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 1039767652 411 KIREKKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd20969     3 AIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 82

                          90
                  ....*....|
gi 1039767652 491 NDTFTASLTV 500
Cdd:cd20969    83 NDSMPAHLHV 92

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039767652  327 NVSQNLLETLEENVFSSPRALEVLSINNNPLACDCRLLWLLQRQPNLQFGGQQP---MCAGPDTIRER 391
Cdd:TIGR00864    1 DISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVRQPeaaLCAGPGALAGQ 68

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 411 KIREKKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd20969     3 AIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 82

                          90
                  ....*....|
gi 1039767652 491 NDTFTASLTV 500
Cdd:cd20969    83 NDSMPAHLHV 92

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 410 PKIrEKKLQHLLVDEGQTVQLECNADGDPQPVISW------VTPRRRFITTKSNGRATvlgdgtLEIRFAQDQDSGMYVC 483
Cdd:pfam07679   1 PKF-TQKPKDVEVQEGESARFTCTVTGTPDPEVSWfkdgqpLRSSDRFKVTYEGGTYT------LTISNVQPDDSGKYTC 73

                          90
                  ....*....|....*..
gi 1039767652 484 IASNAAGNDTFTASLTV 500
Cdd:pfam07679  74 VATNSAGEAEASAELTV 90

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 176 LLSLEQLTLEKCNLTAVptEALSHLRSLIALHLKhlniNNmpvyafkRLFHLKNLEidywplldlmpANSlyglNLTSLS 255
Cdd:cd21340     1 LKRITHLYLNDKNITKI--DNLSLCKNLKVLYLY----DN-------KITKIENLE-----------FLT----NLTHLY 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 256 ITNTNLSTVPFLAfkHLVYLTHLNLSYNPISTIEAgmFSDLIRLQELHIVGAQLR-----TIEPHSFQGL-RFLRVLNVS 329
Cdd:cd21340    53 LQNNQIEKIENLE--NLVNLKKLYLGGNRISVVEG--LENLTNLEELHIENQRLPpgeklTFDPRSLAALsNSLRVLNIS 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039767652 330 QNLLETLEEnvFSSPRALEVLSINNNPLACDCRLLWLLQRQPNL 373
Cdd:cd21340   129 GNNIDSLEP--LAPLRNLEQLDASNNQISDLEELLDLLSSWPSL 170

type III secretion system effector E3 ubiquitin transferase SlrP;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652  39 KSVSCHRRRLLAIPEGIPIETKILDLSKNRLKSInPEEFISypLLEEIDLSDNIIANVePGAFNNlfNLRSLRLKGNRLK 118
Cdd:PRK15370  223 KTLYANSNQLTSIPATLPDTIQEMELSINRITEL-PERLPS--ALQSLDLFHNKISCL-PENLPE--ELRYLSVYDNSIR 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 119 LVPLGVFTGlsnLTKLDISENKIVILLDYMFQdlhNLKSLEVGDNDLVYISHrafSGLLSLEQLTLEKCNLTAVPtEALS 198
Cdd:PRK15370  297 TLPAHLPSG---ITHLNVQSNSLTALPETLPP---GLKTLEAGENALTSLPA---SLPPELQVLDVSKNQITVLP-ETLP 366

                         170
                  ....*....|....*....
gi 1039767652 199 hlRSLIALHLKHLNINNMP 217
Cdd:PRK15370  367 --PTITTLDVSRNALTNLP 383

Leucine rich repeat C-terminal domain;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039767652  355 NPLACDCRLLWLL--QRQPNLQFGGQQPMCAGPDTIRERSFKDFHSTalsfyFTCK 408
Cdd:smart00082   1 NPFICDCELRWLLrwLQANEHLQDPVDLRCASPSSLRGPLLELLHSE-----FKCP 51

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.

                          10        20        30
                  ....*....|....*....|....*....|
gi 1039767652  27 GCPARCECSAqnKSVSCHRRRLLAIPEGIP 56
Cdd:pfam01462   1 ACPVPCHCSA--TVVNCSDRGLTAVPRDLP 28

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. 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 Lingo-1 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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 411 KIREKKLQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd20969     3 AIRDRKAQQVFVDEGHTVQFVCRADGDPPPAILWLSPRKHLVSAKSNGRLTVFPDGTLEVRYAQVQDNGTYLCIAANAGG 82

                          90
                  ....*....|
gi 1039767652 491 NDTFTASLTV 500
Cdd:cd20969    83 NDSMPAHLHV 92

Leucine-rich repeat (LRR) protein [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652  48 LLAIPEGIPIETKILDLSKNRLKSINPEEFISYPLLEEIDLSDNIIANVEPGAFNNLFNLRSLRLKGNRLklvplgvFTG 127
Cdd:COG4886    39 LLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEE-------LSN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 128 LSNLTKLDISENKIViLLDYMFQDLHNLKSLEVGDNDLVYIShRAFSGLLSLEQLTLEKCNLTAVPtEALSHLRSLIALH 207
Cdd:COG4886   112 LTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELD 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 208 LKHLNINNMPvYAFKRLFHLKNLEIDYWPLLDLmpANSLYGL-NLTSLSITNTNLSTVPFLAfkHLVYLTHLNLSYNPIS 286
Cdd:COG4886   189 LSNNQITDLP-EPLGNLTNLEELDLSGNQLTDL--PEPLANLtNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQLT 263

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039767652 287 TIEAgmFSDLIRLQELHIVGAQLRTIEPHSFQGLRFLRVLNVSQNLLETLEENV 340
Cdd:COG4886   264 DLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLI 315

Immunoglobulin I-set domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 410 PKIrEKKLQHLLVDEGQTVQLECNADGDPQPVISW------VTPRRRFITTKSNGRATvlgdgtLEIRFAQDQDSGMYVC 483
Cdd:pfam07679   1 PKF-TQKPKDVEVQEGESARFTCTVTGTPDPEVSWfkdgqpLRSSDRFKVTYEGGTYT------LTISNVQPDDSGKYTC 73

                          90
                  ....*....|....*..
gi 1039767652 484 IASNAAGNDTFTASLTV 500
Cdd:pfam07679  74 VATNSAGEAEASAELTV 90

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039767652 409 KPKIREKKlQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASN 487
Cdd:pfam13927   1 KPVITVSP-SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. 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, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), 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, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 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. The fifth Ig-like domain of Robo 1 and 2 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 Ig 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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 418 QHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFITtkSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTAS 497
Cdd:cd20952     7 QNQTVAVGGTVVLNCQATGEPVPTISWLKDGVPLLG--KDERITTLENGSLQIKGAEKSDTGEYTCVALNLSGEATWSAV 84

                  ...
gi 1039767652 498 LTV 500
Cdd:cd20952    85 LDV 87

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 1039767652 428 VQLECNADGDPQPVISWVTPRRRFITTKSNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAG 63

Leucine-rich repeat (LRR) protein [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 134 LDISENKIVILLDYMFQDLHNLKSLEVGDNDLVYISHRAFSGLLSLEQLTLEKCNLTAVPTEALSHLRSLIALHLKHLNI 213
Cdd:COG4886     2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 214 NNMPVYAFKRLFHLKNLEidywpLLDLMPANSLYGL-NLTSLSITNTNLSTVPFlAFKHLVYLTHLNLSYNPISTIEAGm 292
Cdd:COG4886    82 LSLLLLGLTDLGDLTNLT-----ELDLSGNEELSNLtNLESLDLSGNQLTDLPE-ELANLTNLKELDLSNNQLTDLPEP- 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039767652 293 FSDLIRLQELHIVGAQLRTIePHSFQGLRFLRVLNVSQNLLETLEEnVFSSPRALEVLSINNNPL 357
Cdd:COG4886   155 LGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQL 217

Leucine-rich repeat (LRR) protein [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652  60 KILDLSKNRLKSInPEEFISYPLLEEIDLSDNIIANVePGAFNNLFNLRSLRLKGNRLKLVPlgVFTGLSNLTKLDISEN 139
Cdd:COG4886   185 KELDLSNNQITDL-PEPLGNLTNLEELDLSGNQLTDL-PEPLANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNN 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 140 KIVILLDymFQDLHNLKSLEVGDNDLVYISHRAFSGLLSLEQLTLEkcNLTAVPTEALSHLRSLIALHLKHLNINNMPVY 219
Cdd:COG4886   261 QLTDLPP--LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLL--LLLLNLLELLILLLLLTTLLLLLLLLKGLLVT 336

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039767652 220 AFKRLFHLKNLEIDYWPLLDLMPANSLYGLNLTSLSITNTNLSTVPFLAFKHLVYLTHLNLSYNPI 285
Cdd:COG4886   337 LTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 176 LLSLEQLTLEKCNLTAVptEALSHLRSLIALHLKhlniNNmpvyafkRLFHLKNLEidywplldlmpANSlyglNLTSLS 255
Cdd:cd21340     1 LKRITHLYLNDKNITKI--DNLSLCKNLKVLYLY----DN-------KITKIENLE-----------FLT----NLTHLY 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 256 ITNTNLSTVPFLAfkHLVYLTHLNLSYNPISTIEAgmFSDLIRLQELHIVGAQLR-----TIEPHSFQGL-RFLRVLNVS 329
Cdd:cd21340    53 LQNNQIEKIENLE--NLVNLKKLYLGGNRISVVEG--LENLTNLEELHIENQRLPpgeklTFDPRSLAALsNSLRVLNIS 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039767652 330 QNLLETLEEnvFSSPRALEVLSINNNPLACDCRLLWLLQRQPNL 373
Cdd:cd21340   129 GNNIDSLEP--LAPLRNLEQLDASNNQISDLEELLDLLSSWPSL 170

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 1039767652 425 GQTVQLECNADGDPQPVISWV-----TPRRRFITTKSNGratvlgdgTLEIRFAQDQDSGMYVCIASNAAGNDTFTASLT 499
Cdd:cd05731    10 GGVLLLECIAEGLPTPDIRWIklggeLPKGRTKFENFNK--------TLKIENVSEADSGEYQCTASNTMGSARHTISVT 81

                  ..
gi 1039767652 500 VK 501
Cdd:cd05731    82 VE 83

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 1039767652 425 GQTVQLECNADGDPQPVISW------VTPRRRFITTKSNGRatvlgdGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd05743     1 GETVEFTCVATGVPTPIINWrlnwghVPDSARVSITSEGGY------GTLTIRDVKESDQGAYTCEAINTRG 66

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 424 EGQTVQLECNADGDPQPVISWvtprrrfitTKSNG------RATVLGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFTAS 497
Cdd:cd05745     1 EGQTVDFLCEAQGYPQPVIAW---------TKGGSqlsvdrRHLVLSSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQ 71

                  ...
gi 1039767652 498 LTV 500
Cdd:cd05745    72 LTV 74

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 409 KPKIR--EKKLQHLLVDEgqtVQLECNADGDPQPVISWVTPRRRFITTKS--NGRATVLGD---GTLEIRFAQDQDSGMY 481
Cdd:cd05869     2 KPKITyvENQTAMELEEQ---ITLTCEASGDPIPSITWRTSTRNISSEEKtlDGHIVVRSHarvSSLTLKYIQYTDAGEY 78

                          90
                  ....*....|....*....
gi 1039767652 482 VCIASNAAGNDTFTASLTV 500
Cdd:cd05869    79 LCTASNTIGQDSQSMYLEV 97

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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 417 LQHLLVDEGQTVQLECNADGDPQPVISWVTPRRRFitTKSNGRATV-LGDGTLEIRFAQDQDSGMYVCIASNAAGNDTFT 495
Cdd:cd20976     8 PKDLEAVEGQDFVAQCSARGKPVPRITWIRNAQPL--QYAADRSTCeAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCS 85

                  ....*
gi 1039767652 496 ASLTV 500
Cdd:cd20976    86 AWVTV 90

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the 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 (Slit-1,Slit-2, Slit-3), 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 Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 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 Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039767652 425 GQTVQLECNAD-GDPQPVISWvtpRRRFITTK-SNGRATVLGDGTLEIRFAQDQDSGMYVCIASNAAG-NDTFTASLTV 500
Cdd:cd05724    12 GEMAVLECSPPrGHPEPTVSW---RKDGQPLNlDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGeRESRAARLSV 87

Third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein), and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin-like domain of the human WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein) and similar proteins. WFIKKN is a secreted protein that consists of multiple types of protease inhibitory modules, including two tandem Kunitz-type protease inhibitor-domains. The Ig superfamily is a heterogenous group of proteins built on a common fold comprised of a sandwich of two beta sheets. Members of the Ig superfamily are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as 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. 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.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039767652 419 HLLVDEGQTVQLECNADGDPQPVISW---VTPRRRFITTKSNGRATVL--GDGTLEIRFAQDQDSGMYVCIASNAAG 490
Cdd:cd05765     9 HQTVKVGETASFHCDVTGRPQPEITWekqVPGKENLIMRPNHVRGNVVvtNIGQLVIYNAQPQDAGLYTCTARNSGG 85

Leucine rich repeat;

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                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039767652 298 RLQELHIVGAQLRTIEPHSFQGLRFLRVLNVSQNLLETLEENVFSSPRALEVLSINNNPL 357
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61