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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  50 VEVTTPEEMFVENETDVKLPCTFTSAEVISSAASVSWSFQPEGAATRISFFYYSNGKPYTGKDIPFKDRVTWAGDLNKKD 129
Cdd:cd05715     1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024447853 130 ASISISNMQFQDNGTYICDVKNPPDIVVKPGEIRLRV 166
Cdd:cd05715    81 ASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  50 VEVTTPEEMFVENETDVKLPCTFTSAEVISSAASVSWSFQPEGAATRISFFYYSNGKPYTGKDIPFKDRVTWAGDLNKKD 129
Cdd:cd05715     1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024447853 130 ASISISNMQFQDNGTYICDVKNPPDIVVKPGEIRLRV 166
Cdd:cd05715    81 ASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117

Immunoglobulin V-Type;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853   65 DVKLPCTFTSAEVISSaaSVSWSFQPEGAATRISFFYYSNGKPYtgKDIPFKDRVTWAGDLNKKDASISISNMQFQDNGT 144
Cdd:smart00406   1 SVTLSCKFSGSTFSSY--YVSWVRQPPGKGLEWLGYIGSNGSSY--YQESYKGRFTISKDTSKNDVSLTISNLRVEDTGT 76

                   ....*
gi 2024447853  145 YICDV 149
Cdd:smart00406  77 YYCAV 81

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  50 VEVTTPEEMFVENETDVKLPCTFTSAEVISSAASVSWSFQPEGAATRISFFYYSNGKPYTGKDIPFKDRVTWAGDLNKKD 129
Cdd:cd05715     1 MEVYTPRELNVLNGSDVRLTCTFTSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVGRFKDRVSWAGNPSKKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024447853 130 ASISISNMQFQDNGTYICDVKNPPDIVVKPGEIRLRV 166
Cdd:cd05715    81 ASIVISNLQFSDNGTYTCDVKNPPDIVGGHGEIRLYV 117

Immunoglobulin (Ig)-like domain of protein zero (P0); 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 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  50 VEVTTPEEMFVENETDVKLPCTFTSAEVISSAASVSWSFQPEGAATRISFFYYSNGKPYTGKDIPFKDRVTWAGDLNKKD 129
Cdd:cd05879     1 IVVYTDREVYGTVGSDVTLSCSFWSSEWISDDISFTWHYQPDGSRDAISIFHYGKGQPYIDNVGPFKERIEWVGNPSRKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024447853 130 ASISISNMQFQDNGTYICDVKNPPDIVVKPGEIRLRV 166
Cdd:cd05879    81 GSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYV 117

Immunoglobulin V-Type;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853   65 DVKLPCTFTSAEVISSaaSVSWSFQPEGAATRISFFYYSNGKPYtgKDIPFKDRVTWAGDLNKKDASISISNMQFQDNGT 144
Cdd:smart00406   1 SVTLSCKFSGSTFSSY--YVSWVRQPPGKGLEWLGYIGSNGSSY--YQESYKGRFTISKDTSKNDVSLTISNLRVEDTGT 76

                   ....*
gi 2024447853  145 YICDV 149
Cdd:smart00406  77 YYCAV 81

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. 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. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  61 ENETdVKLPCTFTSaevISSAASVSWSFQ-PEGAATRIsFFYYSNGKPYTGKdipFKDRVTWAGDLNKkDASISISNMQF 139
Cdd:cd00099    12 EGES-VTLSCEVSS---SFSSTYIYWYRQkPGQGPEFL-IYLSSSKGKTKGG---VPGRFSGSRDGTS-SFSLTISNLQP 82

                  ....*...
gi 2024447853 140 QDNGTYIC 147
Cdd:cd00099    83 EDSGTYYC 90

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853   65 DVKLPCTFTSaeviSSAASVSWSFQPegaatrisffyysngkpytGKDIPFKDRVTWagDLNKKDASISISNMQFQDNGT 144
Cdd:smart00410  11 SVTLSCEASG----SPPPEVTWYKQG-------------------GKLLAESGRFSV--SRSGSTSTLTISNVTPEDSGT 65

                           90       100
                   ....*....|....*....|..
gi 2024447853  145 YICDVKNPPDIVVkpGEIRLRV 166
Cdd:smart00410  66 YTCAATNSSGSAS--SGTTLTV 85

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  65 DVKLPCTFTSaEVISSAASVSWsfQPEGAATRISFFYYSNGKpYTGKDIPFKDRVT-WAGDLNKKDASISISNMQFQDNG 143
Cdd:cd20984    14 DGILSCTFTP-DIKLSDIVIQW--LKEGDSGLVHEFKEGKDE-LSRQSPMFRGRTSlFADQVHVGNASLRLKNVQLTDAG 89

                  ....*...
gi 2024447853 144 TYICDVKN 151
Cdd:cd20984    90 TYLCIISN 97

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  66 VKLPCTFTSAEVISSAASVSWsfQPEGAATRISFFYysngkPYTGKDIPFKDRVTW-AGDLNK--KDASISISNMQFQDN 142
Cdd:cd20989    17 VTLPCHLLPPNMVTHVSQVTW--QRHDEHGSVAVFH-----PKQGPSFPESERLSFvAARLGAelRNASLAMFGLRVEDE 89

                          90       100
                  ....*....|....*....|....
gi 2024447853 143 GTYICDVKNPPDIVVKpGEIRLRV 166
Cdd:cd20989    90 GNYTCEFATFPQGSRS-GDTWLRV 112

Immunoglobulin (Ig)-like variable (V) domain of the Signal-Regulatory Protein (SIRP); The members here are composed of the immunoglobulin (Ig)-like domain of the Signal-Regulatory Protein (SIRP). The SIRPs belong to the "paired receptors" class of membrane proteins that comprise several genes coding for proteins with similar extracellular regions, but very different transmembrane/cytoplasmic regions with different (activating or inhibitory) signaling potentials. They are commonly on NK cells, but are also on many myeloid cells. Their extracellular region contains three immunoglobulin superfamily domains, a single V-set, and two C1-set IgSF domains. Their cytoplasmic tails that contain either ITIMs or transmembrane regions have positively charged residues that allow an association with adaptor proteins, such as DAP12/KARAP, containing ITAMs. There are 3 distinct SIRP members: alpha, beta, and gamma. SIRP alpha (also known as CD172a or SRC homology 2 domain-containing protein tyrosine phosphatase substrate 1/Shps-1) is a membrane receptor that interacts with a ligand CD47 expressed on many cells and gives an inhibitory signal through immunoreceptor tyrosine-based inhibition motifs in the cytoplasmic region that interact with phosphatases SHP-1 and SHP-2. SIRP beta has a short cytoplasmic region and associates with a transmembrane adapter protein DAP12 containing immunoreceptor tyrosine-based activation motifs to give an activating signal. SIRP gamma contains a very short cytoplasmic region lacking obvious signaling motifs, but also binds CD47 with much less affinity. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853 108 YTGKDIPFKdRVTWAGDLNKK---DASISISNMQFQDNGTYICdVK----NPPDIVVKPG 160
Cdd:cd16097    46 YNQKEGHFP-RVTTVSDLTKRnnmDFSIRISNITPADAGTYYC-VKfrkgSPDDVEFKSG 103

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  66 VKLPCTFTSaeviSSAASVSWSFQpegaatrisffyysngkpytGKDIPFKDRVTwaGDLNKKDASISISNMQFQDNGTY 145
Cdd:cd00096     1 VTLTCSASG----NPPPTITWYKN--------------------GKPLPPSSRDS--RRSELGNGTLTISNVTLEDSGTY 54

                  ....*..
gi 2024447853 146 ICDVKNP 152
Cdd:cd00096    55 TCVASNS 61

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  66 VKLPCtftSAEVISSAASVSWSFqpegaatrisffyysngkpyTGKDIPFKDRVtWAGDLNKKDASISISNMQFQDNGTY 145
Cdd:pfam00047  14 ATLTC---SASTGSPGPDVTWSK--------------------EGGTLIESLKV-KHDNGRTTQSSLLISNVTKEDAGTY 69

                  ....*....
gi 2024447853 146 ICDVKNPPD 154
Cdd:pfam00047  70 TCVVNNPGG 78

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  45 VKVSAVEVTTPEEmfveneTDVKLPCTFTSAEvisSAASVSWSFQpegaATRISFFYYSNGKpYTGKdipFKDRVTWAGd 124
Cdd:cd20946     2 VPSSQQVVTVVEN------QEVILSCKTPKKT---SSPRVEWKKL----QRDVTFVVFQNNK-IQGD---YKGRAEILG- 63

                          90       100       110
                  ....*....|....*....|....*....|
gi 2024447853 125 lnkkdASISISNMQFQDNGTYICDVKNPPD 154
Cdd:cd20946    64 -----TNITIKNVTRSDSGKYRCEVSARSD 88

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  65 DVKLPCTFT--SAEVISsaasvsWsFQPEGAATRISFFYYSN-----GKPYTGKDIPFKDRvtwagdLNKKDASISISNM 137
Cdd:cd16091    14 DCILPCSFTpgSEVVIH------W-YKQDSDIKVHSYYYGKDqlesqDQRYRNRTSLFKDQ------ISNGNASLLLRRV 80

                          90
                  ....*....|....
gi 2024447853 138 QFQDNGTYICDVKN 151
Cdd:cd16091    81 QLQDEGRYKCYTST 94

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024447853  53 TTPEEMFVENETDVKLPCTFTSaEVISSAAS---VSWSFQPEGAATRISFFYySNGKPYT--GKdipFKDRVTW--AGDL 125
Cdd:cd05877     2 TVQAKVFSHRGGNVTLPCRYHY-EPELSAPRkirVKWTKLEVDYAKEEDVLV-AIGTRHKsyGS---YQGRVFLrrADDL 76

                          90       100
                  ....*....|....*....|....
gi 2024447853 126 nkkDASISISNMQFQDNGTYICDV 149
Cdd:cd05877    77 ---DASLVITDLRLEDYGRYRCEV 97