GST_N family, Metaxin subfamily, Metaxin 2; a metaxin 1 binding protein identified through a yeast two-hybrid system using metaxin 1 as the bait. Metaxin 2 shares sequence similarity with metaxin 1 but does not contain a C-terminal mitochondrial outer membrane signal-anchor domain. It associates with mitochondrial membranes through its interaction with metaxin 1, which is a component of the mitochondrial preprotein import complex of the outer membrane. The biological function of metaxin 2 is unknown. It is likely that it also plays a role in protein translocation into the mitochondria. However, this has not been experimentally validated. In a recent proteomics study, it has been shown that metaxin 2 is overexpressed in response to lipopolysaccharide-induced liver injury.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086881  22 AALYQPLKEDQILLSDSASSLAVQTFLRMCGLPVQVSCRANAEYMSPSGKVPFIQVGNQVVSELGPIVQFTKAK 95
Cdd:cd03079   1 AALYQPYEEEQILLPDNASCLAVQTFLKMCNLPFNVRCRANAEFMSPSGKVPFIRVGNQIVSEFGPIVQFVEAK 74

GST_N family, Metaxin subfamily, Metaxin 2; a metaxin 1 binding protein identified through a yeast two-hybrid system using metaxin 1 as the bait. Metaxin 2 shares sequence similarity with metaxin 1 but does not contain a C-terminal mitochondrial outer membrane signal-anchor domain. It associates with mitochondrial membranes through its interaction with metaxin 1, which is a component of the mitochondrial preprotein import complex of the outer membrane. The biological function of metaxin 2 is unknown. It is likely that it also plays a role in protein translocation into the mitochondria. However, this has not been experimentally validated. In a recent proteomics study, it has been shown that metaxin 2 is overexpressed in response to lipopolysaccharide-induced liver injury.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086881  22 AALYQPLKEDQILLSDSASSLAVQTFLRMCGLPVQVSCRANAEYMSPSGKVPFIQVGNQVVSELGPIVQFTKAK 95
Cdd:cd03079   1 AALYQPYEEEQILLPDNASCLAVQTFLKMCNLPFNVRCRANAEFMSPSGKVPFIRVGNQIVSEFGPIVQFVEAK 74

Outer mitochondrial membrane transport complex protein; The TOM37 protein is one of the outer membrane proteins that make up the TOM complex for guiding cytosolic mitochondrial beta-barrel proteins from the cytosol across the outer mitochondrial membrane into the intra-membrane space. In conjunction with TOM70 it guides peptides without an MTS into TOM40, the protein that forms the passage through the outer membrane. It has homology with Metaxin-1, also part of the outer mitochondrial membrane beta-barrel protein transport complex.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086881    41 SLAVQTFLRMCGLP--VQVSCRANAEyMSPSGKVPFIQVGN-QVVSELGPIVQF--TKAKGHSLSDGLDDVQRAEMKAYM 115
Cdd:pfam10568   1 CLAAIAYLKLLALPapFEVVPSNNPD-LSPTGELPALIDGDgTWVSGFDSIVEYlrSKGGGYDLDADLSAKQKADSLAYI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 47086881   116 ELVNNMLLTAELYIQWCDDFTATEISRPRYSSPYSWPLNHILAYQKQ 162
Cdd:pfam10568  80 SLLESKLYPLLLYSLWVDEENYEEVTRPAYSKLLPFPLNYILPLKYR 126

GST_N family, Metaxin subfamily, Metaxin 2; a metaxin 1 binding protein identified through a yeast two-hybrid system using metaxin 1 as the bait. Metaxin 2 shares sequence similarity with metaxin 1 but does not contain a C-terminal mitochondrial outer membrane signal-anchor domain. It associates with mitochondrial membranes through its interaction with metaxin 1, which is a component of the mitochondrial preprotein import complex of the outer membrane. The biological function of metaxin 2 is unknown. It is likely that it also plays a role in protein translocation into the mitochondria. However, this has not been experimentally validated. In a recent proteomics study, it has been shown that metaxin 2 is overexpressed in response to lipopolysaccharide-induced liver injury.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086881  22 AALYQPLKEDQILLSDSASSLAVQTFLRMCGLPVQVSCRANAEYMSPSGKVPFIQVGNQVVSELGPIVQFTKAK 95
Cdd:cd03079   1 AALYQPYEEEQILLPDNASCLAVQTFLKMCNLPFNVRCRANAEFMSPSGKVPFIRVGNQIVSEFGPIVQFVEAK 74

Outer mitochondrial membrane transport complex protein; The TOM37 protein is one of the outer membrane proteins that make up the TOM complex for guiding cytosolic mitochondrial beta-barrel proteins from the cytosol across the outer mitochondrial membrane into the intra-membrane space. In conjunction with TOM70 it guides peptides without an MTS into TOM40, the protein that forms the passage through the outer membrane. It has homology with Metaxin-1, also part of the outer mitochondrial membrane beta-barrel protein transport complex.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086881    41 SLAVQTFLRMCGLP--VQVSCRANAEyMSPSGKVPFIQVGN-QVVSELGPIVQF--TKAKGHSLSDGLDDVQRAEMKAYM 115
Cdd:pfam10568   1 CLAAIAYLKLLALPapFEVVPSNNPD-LSPTGELPALIDGDgTWVSGFDSIVEYlrSKGGGYDLDADLSAKQKADSLAYI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 47086881   116 ELVNNMLLTAELYIQWCDDFTATEISRPRYSSPYSWPLNHILAYQKQ 162
Cdd:pfam10568  80 SLLESKLYPLLLYSLWVDEENYEEVTRPAYSKLLPFPLNYILPLKYR 126

C-terminal, alpha helical domain of Metaxin 1, Metaxin 3, and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Metaxin subfamily, Metaxin 1-like proteins; composed of metaxins 1 and 3, and similar proteins. Mammalian metaxin (or metaxin 1) is a component of the preprotein import complex of the mitochondrial outer membrane. Metaxin extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. Like the murine gene, the human metaxin gene is located downstream to the glucocerebrosidase (GBA) pseudogene and is convergently transcribed. Inherited deficiency of GBA results in Gaucher disease, which presents many diverse clinical phenotypes. Alterations in the metaxin gene, in addition to GBA mutations, may be associated with Gaucher disease. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken, and mammals.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086881 125 AELYIQWCDDFTATEISRPRYSSPYSWPLNHILaYQKQweVRRKMNAIG--------WSGKSLE-QVYEDVSQCCQALSQ 195
Cdd:cd03212   2 ALLYTLWVDEKNYVEVTRPWYAKALPFPLNFYY-PGRY--QRRAKDRLQllrglselDSEEEVEkELYKDAKECLNLLSE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 47086881 196 RLGTQPYFFNKQPTELDALVFGHLFTILTTQLTSDELVEKVKSYSNLLSFCHRIEQAYF 254
Cdd:cd03212  79 RLGEKKFFFGDRPTSLDALVFGYLAPLLKAPLPNNKLQNHLKGCPNLVQFVDRILQNYF 137

GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47086881  24 LYQPlKEDQILLSDSASSLAVQTFLRMCGLPVQVSCRANAEyMSPSGKVPFIQVGNQVVSELGPIVQFTKAK 95
Cdd:cd03054   3 LYQW-GRAFGLPSLSPECLKVETYLRMAGIPYEVVFSSNPW-RSPTGKLPFLELNGEKIADSEKIIEYLKKK 72

Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK subfamily, a member of the DsbA family). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxin 2 and stringent starvation protein A.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47086881  38 SASSLAVQTFLRMCGLPVQV-----SCRANAEY--MSPSGKVPFIQVGNQVVSELGPIVQF 91
Cdd:cd00570   9 SPRSLRVRLALEEKGLPYELvpvdlGEGEQEEFlaLNPLGKVPVLEDGGLVLTESLAILEY 69

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086881 125 AELYIQWCDDFTATEISRPRYSSPYSWPlnhilayqkqwevrrkmnaigWSGKSLEQVYEDVSQCCQALSQRLGTQPYFF 204
Cdd:cd00299   1 VRALEDWADATLAPPLVRLLYLEKVPLP---------------------KDEAAVEAAREELPALLAALEQLLAGRPYLA 59

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 47086881 205 NKQPTELDALVFGHLFTILTTQLTSDELvekvKSYSNLLSFCHRI 249
Cdd:cd00299  60 GDQFSLADVALAPVLARLEALGPYYDLL----DEYPRLKAWYDRL 100