First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667  29 RFRGRHYKREFRLEGEPVALRCPQVPYWLwaSVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVC 108
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL--AQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYC 78

                         90
                 ....*....|....*...
gi 767919667 109 TTRNASYCDKMSIELRVF 126
Cdd:cd05756   79 VVRNSTYCSKVSISLEVV 96

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667  29 RFRGRHYKREFRLEGEPVALRCPQVPYWLwaSVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVC 108
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL--AQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYC 78

                         90
                 ....*....|....*...
gi 767919667 109 TTRNASYCDKMSIELRVF 126
Cdd:cd05756   79 VVRNSTYCSKVSISLEVV 96

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667  241 SPLKTISASLGSRLTIPCKVFlgTGTPLTTMLWWTANDTHIESAypggRVTEGPRQEYSENnenyievpLIFDPVTREDL 320
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIESL----KVKHDNGRTTQSS--------LLISNVTKEDA 66

                          90       100
                  ....*....|....*....|.
gi 767919667  321 HmDFKCVVHNTLSFQTLRTTV 341
Cdd:pfam00047  67 G-TYTCVVNNPGGSATLSTSL 86

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919667   41 LEGEPVALRCpqvpywlWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 112
Cdd:pfam13927  14 REGETVTLTC-------EATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767919667  166 KIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCV 208
Cdd:pfam13927  32 TITWYKNgEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667  29 RFRGRHYKREFRLEGEPVALRCPQVPYWLwaSVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVC 108
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL--AQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYC 78

                         90
                 ....*....|....*...
gi 767919667 109 TTRNASYCDKMSIELRVF 126
Cdd:cd05756   79 VVRNSTYCSKVSISLEVV 96

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667 136 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNeKFLSVRgtTHLLVHDVALEDAGYYRCVLTFAHEG 215
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDK-RFIPKG--SKLLIQNVTEEDAGNYTCKFTYTHNG 77

                         90
                 ....*....|....
gi 767919667 216 QQYNITRSIELRIK 229
Cdd:cd05757   78 KQYNVTRTISLTVT 91

IL-1 receptor-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667  27 SCRFRGRHYKREFRLEGEPVALRCPQVPY----WLWASVSPRINLTWHKNDS--------ART-----VPGEEETRmwaq 89
Cdd:PHA02826  21 YCKYRGGDLTPVYAKFGDPMVLLCTGKHYkksiFFDKTFITSYNVTWSKTDSlafvrdsgARTkikkiTHNEIGDR---- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667  90 DGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFlPFISypqiltlSTSGVLVCPDLSEFTRDKTDVKIQW 169
Cdd:PHA02826  97 SENLWIGNVINIDEGIYICTISSGNICEESTIRLTFDSGTINY-QFNS-------GKDSKLHCYGTDGISSTFKDYTLTW 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767919667 170 YKDSLLLDKDnEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRI 228
Cdd:PHA02826 169 YKNGNIVLYT-DRIQLRNNNSTLVIKSATHDDSGIYTCNLRFNKNSNNYNITKEYKVTI 226

First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. IL1RAPL is encoded by a gene on the X-chromosome, this gene is wholly or partially deleted in multiple cases of non-syndromic intellectual disability. This group also contains IL1RAPL-2 which is also encoded by a gene on the X-chromosome and is a candidate for another non-syndromic intellectual disability loci.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667  35 YKREFRLEGEPVALRCPQVPYWLWASV----SPRINLTWHKNDSARTVpgEE-----ETRMWAQDGALWLLPALQEDSGT 105
Cdd:cd05896    7 LKKYMVLAGEPVRIKCALFYGYIRTNYsmaqSAGLSLMWYKSSGPGDF--EEpiifdGVRMSKEEDSIWFRPAELQDSGL 84

                         90       100
                 ....*....|....*....|
gi 767919667 106 YVCTTRNASYCDKMSIELRV 125
Cdd:cd05896   85 YTCVLRNSTYCMKVSMSLTV 104

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667  41 LEGEPVALRCPQVPYWL---WASV-SPRINLTWHKNDSARTVpgEE-------ETRMWAQDGALWLLPALQEDSGTYVCT 109
Cdd:cd20992   14 FEGEPARIKCPLFEHFLkynYSTAhSAGLTLIWYWTRQDRDL--EEpinfrlpDNRISKEKDVLWFRPTLLNDTGNYTCM 91

                         90
                 ....*....|....*.
gi 767919667 110 TRNASYCDKMSIELRV 125
Cdd:cd20992   92 LRNTTYCSKVAFPLEV 107

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 767919667  29 RFRGRHYKREFRLEGEPVALRC------PQVPYWLWASVSPrinLTWHKNDSARTVPgeeetrmwaqDGALWLLPALQED 102
Cdd:cd20969    3 AIRDRKAQQVFVDEGHTVQFVCradgdpPPAILWLSPRKHL---VSAKSNGRLTVFP----------DGTLEVRYAQVQD 69

                         90       100
                 ....*....|....*....|...
gi 767919667 103 SGTYVCTTRNASYCDKMSIELRV 125
Cdd:cd20969   70 NGTYLCIAANAGGNDSMPAHLHV 92

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919667 149 VLVCPdlsefTRDKTDVKIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQ 217
Cdd:cd00096    2 TLTCS-----ASGNPPPTITWYKNgKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66

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 767919667  46 VALRCPqvpywlwASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 112
Cdd:cd00096    1 VTLTCS-------ASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASN 60

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767919667  40 RLEGEPVALRCPqvpywlwASVSPRINLTWHKNdsARTVPGEEETRMWaQDGALWLLPALQEDSGTYVCTTRN 112
Cdd:cd20978   13 VKGGQDVTLPCQ-------VTGVPQPKITWLHN--GKPLQGPMERATV-EDGTLTIINVQPEDTGYYGCVATN 75

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 767919667  41 LEGEPVALRCPqvpywlwASVSPRINLTWHKNDSARTVPGEEETrMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMS 120
Cdd:cd20976   14 VEGQDFVAQCS-------ARGKPVPRITWIRNAQPLQYAADRST-CEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCS 85

                 ....*
gi 767919667 121 IELRV 125
Cdd:cd20976   86 AWVTV 90

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767919667   42 EGEPVALRCPqvpywlwASVSPRINLTWHKNDSArtvpgeeetrmWAQDGALWLLPALQEDSGTYVCTTRNASYC 116
Cdd:pfam13895  13 EGEPVTLTCS-------APGNPPPSYTWYKDGSA-----------ISSSPNFFTLSVSAEDSGTYTCVARNGRGG 69

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767919667  166 KIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCV 208
Cdd:pfam13927  32 TITWYKNgEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75

hypothetical protein; Provisional

                         10        20        30
                 ....*....|....*....|....*....|.
gi 767919667  95 LLPALQEDSGTYVCTTRNASYCDKMSIELRV 125
Cdd:PHA02633  22 ILNPTQSDSGIYMCITKNETYSDMMKFDLCI 52