lipocalin/cytosolic fatty acid-binding protein family; Lipocalins are diverse, mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules as well as membrane bound-receptors. They have a large beta-barrel ligand-binding cavity. Members include retinol-binding protein, retinoic acid-binding protein, complement protein C8 gamma, Can f 2, apolipoprotein D, extracellular fatty acid-binding protein, beta-lactoglobulin, oderant-binding protein, and bacterial lipocalin Blc. Lipocalins are involved in many important processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty acid-binding proteins also bind hydrophobic ligands in a non-covalent, reversible manner, and are involved in protection and shuttling of fatty acids within the cell, and in acquisition and removal of fatty acids from intracellular sites.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  11 GVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGDKPTTI 90
Cdd:cd19852  23 GVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEETLDGRKVKSIITFDGNKLVQEQKGDHPTII 102

                        90       100
                ....*....|....*....|....*.
gi 78706756  91 VREFTDNELITTLTIGNVKCVRVYKA 116
Cdd:cd19852 103 IREFSKEEMKAVLTAGDVVCTRVYKA 128

fatty acid-binding protein similar to Locusta migratoria FABP (Lm-FABP); This subfamily includes fatty acid-binding protein found mainly in insects such as the migratory locust (Locusta migratoria) FABP (Lm-FABP) and the desert locust (Schistocerca gregaria) FABP (Sg-FABP), having flight muscle tissues that contain unusually high levels FABP, similar to migratory birds. Both Sg- and Lm-FABP are closely related to the mammalian i-LBP subfamily IV, especially to the heart and adipocyte FABP forms. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  11 GVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGDKPTTI 90
Cdd:cd19852  23 GVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEETLDGRKVKSIITFDGNKLVQEQKGDHPTII 102

                        90       100
                ....*....|....*....|....*.
gi 78706756  91 VREFTDNELITTLTIGNVKCVRVYKA 116
Cdd:cd19852 103 IREFSKEEMKAVLTAGDVVCTRVYKA 128

fatty acid-binding protein similar to Locusta migratoria FABP (Lm-FABP); This subfamily includes fatty acid-binding protein found mainly in insects such as the migratory locust (Locusta migratoria) FABP (Lm-FABP) and the desert locust (Schistocerca gregaria) FABP (Sg-FABP), having flight muscle tissues that contain unusually high levels FABP, similar to migratory birds. Both Sg- and Lm-FABP are closely related to the mammalian i-LBP subfamily IV, especially to the heart and adipocyte FABP forms. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  11 GVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGDKPTTI 90
Cdd:cd19852  23 GVGLITRKAGNALTPVVELELEDGTYTLTTSTTFKTTEFKFKLGEEFDEETLDGRKVKSIITFDGNKLVQEQKGDHPTII 102

                        90       100
                ....*....|....*....|....*.
gi 78706756  91 VREFTDNELITTLTIGNVKCVRVYKA 116
Cdd:cd19852 103 IREFSKEEMKAVLTAGDVVCTRVYKA 128

fatty acid-binding protein 3 and similar proteins including FABP4, -5, -7, -8, -9, -11, and -12; This FABP3-like subfamily includes FABP3, -4, -5, -7, -8, -9, -11, -12, and similar proteins and belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756   9 SFGVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGD-KP 87
Cdd:cd19443  20 ALGVGFATRKLGNLAKPTVIISVDGDKITIKTESTFKNTEISFKLGEEFDETTADGRKTKSTVTLDNGKLVQVQKWDgKE 99

                        90       100
                ....*....|....*....|....*...
gi 78706756  88 TTIVREFTDNELITTLTIGNVKCVRVYK 115
Cdd:cd19443 100 TTIVRELKDGKLVVTCTMGDVVCTRTYE 127

Fatty acid binding protein 7; FABP7 (also known as brain FABP, B-FABP, BLBP, brain lipid binding protein) is highly expressed in glial cells through development of the nervous system. In the developing brain, FABP7 is required for the establishment of the radial glial fiber system, which is involved in the migration of immature neurons. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756   9 SFGVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGD-KP 87
Cdd:cd19470  22 ALGVGFATRQVGNVTKPTVIISQEGDKVVIRTLSTFKNTEISFKLGEEFDETTADDRNCKSVVSLDGDKLVHVQKWDgKE 101

                        90       100
                ....*....|....*....|....*...
gi 78706756  88 TTIVREFTDNELITTLTIGNVKCVRVYK 115
Cdd:cd19470 102 TNFVREIKDGKMVMTLTFGDVVAVRHYE 129

mite group 13 allergens similar to Dermatophagoides farinae Der p 13, and related proteins; The minor house dust mite allergen Der p 13 is a fatty acid-binding protein and an activator of a TLR2-mediated innate immune response. This group also contains other mite group 13 allergens, including Tyrophagus putrescentiae Tyr p 13 and Blomia tropicalis mite blo t 13. blo t 13 binds the natural fluorescent fatty acid cis-parinaric acid and oleic acid by competition, but not retinol, retinoic acid, cholesterol, or dansylated or anthroxylated fatty acids. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  10 FGVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDG-NKLTQEQKGDKPT 88
Cdd:cd19614  21 LGVGFMVKTAAKTLKPTVEVIVDGDSYTFRSLSTFKNTEIKFKLGEEFEEDRADGKKVKTVVTKEGdNKLVQTQFGDKEV 100

                        90       100
                ....*....|....*....|....*..
gi 78706756  89 TIVREFTDNELITTLTIGNVKCVRVYK 115
Cdd:cd19614 101 KIVREFNGDGVVVTASVDGVTSVRTYK 127

fatty acid binding protein 8; FABP8 (also known as peripheral myelin protein 2, PMP2, myelin fatty acid binding protein, M-FABP, myelin P2 protein, MP2) is a fatty acid-binding structural component of the myelin sheath in the peripheral nervous system and may play a role in lipid transport and homeostasis in myelin. It may bind cholesterol which is present in myelin at high concentrations. In addition to binding momomeric ligands, P2 is able to bind membrane surfaces, and to stack lipid bilayers together. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756   9 SFGVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGD-KP 87
Cdd:cd19469  21 ALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTKSTVTLARGSLNQVQKWNgKE 100

                        90       100
                ....*....|....*....|....*...
gi 78706756  88 TTIVREFTDNELITTLTIGNVKCVRVYK 115
Cdd:cd19469 101 TTIKRKLVDGKMVVECKMKGVVCTRIYE 128

fatty acid-binding protein 12; FABP12 is expressed in rodent retina and testis, as well as in human retinoblastoma cell lines. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  10 FGVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGD-KPT 88
Cdd:cd19617  21 LGIGRASRKLGCLAKPTVTISTDGDVITIKTKSIFKNKEISFKLGEEFEEITPGGRKSKSTVTLDNDSLVQVQDWDgKEA 100

                        90       100
                ....*....|....*....|....*..
gi 78706756  89 TIVREFTDNELITTLTIGNVKCVRVYK 115
Cdd:cd19617 101 TITRRLVDGKMVVESAVNNVTCTRTYQ 127

fatty acid-binding protein similar to Manduca sexta and Eriocheir sinensis fatty acid-binding protein 1; This subfamily includes fatty acid-binding protein found mainly in insects such as Manduca sexta FABP1 (also known as MFB1) and Luciola cerata FABP (LcFABP), and crustacea such as Eriocheir sinensis FABP (Es-FABP). MFB1, which is isolated from midgut cytosol, binds fatty acids in a 1:1 molar ratio. LcFABP, abundantly and specifically expressed in the cytosol as well as the nucleus of cells of the photogenic layer of firefly light organ, binds fatty acids of length C14-C18. Es-FABP plays a role in lipid transport during the period of rapid ovarian growth and is involved in lipid nutrient absorption and utilization processes in the hepatopancreas, ovary, and hemocytes. It is also expressed in gills, muscle, thoracic ganglia, heart, and intestine. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  21 NSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGD-KPTTIVREFTDNEL 99
Cdd:cd19448  32 LQYKPSLEVSQNGDKYTFKSTSGDKTKTNTFKLGVEFEETLPGGREFKSVTTLEGNTLTQTSKFGgKKGTRTYEFSDDGL 111

                        90
                ....*....|....*....
gi 78706756 100 ITTLTIGN--VKCVRVYKA 116
Cdd:cd19448 112 VVTLTSNKwdGKAKRYYKR 130

Cellular retinoic acid-binding protein 2; Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. This subgroup includes CRABP2 (also known as CRABP-II, RBP6) which transports retinoic acid to the nucleus, and delivers all-trans-retinoic acid to nuclear retinoic acid receptors. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756   9 SFGVGLVTRKMGNSLS--PTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDG-NKLTQEQ--- 82
Cdd:cd19461  20 VLGVNVMLRKIAVAAAskPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCKSLVKWESeNKMVCEQkll 99

                        90       100       110
                ....*....|....*....|....*....|....
gi 78706756  83 KGDKP-TTIVREFT-DNELITTLTIGNVKCVRVY 114
Cdd:cd19461 100 KGEGPkTSWTRELTnDGELILTMTADDVVCTRVY 133

fatty acid binding protein 11 similar to zebrafish FABP11; This group includes zebrafish FABP11a and FABP11b, Senegalese sole FABP11, and similar proteins. The two copies of the fabp11 gene in the zebrafish genome may have resulted from a fish-specific whole genome duplication event. Fabp11a transcripts have been detected in the liver, brain, heart, testis, muscle, ovary and skin of adult zebrafish while fabp11b transcripts have been found in the brain, heart, ovary and eye in adult tissues. This subgroup belongs to the intracellular fatty-acid binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756   9 SFGVGLVTRKMGNSLSPTVEVTL-EGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTQEQKGD-K 86
Cdd:cd19616  20 AIGVSFATRQMGNRAKPNLVICVdEQGVICMKSQSTFKTTEIKFKLNEEFDETTADDRKTKTTMTLENGKLVQKQTWDgK 99

                        90       100
                ....*....|....*....|....*...
gi 78706756  87 PTTIVREFTDNELITTLTIGNVKCVRVY 114
Cdd:cd19616 100 ETTIEREVQDGKLIAKCTMGDVVAVRTY 127

cellular retinol-binding protein 2; Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. CRBP2 is also known as: "retinol-binding protein 2, cellular", CRABP-II, CRBP2, CRBPII, and RBPC2. Expression of CRBP2 is limited to the small intestine. CRBP2 binds both retinol and retinal; rat CRBP2 appears to bind both with equal affinity, human CRBP2 showed a significantly higher affinity for retinol relative to retinal. CRBP2 can bind all-trans-retinol, all trans-retinal and 13-cis-retinol, but not 9-cis-retinol. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  12 VGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEET--LDGRNVKSIITLDGNKLTQEQKGDKPTT 89
Cdd:cd19463  23 IDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTksLDNRHVKALVTWEGDVLVCVQKGEKENR 102

                        90       100
                ....*....|....*....|....*..
gi 78706756  90 IVREFTD-NELITTLTIGNVKCVRVYK 115
Cdd:cd19463 103 GWKQWIEgDKLYLELTCGDQVCRQVFK 129

liver bile acid-binding protein and similar proteins; Liver bile acid-binding protein (also known as "fatty acid-binding protein, liver", LB-FABP, L-BABP, L-FABP, FABP1) is present in the liver of the vertebrates fish, amphibians, reptiles, and birds but not in mammals. L-BABPs bind free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. The role of L-BABPs may be that of cellular and metabolic trafficking of bile acids; they may be involved in intracellular lipid transport. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  18 KMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKLTqeQKGDKPTTIvREFTDN 97
Cdd:cd19447  29 KMAKDVKPVTEIQQNGDEFVVTSKTPRQTVTNSFTIGKEAEITTMDGKKIKCTVHLEGGKLV--CKSEKFSHI-QEVKGG 105

                        90
                ....*....|....*
gi 78706756  98 ELITTLTIGNVKCVR 112
Cdd:cd19447 106 EMVETLTVGGVTLIR 120

cellular retinol-binding protein 3; Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. This group includes human CRBP3 (also known as retinol-binding protein 5, HRBPiso) which is expressed at highest levels in kidney and liver. CRBP3 binds retinol, and may be a human intracellular carrier of retinol in such tissues. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  12 VGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEE--TLDGRNVKSIITLDGNKLTQEQKGDKPTT 89
Cdd:cd19464  23 VNMALRKIVLLLKPDKEIEHQGNHMTVRTLSTFRNYVMDFDLGVEFEEDlrSVDGRKCQTTVTWEEEKLVCVQKGEVPNR 102

                        90       100
                ....*....|....*....|....*....
gi 78706756  90 IVREFTDNELI-TTLTIGNVKCVRVYKAV 117
Cdd:cd19464 103 GWRHWLEGEMLhLELTARDAVCKQVFRKV 131

fatty acid-binding protein 2; FABP2 (also known as fatty acid-binding protein 2, intestinal, and I-FABP) is a small cytosolic protein abundantly present in mature enterocytes of small and large intestine and responsible for the absorption and intracellular transport of fatty acids. It is present throughout the small intestine; its highest expression is in the jejunum. It is a sensitive marker for damage to the intestinal epithelium. This subgroup belongs to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706756  11 GVGLVTRKMGNSLSPTVEVTLEGDTYTLTTTSTFKTSAISFKLGVEFDEETLDGRNVKSIITLDGNKL----TQEQKGdK 86
Cdd:cd19445  22 GVNIVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIEIVFELGVTFEYSLADGTELTGTWSLEGNKLvgkfKRKDNG-K 100

                        90       100
                ....*....|....*....|....*....
gi 78706756  87 PTTIVREFTDNELITTLTIGNVKCVRVYK 115
Cdd:cd19445 101 ELTTVREIIGDELVQTYVYEGVEAKRIFK 129