C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536  28 QKVCFADVKHPCYKMAYFHELSSRVSFQEARLACESEGGVLLSLENEAEQKLIESMLQNLtkpgtGISDGDFWIGLLRSG 107
Cdd:cd03595    1 QRICRRGTEKPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTL-----RASDGDFWIGLRRSS 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568997536 108 DGQ-TSGACPDLYQWSDGSSSQFRNWYTDEPSCGSEKCVVMYHQPTANPGLGGPYLYQWNDDRCNMKHNYICKY 180
Cdd:cd03595   76 QYNvTSSACSSLYYWLDGSISTFRNWYVDEPSCGSEVCVVMYHQPSAPAGQGGPYLFQWNDDNCNMKNNFICKY 149

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536  28 QKVCFADVKHPCYKMAYFHELSSRVSFQEARLACESEGGVLLSLENEAEQKLIESMLQNLtkpgtGISDGDFWIGLLRSG 107
Cdd:cd03595    1 QRICRRGTEKPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTL-----RASDGDFWIGLRRSS 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568997536 108 DGQ-TSGACPDLYQWSDGSSSQFRNWYTDEPSCGSEKCVVMYHQPTANPGLGGPYLYQWNDDRCNMKHNYICKY 180
Cdd:cd03595   76 QYNvTSSACSSLYYWLDGSISTFRNWYVDEPSCGSEVCVVMYHQPSAPAGQGGPYLFQWNDDNCNMKNNFICKY 149

Lectin C-type domain; This family includes both long and short form C-type

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536   51 RVSFQEARLACESEGGVLLSLENEAEQKLIESMLQNltkpgtgiSDGDFWIGLLRSGDGQTsgacpdlYQWSDGSSSQFR 130
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKK--------SNKYFWIGLTDRKNEGT-------WKWVDGSPVNYT 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568997536  131 NWYTDEPSCG-SEKCVVMYHQPtanpglggpylYQWNDDRCNMKHNYICKY 180
Cdd:pfam00059  66 NWAPEPNNNGeNEDCVELSSSS-----------GKWNDENCNSKNPFVCEK 105

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536  28 QKVCFADVKHPCYKMAYFHELSSRVSFQEARLACESEGGVLLSLENEAEQKLIESMLQNLtkpgtGISDGDFWIGLLRSG 107
Cdd:cd03595    1 QRICRRGTEKPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTL-----RASDGDFWIGLRRSS 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568997536 108 DGQ-TSGACPDLYQWSDGSSSQFRNWYTDEPSCGSEKCVVMYHQPTANPGLGGPYLYQWNDDRCNMKHNYICKY 180
Cdd:cd03595   76 QYNvTSSACSSLYYWLDGSISTFRNWYVDEPSCGSEVCVVMYHQPSAPAGQGGPYLFQWNDDNCNMKNNFICKY 149

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536    39 CYKMAyfhelSSRVSFQEARLACESEGGVLLSLENEAEQKLIESMLQNLTKPGTgisdgdFWIGLLRSGDGQTsgacpdl 118
Cdd:smart00034  12 CYKFS-----TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDY------YWIGLSDPDSNGS------- 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568997536   119 YQWSDGSSS-QFRNWYTDEPSCGSEKCVVMYhqptANPGlggpylyQWNDDRCNMKHNYICK 179
Cdd:smart00034  74 WQWSDGSGPvSYSNWAPGEPNNSSGDCVVLS----TSGG-------KWNDVSCTSKLPFVCE 124

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536  39 CYKmaYFhelSSRVSFQEARLACE--SEGGV---LLSLENEAEQKLIESMLQNLTKPGTgisDGDFWIGLL-RSGDGQts 112
Cdd:cd03589   12 CYR--FF---GDRLTWEEAELRCRsfSIPGLiahLVSIHSQEENDFVYDLFESSRGPDT---PYGLWIGLHdRTSEGP-- 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568997536 113 gacpdlYQWSDGSSSQFRNWYTDEPS--CGSEKCVVMYHQPTAnpglggpyLYQWNDDRCNMKHNYICK 179
Cdd:cd03589   82 ------FEWTDGSPVDFTKWAGGQPDnyGGNEDCVQMWRRGDA--------GQSWNDMPCDAVFPYICK 136

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536  39 CYKmaYFhelSSRVSFQEARLACES--EGGVLLSLENEAEQKLIESMLQNLTKpgtgiSDGDFWIGLLRSGDGQTsgacp 116
Cdd:cd03594   12 CYG--YF---RQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQK-----AYQPVWIGLHDPQQSRG----- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568997536 117 dlYQWSDGSSSQFRNWYTDEPSCGSEKCVVMyHQPTAnpglggpYLyQWNDDRCNMKHNYICKY 180
Cdd:cd03594   77 --WEWSDGSKLDYRSWDRNPPYARGGYCAEL-SRSTG-------FL-KWNDANCEERNPFICKY 129

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536  51 RVSFQEARLACESEGGVLLSLENEAEQKLIESML-QNLTKPGTGISdgdfwigllrsgDGQTSGAcpdlYQWSDGSSSQF 129
Cdd:cd03591   10 EKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVkKGNTYAFIGIT------------DLETEGQ----FVYLDGGPLTY 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568997536 130 RNWYTDEPS--CGSEKCVVMYhqptaNPGlggpylyQWNDDRCNMKHNYICKY 180
Cdd:cd03591   74 TNWKPGEPNnaGGGEDCVEMY-----TSG-------KWNDVACNLTRLFVCEF 114

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536  49 SSRVSFQEARLACESEGGVLLSLENEAEQKLIESMLqnltkpgtgISDGDFWIGLlrsGDGQTSGAcpdlYQWSDGSSSQ 128
Cdd:cd03603    7 DGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNF---------GGYGASWIGA---SDAATEGT----WKWSDGEEST 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568997536 129 FRNWYTDEPSCGSEkcvvmyhQP--TANPGLGGPYLYQWND 167
Cdd:cd03603   71 YTNWGSGEPHNNGG-------GNedYAAINHFPGISGKWND 104

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536  50 SRVSFQEARLACESEGGVLLSLENEAEQKLiesmLQNLTKPgtgISDGDFWIGLLRSGDGQTsgacpdlyqW--SDGSSS 127
Cdd:cd03592    8 EKMTFNEAVKYCKSRGTDLVAIQNAEENAL----LNGFALK---YNLGYYWIDGNDINNEGT---------WvdTDKKEL 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568997536 128 QFRNWYTDEPSCG-SEKCVVMYHQPTANpglggpylyqWNDDRCNMKHNYIC 178
Cdd:cd03592   72 EYKNWAPGEPNNGrNENCLEIYIKDNGK----------WNDEPCSKKKSAIC 113

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        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536    33 ADVKHP-CYKMAYFHELSSR--------VSFQEARLACESEGGVLLSL-ENEAEQKLIESMLqnltkpgTGISDGDFWIG 102
Cdd:TIGR00864  311 AKASHPhCPKDGEIFEENGHcfqivpeeAAWLDAQEQCLARAGAALAIvDNDALQNFLARKV-------THSLDRGVWIG 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536   103 LlrsGDGQTSGACPdlYQWSDGSSSQ-FRNWYTDEPSCGS-EKCVVMyhQPTAnpglggpylyQWNDDRCNMKHNYICKY 180
Cdd:TIGR00864  384 F---SDVNGAEKGP--AHQGEAFEAEeCEEGLAGEPHPARaEHCVRL--DPRG----------QCNSDLCNAPHAYVCEL 446

                          170
                   ....*....|.
gi 568997536   181 EPEIhPTEPAE 191
Cdd:TIGR00864  447 NPGG-PVPDAE 456

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568997536  35 VKHPCYkmayfheLSSRV--SFQEARLACESEGGVLLSLENEAEQKLIESMLQNLTKPGTgisdgDFWIGLlrsGDGQTS 112
Cdd:cd03596    7 IHKKCY-------LVSEEtkHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGNW-----EVWLGI---NDMVAE 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568997536 113 GACPDLyqwsDGSSSQFRNW---YTDEPSCG-SEKCVVMyhqPTANPGlggpylyQWNDDRCNMKHNYICKY 180
Cdd:cd03596   72 GKWVDV----NGSPISYFNWereITAQPDGGkRENCVAL---SSSAQG-------KWFDEDCRREKPYVCEF 129