sujigwak/NVAR huggingface dataset:
UniProt ID: P24892
Variant: I -> S at position 61-61
Variant annotation: in strain: PB306
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24892
Variant: S -> G at position 64-64
Variant annotation: in strain: PB306
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24892
Variant: L -> V at position 70-70
Variant annotation: in strain: PB306
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24892
Variant: G -> S at position 317-317
Variant annotation: in strain: PB303
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24892
Variant: SAPLVLMMYNVFWLSVFY -> QHH at position 392-409
Variant annotation: in strain: KR314
Protein function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Reference sequence:
MLEFLFISLLWLFKPIYFLLFTVMFSFLIFNNFSWGGLFLVLDSYSFILLIVMSLFILGIIVISEKNNNLLILSEILVFICIIFFIPSNMMMLYMFFELSMFPILVMILGYGSQIEKINSSYYLMFYAAFCSFPFLFVYFKSNFLLVFTYYNFVISWEMFFILSLSFMMKFPIYFLHLWLPKAHVEAPTTASMLLAGLLLKLGTAGFLRILGSLSFVHNNVWILIAFLGMILGSFCCVFQSDSKALAAYSSVTHMSFLLLSLVFITMSSKISSVMLMLAHGYTSTLMFYLIGEFYHTSGSRMIYFMSSFFSSSMIMGILFSVVFLSNSGVPPSLSFLSEFLVISNSMLISKSMFVMIFIYFVVSFYYSLFLITSSLMGKGYHNFNTWNVGFSAPLVLMMYNVFWLSVFY
UniProt ID: P24893
Variant: A -> S at position 12-12
Variant annotation: in strain: CB4856 and CB4857
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MNLYKKYQGGLAVWLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPLMLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHAAGLSSILGGINFMCTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLATLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISDYYSNSSPEYCMSNYVFGHSYQSEIYFSTTSLKN
UniProt ID: P24893
Variant: I -> M at position 466-466
Variant annotation: in strain: AB1, AB2, CB4852, CB4853, CB4855, CB4857, CB4858, KR314 and PB306
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MNLYKKYQGGLAVWLESSNHKDIGTLYFIFGLWSGMVGTSFSLLIRLELAKPGFFLSNGQLYNSVITAHAILMIFFMVMPTMIGGFGNWLLPLMLGAPDMSFPRLNNLSFWLLPTSMLLILDACFVDMGCGTSWTVYPPLSTMGHPGSSVDLAIFSLHAAGLSSILGGINFMCTTKNLRSSSISLEHMTLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLIYQHLFWFFGHPEVYILILPAFGIVSQSTLYLTGKKEVFGALGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFSAATMVIAVPTGVKVFSWLATLFGMKMVFNPLLLWVLGFIFLFTLGGLTGVVLSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGVTLWWSFITGYVLDKLMMSAVFILLFIGVNLTFFPLHFAGLHGFPRKYLDYPDVYSVWNIIASYGSIISTAGLFLFIYVLLESFFSYRLVISDYYSNSSPEYCMSNYVFGHSYQSEIYFSTTSLKN
UniProt ID: P24894
Variant: S -> N at position 132-132
Variant annotation: in strain: PB303
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MNNFFQGYNLLFQHSLFASYMDWFHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLDQLSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFSYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME
UniProt ID: P24894
Variant: N -> I at position 143-143
Variant annotation: in strain: CB4857
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MNNFFQGYNLLFQHSLFASYMDWFHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLDQLSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFSYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME
UniProt ID: P24894
Variant: S -> N at position 186-186
Variant annotation: in strain: AB2, CB4852, CB4853, CB4855, CB4858 and PB306
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MNNFFQGYNLLFQHSLFASYMDWFHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLDQLSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFSYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME
UniProt ID: P24894
Variant: V -> M at position 216-216
Variant annotation: in strain: AB1 and KR314
Protein function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Reference sequence:
MNNFFQGYNLLFQHSLFASYMDWFHSFNCSLLLGVLVFVTLLFGYLIFGTFYFKSKKIEYQFGELLCSIFPTIILLMQMVPSLSLLYYYGLMNLDSNLTVKVTGHQWYWSYEYSDIPGLEFDSYMKSLDQLSLGEPRLLEVDNRCVIPCDTNIRFCITSADVIHAWALNSLSVKLDAMSGILSTFSYSFPMVGVFYGQCSEICGANHSFMPIALEVTLLDNFKSWCFGTME
UniProt ID: P24903
Variant: S -> P at position 38-38
Variant annotation: in allele CYP2F1*4; dbSNP:rs58285195
Protein function: May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3-methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine.
Reference sequence:
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNLPRPFQLCLRPR
UniProt ID: P24903
Variant: R -> P at position 98-98
Variant annotation: in allele CYP2F1*6; dbSNP:rs57670668
Protein function: May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3-methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine.
Reference sequence:
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNLPRPFQLCLRPR
UniProt ID: P24903
Variant: D -> N at position 218-218
Variant annotation: in allele CYP2F1*3 and in allele CYP2F1*4; dbSNP:rs305974
Protein function: May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3-methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine.
Reference sequence:
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNLPRPFQLCLRPR
UniProt ID: P24903
Variant: Q -> H at position 266-266
Variant annotation: in allele CYP2F1*3; dbSNP:rs75405062
Protein function: May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3-methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine.
Reference sequence:
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNLPRPFQLCLRPR
UniProt ID: P24903
Variant: L -> P at position 391-391
Variant annotation: in allele CYP2F1*5A and in allele CYP2F1*5B; dbSNP:rs144315434
Protein function: May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3-methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine.
Reference sequence:
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNLPRPFQLCLRPR
UniProt ID: P24903
Variant: P -> L at position 490-490
Variant annotation: in allele CYP2F1*3; dbSNP:rs7246981
Protein function: May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3-methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine.
Reference sequence:
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNLPRPFQLCLRPR
UniProt ID: P25024
Variant: M -> R at position 31-31
Variant annotation: in dbSNP:rs16858811
Protein function: Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor . Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system .
Reference sequence:
MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL
UniProt ID: P25024
Variant: R -> C at position 71-71
Variant annotation: in dbSNP:rs1805038
Protein function: Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor . Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system .
Reference sequence:
MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL
UniProt ID: P25024
Variant: M -> L at position 268-268
Variant annotation: in dbSNP:rs9282752
Protein function: Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor . Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system .
Reference sequence:
MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL
UniProt ID: P25024
Variant: S -> T at position 276-276
Variant annotation: in dbSNP:rs2234671
Protein function: Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor . Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system .
Reference sequence:
MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL
UniProt ID: P25024
Variant: A -> T at position 306-306
Variant annotation: in dbSNP:rs201583693
Protein function: Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor . Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system .
Reference sequence:
MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL