C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291706 107 CPKDWKPFGSYCYFTSTDLvASWNESKENCFHMGAHLVVIHSQEEQDFITGILDTGTAYFIGLSNP-GDQQWQWIDQTPY 185
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEK-KSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEeTEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 54291706 186 DDNTTFWHKGEPSS---DNEQCVIINHRQstgWGWSDIPCSDKQNSIC 230
Cdd:cd03590  80 NSSKTFWHPGEPNNwggGGEDCAELVYDS---GGWNDVPCNLEYRWIC 124

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291706 107 CPKDWKPFGSYCYFTSTDLvASWNESKENCFHMGAHLVVIHSQEEQDFITGILDTGTAYFIGLSNP-GDQQWQWIDQTPY 185
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEK-KSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEeTEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 54291706 186 DDNTTFWHKGEPSS---DNEQCVIINHRQstgWGWSDIPCSDKQNSIC 230
Cdd:cd03590  80 NSSKTFWHPGEPNNwggGGEDCAELVYDS---GGWNDVPCNLEYRWIC 124

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291706   128 SWNESKENCFHMGAHLVVIHSQEEQDFITGIL-DTGTAYFIGLS-NPGDQQWQWIDQTPYddNTTFWHKGE-PSSDNEQC 204
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLkKSNKYFWIGLTdRKNEGTWKWVDGSPV--NYTNWAPEPnNNGENEDC 80

                          90       100
                  ....*....|....*....|....*..
gi 54291706   205 VIINhrqSTGWGWSDIPCSDKQNSICH 231
Cdd:pfam00059  81 VELS---SSSGKWNDENCNSKNPFVCE 104

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291706 107 CPKDWKPFGSYCYFTSTDLvASWNESKENCFHMGAHLVVIHSQEEQDFITGILDTGTAYFIGLSNP-GDQQWQWIDQTPY 185
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEK-KSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEeTEGEWKWVDGTPL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 54291706 186 DDNTTFWHKGEPSS---DNEQCVIINHRQstgWGWSDIPCSDKQNSIC 230
Cdd:cd03590  80 NSSKTFWHPGEPNNwggGGEDCAELVYDS---GGWNDVPCNLEYRWIC 124

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 54291706 117 YCYFTSTDLVaSWNESKENCFHMGAHLVVIHSQEEQDFITGILDTG--TAYFIGLS-NPGDQQWQWIDQTPYDDNtTFWH 193
Cdd:cd00037   1 SCYKFSTEKL-TWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSssSDVWIGLNdLSSEGTWKWSDGSPLVDY-TNWA 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 54291706 194 KGEPSSD-NEQCVIINHrqSTGWGWSDIPCSDKQNSIC 230
Cdd:cd00037  79 PGEPNPGgSEDCVVLSS--SSDGKWNDVSCSSKLPFIC 114

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291706 107 CPKDWKPFGSYCYFTSTDlVASWNESKENCFHMGAHLVVIHSQEEQDFITGILDTGTaYFIGLS-NPGDQQWQWIDQTPY 185
Cdd:cd03593   1 CPKDWICYGNKCYYFSME-KKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS-YWIGLSrEKSEKPWKWIDGSPL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 54291706 186 DDNTTFwhkgEPSSDNEQCVIINHrqstgWGWSDIPCSDKQNSIC 230
Cdd:cd03593  79 NNLFNI----RGSTKSGNCAYLSS-----TGIYSEDCSTKKRWIC 114

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291706   128 SWNESKENCFHMGAHLVVIHSQEEQDFITGIL-DTGTAYFIGLS-NPGDQQWQWIDQTPYddNTTFWHKGE-PSSDNEQC 204
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLkKSNKYFWIGLTdRKNEGTWKWVDGSPV--NYTNWAPEPnNNGENEDC 80

                          90       100
                  ....*....|....*....|....*..
gi 54291706   205 VIINhrqSTGWGWSDIPCSDKQNSICH 231
Cdd:pfam00059  81 VELS---SSSGKWNDENCNSKNPFVCE 104

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 54291706 112 KPFGSYCYFTSTDLVASWNESKENCFHMGAHLVVIHSQEEQ----DFITGILDTGTAYFIGL-------SNPGD--QQWQ 178
Cdd:cd03595  10 KPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQklieRFIQTLRASDGDFWIGLrrssqynVTSSAcsSLYY 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54291706 179 WIDQTPyddnTTF--WHKGEPSSDNEQCVIINHRQSTGWG--------WSDIPCSDKQNSIC 230
Cdd:cd03595  90 WLDGSI----STFrnWYVDEPSCGSEVCVVMYHQPSAPAGqggpylfqWNDDNCNMKNNFIC 147

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 54291706 119 YFTSTDLVASWNESKENCFHMGAHLVVIHSQEEQDFITGILDTGTAY-FIGLSN---PGdqQWQWIDQTPYddNTTFWHK 194
Cdd:cd03591   3 IFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYaFIGITDletEG--QFVYLDGGPL--TYTNWKP 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 54291706 195 GEPS--SDNEQCVIInhrQSTGwGWSDIPCSDKQNSIC 230
Cdd:cd03591  79 GEPNnaGGGEDCVEM---YTSG-KWNDVACNLTRLFVC 112

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291706  107 CPKDWKPFGSYCYFTSTDlVASWNESKENCFHMGAHLVVIHSQEEQDFITGILDTgTAYFIGLS-NPGDQQWQWIDQTPY 185
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSED-SKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDS-SDHWIGLNrESSNHPWKWADNSNY 165

                         90
                 ....*....|....*..
gi 54291706  186 DDNTTFWHKGEPSSDNE 202
Cdd:PHA02642 166 NASFVITGTGECAYLND 182

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54291706 107 CPKDWKPFGSYC--YFTSTDlvaSWNESKENCFHMGAHLVVIHSQEEQDFITGILDTGTAY------FIGLSNPGDQQWQ 178
Cdd:cd03597   1 CGEGWHLVGNSClkINTARE---SYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTkqkltpWVGLRKINVSYWC 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 54291706 179 WIDQTPYDDNTTFWHKGEPsSDNEQCVIINHRQSTGWGWSdiPCSDKQN-SIC 230
Cdd:cd03597  78 WEDMSPFTNTTLQWLPGEP-SDAGFCGYLEEPAVSGLKAN--PCTNPVNgSVC 127