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 226958426  38 QLVCRGGTRRPCYKVIYFHDAFQRLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIENLLASDGDFWIGLKRLEEKQSN 117
Cdd:cd03595    1 QRICRRGTEKPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIGLRRSSQYNVT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226958426 118 NTACQDLYAWTDGSTSQFRNWYVDEPSCGSEVCVVMYHQPSAPPGIGGSYMFQWNDDRCNMKNNFICKY 186
Cdd:cd03595   81 SSACSSLYYWLDGSISTFRNWYVDEPSCGSEVCVVMYHQPSAPAGQGGPYLFQWNDDNCNMKNNFICKY 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 226958426  38 QLVCRGGTRRPCYKVIYFHDAFQRLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIENLLASDGDFWIGLKRLEEKQSN 117
Cdd:cd03595    1 QRICRRGTEKPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIGLRRSSQYNVT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226958426 118 NTACQDLYAWTDGSTSQFRNWYVDEPSCGSEVCVVMYHQPSAPPGIGGSYMFQWNDDRCNMKNNFICKY 186
Cdd:cd03595   81 SSACSSLYYWLDGSISTFRNWYVDEPSCGSEVCVVMYHQPSAPAGQGGPYLFQWNDDNCNMKNNFICKY 149

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958426   61 RLNFEEAKETCMEDGGQLVSIETEDEQrlieKFIENLLASDG-DFWIGLKRlEEKQSNNTacqdlyaWTDGSTSQFRNWY 139
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEEL----DFLSSTLKKSNkYFWIGLTD-RKNEGTWK-------WVDGSPVNYTNWA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 226958426  140 VDEPSCG-SEVCVVMYHQPSappgiggsymfQWNDDRCNMKNNFICKY 186
Cdd:pfam00059  69 PEPNNNGeNEDCVELSSSSG-----------KWNDENCNSKNPFVCEK 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 226958426  38 QLVCRGGTRRPCYKVIYFHDAFQRLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIENLLASDGDFWIGLKRLEEKQSN 117
Cdd:cd03595    1 QRICRRGTEKPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIGLRRSSQYNVT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226958426 118 NTACQDLYAWTDGSTSQFRNWYVDEPSCGSEVCVVMYHQPSAPPGIGGSYMFQWNDDRCNMKNNFICKY 186
Cdd:cd03595   81 SSACSSLYYWLDGSISTFRNWYVDEPSCGSEVCVVMYHQPSAPAGQGGPYLFQWNDDNCNMKNNFICKY 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 226958426    49 CYKviyFHDafQRLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIENLLASDgDFWIGLKRLeekqSNNTACQdlyaWT 128
Cdd:smart00034  12 CYK---FST--EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDP----DSNGSWQ----WS 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 226958426   129 DGS-TSQFRNWYVDEPSCGSEVCVVMYHqpsappgiggsYMFQWNDDRCNMKNNFICK 185
Cdd:smart00034  78 DGSgPVSYSNWAPGEPNNSSGDCVVLST-----------SGGKWNDVSCTSKLPFVCE 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 226958426  54 YFHDAfQRLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIEnllaSDGDFWIGLKrleEKQSNNTacqdlYAWTDGS-- 131
Cdd:cd03590   13 YFFST-EKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS----GNRSYWIGLS---DEETEGE-----WKWVDGTpl 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226958426 132 TSQFRNWYVDEPS---CGSEVCVVMYHqpsappgiggsYMFQWNDDRCNMKNNFICK 185
Cdd:cd03590   80 NSSKTFWHPGEPNnwgGGGEDCAELVY-----------DSGGWNDVPCNLEYRWICE 125

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958426  49 CYKViyfHdaFQRLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIENLL----ASDGDFWIGLKRleekqsNNTACQDL 124
Cdd:cd03600    6 CYTL---H--PQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPgrhgRGSLRLWIGLQR------EPRQCSDP 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226958426 125 ------YAW-TDGSTSQFRNWyVDEP--SCGSEVCVVMYHQPSAPPGiggsymFQWNDDRCNMK-NNFICKYH 187
Cdd:cd03600   75 slplrgFSWvTGDQDTDFSNW-LQEPagTCTSPRCVALSAAGSTPDN------LKWKDGPCSARaDGYLCKFS 140

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 226958426  54 YFHDAFQRLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIENLLASdgdFWIGLKRLE-EKQsnntacqdlYAWTDGST 132
Cdd:cd03591    3 IFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTY---AFIGITDLEtEGQ---------FVYLDGGP 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226958426 133 SQFRNWYVDEPS--CGSEVCVVMYHqpsappgiGGsymfQWNDDRCNMKNNFICKY 186
Cdd:cd03591   71 LTYTNWKPGEPNnaGGGEDCVEMYT--------SG----KWNDVACNLTRLFVCEF 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 226958426  49 CYkviYFHDafQRLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIENLlasdgDFWIGLKRLEEKQSnntacqdlYAWT 128
Cdd:cd03593   12 CY---YFSM--EKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS-----SYWIGLSREKSEKP--------WKWI 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226958426 129 DGSTsqFRNWYVDEPSCGSEVCVVMYHqpsapPGIggsymfqwNDDRCNMKNNFICK 185
Cdd:cd03593   74 DGSP--LNNLFNIRGSTKSGNCAYLSS-----TGI--------YSEDCSTKKRWICE 115

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 226958426  61 RLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIENLlaSDGDFWIGLkrleekqsNNTACQDLYAWTDGSTSQFRNWYV 140
Cdd:cd03592    9 KMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKY--NLGYYWIDG--------NDINNEGTWVDTDKKELEYKNWAP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 226958426 141 DEPSCG-SEVCVVMYHQPSAppgiggsymfQWNDDRCNMKNNFIC 184
Cdd:cd03592   79 GEPNNGrNENCLEIYIKDNG----------KWNDEPCSKKKSAIC 113

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 226958426  41 CRGGTR--RPCYKViyfhdAFQRLNFEEAKETCMEDGGQLVSIETEDEQRLIEKFIENLLASDGDFWIGLkrleekqsNN 118
Cdd:cd03596    1 CLKGTKihKKCYLV-----SEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGNWEVWLGI--------ND 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226958426 119 TACQDLYAWTDGSTSQFRNW---YVDEPSCG-SEVCVVMyhqpsappgiGGSYMFQWNDDRCNMKNNFICKY 186
Cdd:cd03596   68 MVAEGKWVDVNGSPISYFNWereITAQPDGGkRENCVAL----------SSSAQGKWFDEDCRREKPYVCEF 129

TMEM154 protein family; The function of this family of transmembrane proteins has not, as yet, been determined. However, it is thought to be a therapeutic target for ovine lentivirus infection. This family of proteins is found in eukaryotes and members are typically between 138 and 320 amino acids in length.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958426  199 PGGEATEPATPLLPEETQKEDTKETfkERREAALNLAYILIPSIPLFLLLVVTSAVCWV-WICRRKREQTDPSTKEQHTi 277
Cdd:pfam15102  28 TATFAAVTTTESFNQTTANANLSST--DFDNDSNQLEFILMIIIPLVLLIILLLSVAILiTYYRRKRRKDDPTSEGSQD- 104

                          90       100
                  ....*....|....*....|....*...
gi 226958426  278 wptprQENSPNLDVYNVIRKQSEADLAE 305
Cdd:pfam15102 105 -----ALQTYDLDSENLKVPIFEEDTPS 127