PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825  743 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 822
Cdd:cd01752    1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 31559825  823 YVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVF 859
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117

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 31559825   33 NCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGK--KWWIGQNVMPLKKH---QDNKYPADVAANGPP 107
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTwkwSDGSPLVDYTNWAPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 31559825  108 KPLS-----CTYLSRNfirisSKG----DKCLLKYYFICQ 138
Cdd:cd00037   81 EPNPggsedCVVLSSS-----SDGkwndVSCSSKLPFICE 115

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825  743 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 822
Cdd:cd01752    1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 31559825  823 YVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVF 859
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117

PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825    745 YLIQVYTGYRRSAATTAKVVITLYGSEGRS--EPHHLCDPQktvFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 822
Cdd:pfam01477    1 YQVKVVTGDELGAGTDADVYISLYGKVGESaqLEITLDNPD---FERGAEDSFEIDTDWDVGAILKINLHWDNNGLSDEW 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 31559825    823 YVSQVIVC-DMAVKRKWHFLCNCWLAVDLgDCELDRVF 859
Cdd:pfam01477   78 FLKSITVEvPGETGGKYTFPCNSWVYGSK-KYKETRVF 114

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 31559825   33 NCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGK--KWWIGQNVMPLKKH---QDNKYPADVAANGPP 107
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTwkwSDGSPLVDYTNWAPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 31559825  108 KPLS-----CTYLSRNfirisSKG----DKCLLKYYFICQ 138
Cdd:cd00037   81 EPNPggsedCVVLSSS-----SDGkwndVSCSSKLPFICE 115

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 31559825    634 QCYYWEIHNQT---WSSAGCQVGpQSTILRTQCLCNHLTFFA 672
Cdd:pfam01825    2 QCVFWDFTNSTtgrWSTEGCTTV-SLNDTHTVCSCNHLTSFA 42

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 31559825      31 QNNCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGKK---WWIGQNVMPLKKH---QDNKYPAD---V 101
Cdd:smart00034    9 GGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyYWIGLSDPDSNGSwqwSDGSGPVSysnW 88

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 31559825     102 AANGPPKPL-SCTYLSRNFIRISSKGdkCLLKYYFICQ 138
Cdd:smart00034   89 APGEPNNSSgDCVVLSTSGGKWNDVS--CTSKLPFVCE 124

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825     43 SFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEE-GKKWWIGQNVMPLKKhqDNKYP----------ADVAANGPPKPlS 111
Cdd:pfam00059    3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsNKYFWIGLTDRKNEG--TWKWVdgspvnytnwAPEPNNNGENE-D 79

                           90       100
                   ....*....|....*....|....*...
gi 31559825    112 CTYLSRNFIRISSKGdkCLLKYYFICQT 139
Cdd:pfam00059   80 CVELSSSSGKWNDEN--CNSKNPFVCEK 105

PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825  743 FHYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHHLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSW 822
Cdd:cd01752    1 YLYLVTVFTGWRRGAGTTAKVTITLYGAEGESEPHHLRDPEKPIFERGSVDSFLLTTPFPLGELQSIRLWHDNSGLSPSW 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 31559825  823 YVSQVIVCDMAVKRKWHFLCNCWLAVDLGDCELDRVF 859
Cdd:cd01752   81 YLSRVIVRDLQTGKKWFFLCNDWLSVEEGDGTVERTF 117

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825   1467 IISQVIYYLLVCYYAFIQGCQLKQQKWRFFTGKRNILDTSIILISFILLGLDMKSISLHKKNMARYRDDQDRFISFYEAV 1546
Cdd:pfam08016   11 LLCEIVFVVFFLYFVVEEILKIRKHRPSYLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLIKSVEASPVTFIDFDRVA 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825   1547 KVNSAATHLVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSS 1626
Cdd:pfam08016   91 QLDNLYRIILAFLVFLTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQAPNFSNFVKS 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 31559825   1627 AVTVVGLLMGISHQEEVFALDPVLGTFLILTSVILMVLVVINLFVSAILMAF 1678
Cdd:pfam08016  171 ILTLFRTILGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222

PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825  744 HYLIQVYTGYRRSAATTAKVVITLYGSEGRSEPHhLCDPQKTVFERGGLDVFLLTTWTSLGNLHSLRLWHDNSGVSPSWY 823
Cdd:cd00113    2 RYTVTIKTGDKKGAGTDSNISLALYGENGNSSDI-PILDGPGSFERGSTDTFQIDLKLDIGDITKVYLRRDGSGLSDGWY 80

                         90       100
                 ....*....|....*....|...
gi 31559825  824 VSQVIVCDMAVKRKWHFLCNCWL 846
Cdd:cd00113   81 CESITVQALGTKKVYTFPVNRWV 103

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 31559825   33 NCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGK--KWWIGQNVMPLKKH---QDNKYPADVAANGPP 107
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssDVWIGLNDLSSEGTwkwSDGSPLVDYTNWAPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 31559825  108 KPLS-----CTYLSRNfirisSKG----DKCLLKYYFICQ 138
Cdd:cd00037   81 EPNPggsedCVVLSSS-----SDGkwndVSCSSKLPFICE 115

GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 31559825    634 QCYYWEIHNQT---WSSAGCQVGpQSTILRTQCLCNHLTFFA 672
Cdd:pfam01825    2 QCVFWDFTNSTtgrWSTEGCTTV-SLNDTHTVCSCNHLTSFA 42

Polycystin cation channel protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825  1555 LVGFPVLLATVQLWNLLRHSPRLRVISRTLSRAWDEVVGFLLIILILLTGYAIAFNLLFGCSISDYRTFFSSAVTVVGLL 1634
Cdd:PLN03223 1294 LSGINIILLLGRILKLMDFQPRLGVITRTLWLAGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENL 1373

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31559825  1635 MG-ISHQEEVF----ALDPVLGTFLILTSVILMVLVVINLFVSAILMAFGkERKSLKKEAALIDTllqKLSNLLGISW 1707
Cdd:PLN03223 1374 LGdITYFNEDLknltGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAFG-EVKANAAETVSVHT---ELFPMLRDKW 1447

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 31559825      31 QNNCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEEGKK---WWIGQNVMPLKKH---QDNKYPAD---V 101
Cdd:smart00034    9 GGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdyYWIGLSDPDSNGSwqwSDGSGPVSysnW 88

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 31559825     102 AANGPPKPL-SCTYLSRNFIRISSKGdkCLLKYYFICQ 138
Cdd:smart00034   89 APGEPNNSSgDCVVLSTSGGKWNDVS--CTSKLPFVCE 124

C-type lectin-like protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825    11 LYIRTSIILGSELNSPAPHGQ--NNCYQLNRFQCSFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLeEGKKWWIGqnvMP 88
Cdd:PHA03097   32 LSCKLSPGDRSGLNCRSGWVGynNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYK-GGQDLWIG---IE 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 31559825    89 LKKHQDNKYPADVAANGPPKPLSCTYLSRNFIrISSkgdKCLLKYYFIC 137
Cdd:PHA03097  108 KKKGDDDDREVLDKVVKPPKSGKCAYLKDKTI-ISS---NCNATKGWIC 152

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31559825     43 SFEEAQHYCHVQRGFLAHIWNKEVQDLIRDYLEE-GKKWWIGQNVMPLKKhqDNKYP----------ADVAANGPPKPlS 111
Cdd:pfam00059    3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsNKYFWIGLTDRKNEG--TWKWVdgspvnytnwAPEPNNNGENE-D 79

                           90       100
                   ....*....|....*....|....*...
gi 31559825    112 CTYLSRNFIRISSKGdkCLLKYYFICQT 139
Cdd:pfam00059   80 CVELSSSSGKWNDEN--CNSKNPFVCEK 105