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 86565338  163 YWpLGPPPNTNTSEGEKVIFDCTTYGKPTPKVTFYKNGVEIESQKDDRYLIEGTRLTIFDVKKgtygKGDNAVYQCKSEN 242
Cdd:cd04978    1 YW-IIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGRTLIFSNLQ----PNDTAVYQCNASN 75

                         90
                 ....*....|....
gi 86565338  243 KHGWLWTNFYLNLL 256
Cdd:cd04978   76 VHGYLLANAFLHVL 89

Fibronectin type 3 domain [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  758 KTVVFGPSATQGTLTDLKPATLNHAYIQVTNGAHEGSASDTIDFQTDEGVPSPVRSLRAYPMNSkvggekGVVVLVWKKP 837
Cdd:COG3401  183 TSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTP------GSVTLSWDPV 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  838 rqTNGKLARYEVEYCKTQNGKLVEKScprkqiDADSKEIRITGLENETPYRFILRAHTSAGEGDPNSSDATTLPETTAag 917
Cdd:COG3401  257 --TESDATGYRVYRSNSGDGPFTKVA------TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTP-- 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  918 vdPGVPS-LVENAIGDKYFNVSFRPAKYDDESRapvgntYEVQYKPQDADEWETVKPADDGLTVHVDGLSPGTKYDVRVA 996
Cdd:COG3401  327 --PAAPSgLTATAVGSSSITLSWTASSDADVTG------YNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVT 398

                        250       260
                 ....*....|....*....|....*...
gi 86565338  997 ALQVDPEGGETTKTLSGISKITTTGTSS 1024
Cdd:COG3401  399 AVDAAGNESAPSEEVSATTASAASGESL 426

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 86565338    353 PTIVQPfPRVEEVRmAGEEMRLACDATADNQLEVkyEWLVDGKSLPEDRissgHYKI---DDDHSLVISNPTQDDTAKYK 429
Cdd:pfam07679    1 PKFTQK-PKDVEVQ-EGESARFTCTVTGTPDPEV--SWFKDGQPLRSSD----RFKVtyeGGTYTLTISNVQPDDSGKYT 72

                           90
                   ....*....|....*..
gi 86565338    430 CVVSTKLDQVEKEIKIQ 446
Cdd:pfam07679   73 CVATNSAGEAEASAELT 89

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 86565338   76 QSSPIALQGNQHKLHCFFSGYPAPKPRWFHNGREISEDSdaagFRFESYGKTL-VFNVTQDKAGKYDCRFA-TQQDIDRT 153
Cdd:cd05731    2 ESSTMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGR----TKFENFNKTLkIENVSEADSGEYQCTASnTMGSARHT 77

                 ....*.
gi 86565338  154 FNVVVE 159
Cdd:cd05731   78 ISVTVE 83

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86565338  483 APIKEFWVQYQidsETEGSQWRTHPVPSAAHPNDKIDNnlrhttgdatvsLQPFGKYVFRVIARNSVGDSA 553
Cdd:cd00063   29 GPITGYVVEYR---EKGSGDWKEVEVTPGSETSYTLTG------------LKPGTEYEFRVRAVNGGGESP 84

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 86565338  163 YWpLGPPPNTNTSEGEKVIFDCTTYGKPTPKVTFYKNGVEIESQKDDRYLIEGTRLTIFDVKKgtygKGDNAVYQCKSEN 242
Cdd:cd04978    1 YW-IIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGRTLIFSNLQ----PNDTAVYQCNASN 75

                         90
                 ....*....|....
gi 86565338  243 KHGWLWTNFYLNLL 256
Cdd:cd04978   76 VHGYLLANAFLHVL 89

Fibronectin type 3 domain [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  758 KTVVFGPSATQGTLTDLKPATLNHAYIQVTNGAHEGSASDTIDFQTDEGVPSPVRSLRAYPMNSkvggekGVVVLVWKKP 837
Cdd:COG3401  183 TSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTP------GSVTLSWDPV 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  838 rqTNGKLARYEVEYCKTQNGKLVEKScprkqiDADSKEIRITGLENETPYRFILRAHTSAGEGDPNSSDATTLPETTAag 917
Cdd:COG3401  257 --TESDATGYRVYRSNSGDGPFTKVA------TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTP-- 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  918 vdPGVPS-LVENAIGDKYFNVSFRPAKYDDESRapvgntYEVQYKPQDADEWETVKPADDGLTVHVDGLSPGTKYDVRVA 996
Cdd:COG3401  327 --PAAPSgLTATAVGSSSITLSWTASSDADVTG------YNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVT 398

                        250       260
                 ....*....|....*....|....*...
gi 86565338  997 ALQVDPEGGETTKTLSGISKITTTGTSS 1024
Cdd:COG3401  399 AVDAAGNESAPSEEVSATTASAASGESL 426

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  571 NPDEVAAKGTSPENIIVQWKPMsrEEWNGADFHYVVKYRPKDEdqrvGDWKEVAVEDPFADRVTVnlddeKDVKPFQPYE 650
Cdd:cd00063    3 PPTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYREKGS----GDWKEVEVTPGSETSYTL-----TGLKPGTEYE 71

                         90       100
                 ....*....|....*....|...
gi 86565338  651 VQVQAVNSEGRTNVVpETVEGRT 673
Cdd:cd00063   72 FRVRAVNGGGESPPS-ESVTVTT 93

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  808 PSPVRSLRAYPMNSkvggekGVVVLVWKKPRQTNGKLARYEVEYCKTQNGKLVEksCPRKqiDADSKEIRITGLENETPY 887
Cdd:cd00063    1 PSPPTNLRVTDVTS------TSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKE--VEVT--PGSETSYTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|...
gi 86565338  888 RFILRAHTSAGEGDP-NSSDATT 909
Cdd:cd00063   71 EFRVRAVNGGGESPPsESVTVTT 93

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338     269 EEVEAVAGKKVTLECKFFASPNAAVKW--EAPMISGSKGNQIPADAYGVGKLVFSEVTAAEEGEYECIGTNKYGQATGLI 346
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPPEVTWykQGGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                    ....
gi 86565338     347 TLKV 350
Cdd:smart00410   82 TLTV 85

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338   76 QSSPIALQGNQHKLHCFFSGYPAPKPRWFHNGREISEDSdaagFRFESYGKTL-VFNVTQDKAGKYDCRFA-TQQDIDRT 153
Cdd:cd05731    2 ESSTMVLRGGVLLLECIAEGLPTPDIRWIKLGGELPKGR----TKFENFNKTLkIENVSEADSGEYQCTASnTMGSARHT 77

                 ....*.
gi 86565338  154 FNVVVE 159
Cdd:cd05731   78 ISVTVE 83

Fibronectin type III domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338    809 SPVRSLRAYPMNSkvggekGVVVLVWKKPRQTNGKLARYEVEYCKTQNGKLVekscPRKQIDADSKEIRITGLENETPYR 888
Cdd:pfam00041    1 SAPSNLTVTDVTS------TSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPW----NEITVPGTTTSVTLTGLKPGTEYE 70

                           90
                   ....*....|....
gi 86565338    889 FILRAHTSAGEGDP 902
Cdd:pfam00041   71 VRVQAVNGGGEGPP 84

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 86565338  373 RLACDATADNQLEVKyeWLVDGKSLPEDRISSGHYkIDDDHSLVISNPTQDDTAKYKCVVSTKL 436
Cdd:cd00096    2 TLTCSASGNPPPTIT--WYKNGKPLPPSSRDSRRS-ELGNGTLTISNVTLEDSGTYTCVASNSA 62

Fifth immunoglobulin (Ig) domain of contactin; The members here are composed of the fifth 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  260 PQLLIDPGKEEVEAVAGKKVTLECKFFASPNAAVKWeapmisgSKGNQIPADAYGV-----GKLVFSEVTAAEEGEYECI 334
Cdd:cd04969    1 PDFELNPVKKKILAAKGGDVIIECKPKASPKPTISW-------SKGTELLTNSSRIcilpdGSLKIKNVTKSDEGKYTCF 73

                         90
                 ....*....|....*.
gi 86565338  335 GTNKYGQATGLITLKV 350
Cdd:cd04969   74 AVNFFGKANSTGSLSV 89

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  680 SIPSGLRVLEKSGTTVTLAWNGvdPQTANGNFTGYKITYwvdeadqdsddsseddeddekrkfrwkrsiRVKRQSGIRKT 759
Cdd:cd00063    2 SPPTNLRVTDVTSTSVTLSWTP--PEDDGGPITGYVVEY------------------------------REKGSGDWKEV 49

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 86565338  760 VVFGPSATQGTLTDLKPATLNHAYIQVTNGAHEGSASDTIDFQT 803
Cdd:cd00063   50 EVTPGSETSYTLTGLKPGTEYEFRVRAVNGGGESPPSESVTVTT 93

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338     74 VNQSSPIALQGNQHKLHCFFSGYPAPKPRWFHNGREISEDSDAAGFRFESYGKTLVFNVTQDKAGKYDCR 143
Cdd:pfam13927    6 VSPSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86565338  483 APIKEFWVQYQidsETEGSQWRTHPVPSAAHPNDKIDNnlrhttgdatvsLQPFGKYVFRVIARNSVGDSA 553
Cdd:cd00063   29 GPITGYVVEYR---EKGSGDWKEVEVTPGSETSYTLTG------------LKPGTEYEFRVRAVNGGGESP 84

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338      76 QSSPIALQGNQHKLHCFFSGYPAPKPRWFHNGREISEDSDAAGFRFESYGKTLVF-NVTQDKAGKYDCRfATQQDIDRTF 154
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTIsNVTPEDSGTYTCA-ATNSSGSASS 79

                    ....*
gi 86565338     155 NVVVE 159
Cdd:smart00410   80 GTTLT 84

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 86565338  163 YWpLGPPPNTNTSEGEKVIFDCTTYGKPTPKVTFYKNGVEIESQKDDRYLIEGTRLTIFDVKKgtygKGDNAVYQCKSEN 242
Cdd:cd04978    1 YW-IIEPPSLVLSPGETGELICEAEGNPQPTITWRLNGVPIEPAPEDMRRTVDGRTLIFSNLQ----PNDTAVYQCNASN 75

                         90
                 ....*....|....
gi 86565338  243 KHGWLWTNFYLNLL 256
Cdd:cd04978   76 VHGYLLANAFLHVL 89

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 86565338  162 PYWPLGPPPNTNTSEGEKVIFDCTTYGKPTPKVTFYKNGVEIeSQKDDRYLIEGTRLTIFDVKkgtygKGDNAVYQCKSE 241
Cdd:cd20978    1 PKFIQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPL-QGPMERATVEDGTLTIINVQ-----PEDTGYYGCVAT 74

                         90
                 ....*....|...
gi 86565338  242 NKHGWLWTNFYLN 254
Cdd:cd20978   75 NEIGDIYTETLLH 87

Fibronectin type 3 domain [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  758 KTVVFGPSATQGTLTDLKPATLNHAYIQVTNGAHEGSASDTIDFQTDEGVPSPVRSLRAYPMNSkvggekGVVVLVWKKP 837
Cdd:COG3401  183 TSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTPTTPPSAPTGLTATADTP------GSVTLSWDPV 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  838 rqTNGKLARYEVEYCKTQNGKLVEKScprkqiDADSKEIRITGLENETPYRFILRAHTSAGEGDPNSSDATTLPETTAag 917
Cdd:COG3401  257 --TESDATGYRVYRSNSGDGPFTKVA------TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTP-- 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  918 vdPGVPS-LVENAIGDKYFNVSFRPAKYDDESRapvgntYEVQYKPQDADEWETVKPADDGLTVHVDGLSPGTKYDVRVA 996
Cdd:COG3401  327 --PAAPSgLTATAVGSSSITLSWTASSDADVTG------YNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVT 398

                        250       260
                 ....*....|....*....|....*...
gi 86565338  997 ALQVDPEGGETTKTLSGISKITTTGTSS 1024
Cdd:COG3401  399 AVDAAGNESAPSEEVSATTASAASGESL 426

Immunoglobulin I-set domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338    166 LGPPPNTNTSEGEKVIFDCTTYGKPTPKVTFYKNGVEIESqkDDRYLI----EGTRLTIFDVKkgtygKGDNAVYQCKSE 241
Cdd:pfam07679    4 TQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRS--SDRFKVtyegGTYTLTISNVQ-----PDDSGKYTCVAT 76

                   ....
gi 86565338    242 NKHG 245
Cdd:pfam07679   77 NSAG 80

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  571 NPDEVAAKGTSPENIIVQWKPMsrEEWNGADFHYVVKYRPKDEdqrvGDWKEVAVEDPFADRVTVnlddeKDVKPFQPYE 650
Cdd:cd00063    3 PPTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYREKGS----GDWKEVEVTPGSETSYTL-----TGLKPGTEYE 71

                         90       100
                 ....*....|....*....|...
gi 86565338  651 VQVQAVNSEGRTNVVpETVEGRT 673
Cdd:cd00063   72 FRVRAVNGGGESPPS-ESVTVTT 93

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  808 PSPVRSLRAYPMNSkvggekGVVVLVWKKPRQTNGKLARYEVEYCKTQNGKLVEksCPRKqiDADSKEIRITGLENETPY 887
Cdd:cd00063    1 PSPPTNLRVTDVTS------TSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKE--VEVT--PGSETSYTLTGLKPGTEY 70

                         90       100
                 ....*....|....*....|...
gi 86565338  888 RFILRAHTSAGEGDP-NSSDATT 909
Cdd:cd00063   71 EFRVRAVNGGGESPPsESVTVTT 93

Fibronectin type 3 domain [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  525 TTGDATVSLQPFGKYVFRVIARNSVGDSAarLAKDQCETPAKQPDKNPDEVAAKGTSPENIIVQWKPmsrEEWNGADfHY 604
Cdd:COG3401  191 TLVDGGGDIEPGTTYYYRVAATDTGGESA--PSNEVSVTTPTTPPSAPTGLTATADTPGSVTLSWDP---VTESDAT-GY 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  605 VVkYRPKDEDqrvGDWKEVAvedpfadRVTVNLDDEKDVKPFQPYEVQVQAVNSEGRTNVVPETVEGRTGEGVPSSiPSG 684
Cdd:COG3401  265 RV-YRSNSGD---GPFTKVA-------TVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTTDLTPPAA-PSG 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  685 LRVLEKSGTTVTLAWNGVDpqtaNGNFTGYKItYwvdeadqdsddsseddeddekrkfrwkrsiRVKRQSGIRKTVVFGP 764
Cdd:COG3401  333 LTATAVGSSSITLSWTASS----DADVTGYNV-Y------------------------------RSTSGGGTYTKIAETV 377

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  765 SATQGTLTDLKPATLNHAYIQVTNGAH-EGSASDTIDFQTDEGVPSPVRSLRAYPMNSKVGGEKGVVVLVWKKPRQTNGK 843
Cdd:COG3401  378 TTTSYTDTGLTPGTTYYYKVTAVDAAGnESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAV 457

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  844 LARYEVEYcktqNGKLVekscprkqiDADSKEIRITGLENETPYRFILRAHTSAGEGDPNSSDATTLPETTAAGVDPGVP 923
Cdd:COG3401  458 LADGGDTG----NAVPF---------TTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAP 524

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 86565338  924 SLVENAIGDKYFNVSFRPAKYD-DESRAPVGNTYEVQY 960
Cdd:COG3401  525 DGTPNVTGASPVTVGASTGDVLiTDLVSLTTSASSSVS 562

First immunoglobulin (Ig)-like constant domain in Robo (roundabout) receptors, and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain in Roundabout (Robo) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit1, Slit2, Slit3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit1, Slit2,and Slit3 are expressed at the ventral midline. Robo3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  169 PPNTNTSEGEKVIFDCTTYGKPTPKVTFYKNGVEIESQKDD----RYLIEGTRLTIFDVKKGTYGKGDNAVYQCKSENKH 244
Cdd:cd07693    7 PSDLIVSKGDPATLNCKAEGRPTPTIQWLKNGQPLETDKDDprshRIVLPSGSLFFLRVVHGRKGRSDEGVYVCVAHNSL 86

                 .
gi 86565338  245 G 245
Cdd:cd07693   87 G 87

First immunoglobulin (Ig)-like domain in neogenin, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain in neogenin and related proteins. Neogenin is a cell surface protein which is expressed in the developing nervous system of vertebrate embryos in the growing nerve cells. It is also expressed in other embryonic tissues and may play a general role in developmental processes such as cell migration, cell-cell recognition, and tissue growth regulation. Included in this group is the tumor suppressor protein DCC which is deleted in colorectal carcinoma. DCC and neogenin each have four Ig-like domains followed by six fibronectin type III domains, a transmembrane domain, and an intracellular domain. 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 86565338  162 PYWPLGPPPNTNTSEGEKVIFDCTTYGKPTPKVTFYKNGVEIESQKDDRY--LIEGTrLTIFDVKKGTYGKGDNAVYQCK 239
Cdd:cd05722    1 ELYFLSEPSDIVAMRGGPVVLNCSAESDPPPKIEWKKDGVLLNLVSDERRqqLPNGS-LLITSVVHSKHNKPDEGFYQCV 79

                 ....
gi 86565338  240 SENK 243
Cdd:cd05722   80 AQNE 83

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338     571 NPDEVAAKGTSPENIIVQWKPMSREEWNGADFHYVVKYRPKDEdqrvgDWKEVAVEDPfADRVTVnlddeKDVKPFQPYE 650
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGS-----EWKEVNVTPS-STSYTL-----TGLKPGTEYE 71

                            90
                    ....*....|.
gi 86565338     651 VQVQAVNSEGR 661
Cdd:smart00060   72 FRVRAVNGAGE 82

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86565338  920 PGVPSLVE-NAIGDKYFNVSFRPAKYDDesrAPVGNtYEVQYKPQDADEWETVKPAD-DGLTVHVDGLSPGTKYDVRVAA 997
Cdd:cd00063    1 PSPPTNLRvTDVTSTSVTLSWTPPEDDG---GPITG-YVVEYREKGSGDWKEVEVTPgSETSYTLTGLKPGTEYEFRVRA 76