Laminin B domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355      493 DGVAKYWRLPQRFLGDKVTAYGGKMEFEIEFSGS--GHHSSEPMVVLKGNQNILVHRvrnQEHVLRSDSPVRITVETYET 570
Cdd:smart00281    1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRrgGTHVSAPDVILEGNGLRISHP---AEGPPLPDELTTVEVRFREE 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 3881355      571 NYEQLNGAAATREDLLMVLADLDAFLIRATHVAHQTSTSLGDVSWEIAVD 620
Cdd:smart00281   78 NWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. 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 3881355    45 VQITVF-PSEKEVRDGRDVSFECRARTSdnSVYPTVRWARVGGPLPSSAHDSGGRLTINPVQLSDAGTYICVSDYNGNTV 123
Cdd:cd05754    1 IQVTVEePRSQEVRPGADVSFICRAKSK--SPAYTLVWTRVNGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNMLDTD 78

                 ....*..
gi 3881355   124 EARATLS 130
Cdd:cd05754   79 EATATLY 85

Low-density lipoprotein receptor domain class A;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 3881355     148 QCMADEKACGNNECVKNDYVCDGEPDCRDRSDEANC 183
Cdd:pfam00057    2 TCSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 3881355    1011 CHCNNHSPRG--CDSF-GRCLlCEHNTEGTHCERCKKGYYGDAtKGSPYDC 1058
Cdd:pfam00053    1 CDCNPHGSLSdtCDPEtGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49

Laminin-type epidermal growth factor-like domai;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 3881355      383 SCDTRGAVTPYPN-NYGTCECKSQVTGPNCDQCKPGAFHlseKSPEGC 429
Cdd:smart00180    2 DCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46

Laminin B domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355      493 DGVAKYWRLPQRFLGDKVTAYGGKMEFEIEFSGS--GHHSSEPMVVLKGNQNILVHRvrnQEHVLRSDSPVRITVETYET 570
Cdd:smart00281    1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRrgGTHVSAPDVILEGNGLRISHP---AEGPPLPDELTTVEVRFREE 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 3881355      571 NYEQLNGAAATREDLLMVLADLDAFLIRATHVAHQTSTSLGDVSWEIAVD 620
Cdd:smart00281   78 NWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3881355   286 GTTFSLTCKAVAVPEPYINWRLNWGPVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKGRVLATPDCIVRV 363
Cdd:cd05743    1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMVFGIPDGILTV 78

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. 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 3881355    45 VQITVF-PSEKEVRDGRDVSFECRARTSdnSVYPTVRWARVGGPLPSSAHDSGGRLTINPVQLSDAGTYICVSDYNGNTV 123
Cdd:cd05754    1 IQVTVEePRSQEVRPGADVSFICRAKSK--SPAYTLVWTRVNGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNMLDTD 78

                 ....*..
gi 3881355   124 EARATLS 130
Cdd:cd05754   79 EATATLY 85

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

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3881355      280 NLQVPRGTTFSLTCKAVAVPEPYINWRLNWG-PVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKG 351
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG 75

Low-density lipoprotein receptor domain class A;

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 3881355     231 SDCKPTEFQCHDRRqCVPSSFHCDGTNDCHDGSDEVGC 268
Cdd:pfam00057    1 STCSPNEFQCGSGE-CIPRSWVCDGDPDCGDGSDEENC 37

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355       51 PSEKEVRDGRDVSFECRARTSDNsvyPTVRWARVGGPLPS-------SAHDSGGRLTINPVQLSDAGTYICVSDYNGNTV 123
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPP---PEVTWYKQGGKLLAesgrfsvSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSA 77

                    ....*...
gi 3881355      124 EARATLSV 131
Cdd:smart00410   78 SSGTTLTV 85

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 3881355     955 CECNGHAS---QCDKEYGYCLdCQHNTEGDQCERCKPGFVGDaRRGTPNDC 1002
Cdd:pfam00053    1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGL-PSDPPQGC 49

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.

                            10        20        30
                    ....*....|....*....|....*....|...
gi 3881355      233 CKPTEFQCHDRRqCVPSSFHCDGTNDCHDGSDE 265
Cdd:smart00192    2 CPPGEFQCDNGR-CIPSSWVCDGVDDCGDGSDE 33

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 3881355   149 CMADEKACGNNECVKNDYVCDGEPDCRDRSDEANC 183
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

Laminin-type epidermal growth factor-like domai;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 3881355      955 CECN--GHAS-QCDKEYGYCLdCQHNTEGDQCERCKPGFVGDARRG 997
Cdd:smart00180    1 CDCDpgGSASgTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45

Laminin-type epidermal growth factor-like domai;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 3881355      383 SCDTRGAVTPYPN-NYGTCECKSQVTGPNCDQCKPGAFHlseKSPEGC 429
Cdd:smart00180    2 DCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46

Laminin-type epidermal growth factor-like domai;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 3881355     1010 PCHCNNHSPRGCDSF-GRCLlCEHNTEGTHCERCKKGYYGDATKG 1053
Cdd:smart00180    2 DCDPGGSASGTCDPDtGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 3881355   684 PAQGQCQCKASVIGPNCDRCAPNSFGLaPTNPQGC 718
Cdd:cd00055   16 PGTGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49

Laminin-type epidermal growth factor-like domai;

                            10        20        30
                    ....*....|....*....|....*....|....*
gi 3881355      684 PAQGQCQCKASVIGPNCDRCAPNSFGlapTNPQGC 718
Cdd:smart00180   15 PDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46

Laminin B domain;

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355      493 DGVAKYWRLPQRFLGDKVTAYGGKMEFEIEFSGS--GHHSSEPMVVLKGNQNILVHRvrnQEHVLRSDSPVRITVETYET 570
Cdd:smart00281    1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRrgGTHVSAPDVILEGNGLRISHP---AEGPPLPDELTTVEVRFREE 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 3881355      571 NYEQLNGAAATREDLLMVLADLDAFLIRATHVAHQTSTSLGDVSWEIAVD 620
Cdd:smart00281   78 NWQYYGGRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127

Immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of the human basement membrane heparan sulfate proteoglycan perlecan, also known as HSPG2, and similar proteins. Perlecan consists of five domains: domain I has three putative heparan sulfate attachment sites, domain II has four LDL receptor-like repeats, and one Ig-like repeat, domain III resembles the short arm of laminin chains, domain IV has multiple Ig-like repeats (21 repeats in human perlecan), and domain V resembles the globular G domain of the laminin A chain and internal repeats of EGF. Perlecan may participate in a variety of biological functions including cell binding, LDL-metabolism, basement membrane assembly and selective permeability, calcium binding, and growth- and neurite-promoting activities.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3881355   286 GTTFSLTCKAVAVPEPYINWRLNWGPVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKGRVLATPDCIVRV 363
Cdd:cd05743    1 GETVEFTCVATGVPTPIINWRLNWGHVPDSARVSITSEGGYGTLTIRDVKESDQGAYTCEAINTRGMVFGIPDGILTV 78

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. 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 3881355    45 VQITVF-PSEKEVRDGRDVSFECRARTSdnSVYPTVRWARVGGPLPSSAHDSGGRLTINPVQLSDAGTYICVSDYNGNTV 123
Cdd:cd05754    1 IQVTVEePRSQEVRPGADVSFICRAKSK--SPAYTLVWTRVNGTLPSRAMDFNGILTIRNVQLSDAGTYVCTGSNMLDTD 78

                 ....*..
gi 3881355   124 EARATLS 130
Cdd:cd05754   79 EATATLY 85

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

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3881355      280 NLQVPRGTTFSLTCKAVAVPEPYINWRLNWG-PVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKG 351
Cdd:smart00410    3 SVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSG 75

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355     271 PTVVDPPQtNLQVPRGTTFSLTCKAVAVPEPYINWRLNWGPVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVK 350
Cdd:pfam07679    1 PKFTQKPK-DVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSA 79

                   ....*.
gi 3881355     351 GRVLAT 356
Cdd:pfam07679   80 GEAEAS 85

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. 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 fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355   271 PTVVDPPQTNLQVPRGTTFSLTCKAVAVPEPYINWRLNWGPVCEPPRCLQTSEggyGTLTIHDAQPVDQGAYTCEAINVK 350
Cdd:cd20978    1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMERATVED---GTLTIINVQPEDTGYYGCVATNEI 77

                 ...
gi 3881355   351 GRV 353
Cdd:cd20978   78 GDI 80

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3881355   289 FSLTCKAVAVPEPYINWRLNWGPVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKGR 352
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGG 64

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355       51 PSEKEVRDGRDVSFECRARTSDNsvyPTVRWARVGGPLPS-------SAHDSGGRLTINPVQLSDAGTYICVSDYNGNTV 123
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPP---PEVTWYKQGGKLLAesgrfsvSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSA 77

                    ....*...
gi 3881355      124 EARATLSV 131
Cdd:smart00410   78 SSGTTLTV 85

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 3881355     955 CECNGHAS---QCDKEYGYCLdCQHNTEGDQCERCKPGFVGDaRRGTPNDC 1002
Cdd:pfam00053    1 CDCNPHGSlsdTCDPETGQCL-CKPGVTGRHCDRCKPGYYGL-PSDPPQGC 49

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.

                            10        20        30
                    ....*....|....*....|....*....|...
gi 3881355      233 CKPTEFQCHDRRqCVPSSFHCDGTNDCHDGSDE 265
Cdd:smart00192    2 CPPGEFQCDNGR-CIPSSWVCDGVDDCGDGSDE 33

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355   273 VVDPPQtNLQVPRGTTFSLTCKAVAVPEPYINWRLNWGPVCE-PPRCLQTSEGgyGTLTIHDAQPVDQGAYTCEAINVKG 351
Cdd:cd04978    2 WIIEPP-SLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPaPEDMRRTVDG--RTLIFSNLQPNDTAVYQCNASNVHG 78

                 ....
gi 3881355   352 RVLA 355
Cdd:cd04978   79 YLLA 82

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355    51 PSEKEVRDGRDVSFECRARTSDNsvyPTVRWARVGGPLPSSA--HDSGGRLTINPVQLSDAGTYICVSDYNGNTVEARAT 128
Cdd:cd05728    6 ISDTEADIGSSLRWECKASGNPR---PAYRWLKNGQPLASENriEVEAGDLRITKLSLSDSGMYQCVAENKHGTIYASAE 82

                 ...
gi 3881355   129 LSV 131
Cdd:cd05728   83 LAV 85

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. 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. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355   270 QPTVVDPPqTNLQVPRGTTFSLTCKAVAVPEPYINWRLNWGPVcEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINV 349
Cdd:cd20976    1 APSFSSVP-KDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPL-QYAADRSTCEAGVGELHIQDVLPEDHGTYTCLAKNA 78

                         90
                 ....*....|....
gi 3881355   350 KGRVlatpDCIVRV 363
Cdd:cd20976   79 AGQV----SCSAWV 88

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 3881355   149 CMADEKACGNNECVKNDYVCDGEPDCRDRSDEANC 183
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. 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. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355   277 PQTNLQVPRGTTFSLTCKAVAVPEPYINWRLNWGPVCEPPRC-LQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKGRvlA 355
Cdd:cd20973    3 TLRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFqIDQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGE--A 80

                 ....*...
gi 3881355   356 TPDCIVRV 363
Cdd:cd20973   81 TCSAELTV 88

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.

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                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3881355    62 VSFECRARTSDNsvyPTVRWARVGGPLPSSAHDS------GGRLTINPVQLSDAGTYICV 115
Cdd:cd00096    1 VTLTCSASGNPP---PTITWYKNGKPLPPSSRDSrrselgNGTLTISNVTLEDSGTYTCV 57