK 165
Cdd:cd21887   1 DYEFLKSWSVEELQRRLASLDPMMEQEIEEIRQKYQSKRQPILDAIEAK 49

C-terminal SARAH domain of mammalian STE20-like protein kinase 1 (MST1); MST1, also called serine/threonine-protein kinase 4, MST-1, STE20-like kinase MST1, or serine/threonine-protein kinase (STK) Krs-2, is a STE20 family stress-activated, pro-apoptotic STK which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. It is a key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain, which mediates homodimerization of MST1. The MST1 SARAH domain also interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
5XCV_E      117 DYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQCKRQPILDAIEAK 165
Cdd:cd21887   1 DYEFLKSWSVEELQRRLASLDPMMEQEIEEIRQKYQSKRQPILDAIEAK 49

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E          9 TQPNSVSTNLGSTVKLSCK-RSTGNIGSNYVNWYQQHEGRSPTTMI--YRDDKRPDGVPDRFSGSIDRSSNSALLTINNV 85
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTySSSMSEASTSVYWYRQPPGKGPTFLIayYSNGSEEGVKKGRFSGRGDPSNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
5XCV_E         86 QTEDEADYFCHSYSSGI-VFGGGTKLTVL 113
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEgVFGKGTRLTVL 109

C-terminal SARAH domain of mammalian STE20-like protein kinase 1 (MST1); MST1, also called serine/threonine-protein kinase 4, MST-1, STE20-like kinase MST1, or serine/threonine-protein kinase (STK) Krs-2, is a STE20 family stress-activated, pro-apoptotic STK which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. It is a key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain, which mediates homodimerization of MST1. The MST1 SARAH domain also interacts with Rassf1 and Rassf5 by forming a heterodimer which mediates the apoptosis process.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
5XCV_E      117 DYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQCKRQPILDAIEAK 165
Cdd:cd21887   1 DYEFLKSWSVEELQRRLASLDPMMEQEIEEIRQKYQSKRQPILDAIEAK 49

Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E        7 VLTQ-PNSVSTNLGSTVKLSCKRSTgNIGSNYVNWYQQHEGRSPTTMIYRDDKRPDGVPDRFSGSidRSSNSALLTINNV 85
Cdd:cd04980   2 VMTQsPASLSVSPGERVTISCKASQ-SISSNYLAWYQQKPGQAPKLLIYYASTLHSGVPSRFSGS--GSGTDFTLTISSV 78

                        90       100
                ....*....|....*....|....*...
5XCV_E       86 QTEDEADYFC-HSYSSGIVFGGGTKLTV 112
Cdd:cd04980  79 EPEDAAVYYCqQGYTFPYTFGGGTKLEI 106

C-terminal SARAH domain found in the mammalian STE20-like protein kinase (MST) subfamily; The MST subfamily includes MST1 and MST2, as well as Drosophila melanogaster homolog protein, Hippo (Hpo). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 and MST2 are STE20 family stress-activated, pro-apoptotic serine/threonine-protein kinases which, following caspase-cleavage, enter the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. They are key components of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. Hpo, also called STE20-like kinase MST (dMST), is the Drosophila homolog of STE20-like protein kinases, MST1 and MST2. It is a STE20 family serine/threonine-protein kinase that functions as a tumor suppressor by restricting cell proliferation, and promotes apoptosis in conjunction with salvador and warts. Hpo plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. This model corresponds to the C-terminal SARAH (Salvador-RassF-Hippo) domain of mammalian STE20-like protein kinases and the Drosophila melanogaster homolog Hippo.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
5XCV_E      118 YEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQCKRQPILDAIEAK 165
Cdd:cd21884   1 FEFLKSLSYEELQERLALLDPEMEREIEELRKRYQAKRQPILDAIEAK 48

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E        9 TQ-PNSVSTNLGSTVKLSCKRSTgnIGSNYVNWYQQHEGRSPTTMIYRDDKRPDGVPDRFSGSIDRSSNSALLTINNVQT 87
Cdd:cd04983   2 TQsPQSLSVQEGENVTLNCNYST--STFYYLFWYRQYPGQGPQFLIYISSDSGNKKKGRFSATLDKSRKSSSLHISAAQL 79

                        90       100
                ....*....|....*....|....*....
5XCV_E       88 EDEADYFC---HSYSSG-IVFGGGTKLTV 112
Cdd:cd04983  80 SDSAVYFCalsESGGTGkLTFGKGTRLTV 108

Immunoglobulin V-Type;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5XCV_E          21 TVKLSCKRSTGNIGSNYVNWYQQHEGRSPTTMIYRDDKR----PDGVPDRFSGSIDRSSNSALLTINNVQTEDEADYFC 95
Cdd:smart00406   1 SVTLSCKFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGssyyQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYC 79

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigens as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain the standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E        8 LTQPN-SVSTNLGSTVKLSCKRSTGNIGSNYVNWYQQHEGRSPTTMIY-----RDDKRPDGVPDRFSGSIDRSSNSALLT 81
Cdd:cd04982   1 LEQPQlSITREESKSVTISCKVSGIDFSTTYIHWYRQKPGQALERLLYvsstsAVRKDSGKTKNKFEARKDVGKSTSTLT 80

                        90       100       110
                ....*....|....*....|....*....|....*.
5XCV_E       82 INNVQTEDEADYFCHSYSSGI-----VFGGGTKLTV 112
Cdd:cd04982  81 ITNLEKEDSATYYCAYWESGSgyyikVFGSGTKLIV 116

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) beta chain; The members here are composed of the immunoglobulin (Ig) variable domain of the beta chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta, polypeptide chains with variable (V) and constant (C) regions. This group includes the variable domain of the alpha chain of alpha/beta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E        8 LTQ-PNSVSTNLGSTVKLSCKRstgNIGSNYVNWYQQHEGRSPTTMIY---RDDKRPDGVP-DRFSGSIDRSSNSALlTI 82
Cdd:cd05899   1 VTQsPRYLIKRRGQSVTLRCSQ---KSGHDNMYWYRQDPGKGLQLLFYsygGGLNEEGDLPgDRFSASRPSLTRSSL-TI 76

                        90       100       110
                ....*....|....*....|....*....|....*
5XCV_E       83 NNVQTEDEADYFCHSySSGI-----VFGGGTKLTV 112
Cdd:cd05899  77 KSAEPEDSAVYLCAS-SLGGgadeaYFGPGTRLTV 110

Immunoglobulin (Ig) heavy chain (H), variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E        8 LTQPNSVSTNLGSTVKLSCKRSTGNIGSNYVNWYQQHEGRSPTTM--IYRDDKRP---DGVPDRFSGSIDRSSNSALLTI 82
Cdd:cd04981   2 LQESGPGLVKPGQSLKLSCKASGFTFTSYGMGWVRQAPGKGLEWIglIYPGGGDTyyaDSFKGRFTITRDTSKSTAYLQL 81

                        90       100       110
                ....*....|....*....|....*....|....*.
5XCV_E       83 NNVQTEDEADYFC-----HSYSSGI-VFGGGTKLTV 112
Cdd:cd04981  82 NSLTSEDTAVYYCarglgGYGYSYFdYWGQGTTVTV 117

C-terminal SARAH domain found in scaffold protein salvador (Sav), Ras-association domain proteins, and mammalian STE20-like protein kinases (MST); The SARAH (Salvador-RassF-Hippo) domain family includes scaffold protein salvador (Sav), Ras-association domain proteins (RASSF1-6), and mammalian STE20-like protein kinase (MST) subfamily members (MST1-2 and Hippo). Sav is a scaffold protein mainly found in metazoans. Drosophila melanogaster Sav, also called Shar-pei (SHRP), promotes both cell cycle exit and apoptosis in Drosophila. It plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Human protein salvador homolog 1, also called 45 kDa WW domain protein (WW45), acts as a mammalian sterile 20-like kinase 1 (MST1)-binding protein required to enhance MST1-mediated apoptosis. It is a regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway. Classical RASSF proteins interact either directly or indirectly with activated Ras. Ras proteins are small GTPases that are involved in cellular signal transduction. They seem to modulate some of the growth inhibitory responses mediated by Ras and may serve as tumor suppressor genes. RASSF1-6 contains a conserved SARAH motif adjacent to the RA domain that functions in scaffolding and regulatory interactions. MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 and MST2 are STE20 family stress-activated, pro-apoptotic serine/threonine-protein kinases which, following caspase-cleavage, enter the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. They are key components of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. Hippo (Hpo), also called STE20-like kinase MST (dMST), is the Drosophila homolog of STE20-like protein kinases, MST1 and MST2. It is a STE20 family serine/threonine-protein kinase that functions as a tumor suppressor by restricting cell proliferation and promotes apoptosis in conjunction with salvador and warts. Hpo also plays a key role in the Hippo/SWH signaling pathway. This model corresponds to the C-terminal SARAH domain, a characteristic coiled-coil structure. It is a small helical module that is important in signal-transduction networks. The central function of the SARAH domain seems to be the mediation of homo- and heterodimerization between SARAH domain-containing proteins.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
5XCV_E      120 FLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQCKRQPILDAIEA 164
Cdd:cd21883   1 QLKNFSLPELQMFLKMLDPEEEREIEQLVKKYTAYRQAILDALEE 45

Immunoglobulin (Ig) variable (V) domain of Cluster of Differentiation (CD) 8 beta chain; The members here are composed of the immunoglobulin (Ig)-like domain in Cluster of Differentiation (CD) 8 beta. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E       11 PNSVSTNLGSTVKLSC--KRSTGNIGsnyVNWYQQHEGRSPttmiyrdDKR--------PDGV--------PDRFSGSID 72
Cdd:cd07700   5 PGSLLVQTNQTVKMSCeaKTSPKNTR---IYWLRQRQAPSK-------DSHfeflaswdPSKGivygegvdQEKLIILSD 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
5XCV_E       73 RSSNSALLTINNVQTEDEADYFCHSY-SSGIVFGGGTKLTV 112
Cdd:cd07700  75 SDSSRYILSLMSVKPEDSGTYFCMTVgSPELIFGTGTKLSV 115

T-cell receptor Mu, Heavy chain, variable (V) domain; The members here are composed of the immunoglobulin (Ig) heavy chain (H), variable (V) domain of the T-cell receptor Mu. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which can associate with any of the heavy chains. This family includes alpha, gamma, delta, epsilon, and mu heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E       19 GSTVKLSCKRSTGNIGSNYVNWYQQHEGRSPTTMIYRDDKRPDGVPDRFSGSIDRSSNSALLTINNVQTEDEADYFCHSY 98
Cdd:cd16095  15 GKTLSLKCQTSGFQFNTSQLSWYLWVPGHAPLWLTSLDHISTKVSEDRITSSREDTNSQIFLQIKGLGLRDSGQYHCARR 94

                        90       100
                ....*....|....*....|
5XCV_E       99 ------SSGIVFGGGTKLTV 112
Cdd:cd16095  95 vgygddTDKLIFGPGTDVIV 114

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E       18 LGSTVKLSCkRSTGNIGSNYVNWyQQHEGRSPTTMIYRDDKRpdGVP------DRFSGSIDRSSNSALlTINNVQTEDEA 91
Cdd:cd05846  12 LGGNATLSC-NLTLPEEVLQVTW-QKIKASSPENIVTYSKKY--GVKiqpsyvRRISFTSSGLNSTSI-TIWNVTLEDEG 86

                        90       100
                ....*....|....*....|...
5XCV_E       92 DYFC--HSYSSGIVfGGGTKLTV 112
Cdd:cd05846  87 CYKClfNTFPDGIK-SGTACLTV 108

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E       19 GSTVKLSCK-RSTGNIGSNY-VNWYQQHEGRSPTT---MIYRDDKRPDGVP---DRFSGSIDRSSNSALLTINNVQTEDE 90
Cdd:cd05715  14 GSDVRLTCTfTSCYTVGDAFsVTWTYQPEGGNTTEsmfHYSKGKPYILKVGrfkDRVSWAGNPSKKDASIVISNLQFSDN 93

                ....*
5XCV_E       91 ADYFC 95
Cdd:cd05715  94 GTYTC 98

Third immunoglobulin (Ig) domain of contactin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig) domain of contactins. Contactins are neural cell adhesion molecules and are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. The first four Ig domains form the intermolecular binding fragment, which arranges as a compact U-shaped module via contacts between Ig domains 1 and 4, and between Ig domains 2 and 3. Contactin-2 (TAG-1, axonin-1) may play a part in the neuronal processes of neurite outgrowth, axon guidance and fasciculation, and neuronal migration. This group also includes contactin-1 and contactin-5. The different contactins show different expression patterns in the central nervous system. During development and in adulthood, contactin-2 is transiently expressed in subsets of central and peripheral neurons. Contactin-5 is expressed specifically in the rat postnatal nervous system, peaking at about 3 weeks postnatal, and a lack of contactin-5 (NB-2) results in an impairment of neuronal activity in the rat auditory system. Contactin-5 is highly expressed in the adult human brain in the occipital lobe and in the amygdala. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5XCV_E       10 QPNSVSTNLGSTVKLSCkRSTGNIGSNyVNWyqqhegrspttmiyrddKRPDGVPdrFSGSIDRSSNsALLTINNVQTED 89
Cdd:cd04968   7 FPADTYALKGQTVTLEC-FALGNPVPQ-IKW-----------------RKVDGSP--SSQWEITTSE-PVLEIPNVQFED 64

                ....*.
5XCV_E       90 EADYFC 95
Cdd:cd04968  65 EGTYEC 70