eF-site ID 3j9p-ABCD PDB Code 3j9p Chain A, B, C, D Title Structure of the TRPA1 ion channel determined by electron cryo-microscopy Classification TRANSPORT PROTEIN Compound Maltose-binding periplasmic protein, Transient receptor potential cation channel subfamily A member 1 chimera Source (TRPA1_HUMAN) Sequence A:  KKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTP LHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGG YTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGHAKAVA LLLSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRW DECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHS TEDKSCRDYYIEYNFKYLYEPLTALNAMVQNNRIELLNHP VCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIK PGMAFNTTNSYLIKTCMILVFLSSIFGYISNVLEWIIYTT GIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQRFE NCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNL QDPFSSPLLSIIQTFSMMLGDINYRESFLEPYLRNELAHP VLSFAQLVSFTIFVPIVLMNLLIGLAVGDIADVQKHASLK RIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYQEIPNADK SLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISET B:  KKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTP LHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGG YTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGHAKAVA LLLSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRW DECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHS TEDKSCRDYYIEYNFKYLYEPLTALNAMVQNNRIELLNHP VCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIK PGMAFNTTNSYLIKTCMILVFLSSIFGYISNVLEWIIYTT GIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQRFE NCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNL QDPFSSPLLSIIQTFSMMLGDINYRESFLEPYLRNELAHP VLSFAQLVSFTIFVPIVLMNLLIGLAVGDIADVQKHASLK RIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYQEIPNADK SLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISET C:  KKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTP LHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGG YTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGHAKAVA LLLSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRW DECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHS TEDKSCRDYYIEYNFKYLYEPLTALNAMVQNNRIELLNHP VCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIK PGMAFNTTNSYLIKTCMILVFLSSIFGYISNVLEWIIYTT GIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQRFE NCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNL QDPFSSPLLSIIQTFSMMLGDINYRESFLEPYLRNELAHP VLSFAQLVSFTIFVPIVLMNLLIGLAVGDIADVQKHASLK RIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYQEIPNADK SLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISET D:  KKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTP LHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGG YTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGHAKAVA LLLSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRW DECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHS TEDKSCRDYYIEYNFKYLYEPLTALNAMVQNNRIELLNHP VCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIK PGMAFNTTNSYLIKTCMILVFLSSIFGYISNVLEWIIYTT GIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQRFE NCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNL QDPFSSPLLSIIQTFSMMLGDINYRESFLEPYLRNELAHP VLSFAQLVSFTIFVPIVLMNLLIGLAVGDIADVQKHASLK RIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYQEIPNADK SLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISET Description Functional site 1) chain D residue 1046 type BINDING sequence K description BINDING => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI14 2) chain A residue 1046 type BINDING sequence K description BINDING => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI14 3) chain B residue 1046 type BINDING sequence K description BINDING => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI14 4) chain C residue 1046 type BINDING sequence K description BINDING => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI14 5) chain D residue 620 type SITE sequence K description Required for C-621 reactivity => ECO:0000269|PubMed:27241698 source Swiss-Prot : SWS_FT_FI15 6) chain A residue 620 type SITE sequence K description Required for C-621 reactivity => ECO:0000269|PubMed:27241698 source Swiss-Prot : SWS_FT_FI15 7) chain B residue 620 type SITE sequence K description Required for C-621 reactivity => ECO:0000269|PubMed:27241698 source Swiss-Prot : SWS_FT_FI15 8) chain C residue 620 type SITE sequence K description Required for C-621 reactivity => ECO:0000269|PubMed:27241698 source Swiss-Prot : SWS_FT_FI15 9) chain D residue 634 type SITE sequence M description Important residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI17 10) chain D residue 646 type SITE sequence T description Important residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI17 11) chain A residue 634 type SITE sequence M description Important residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI17 12) chain A residue 646 type SITE sequence T description Important residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI17 13) chain B residue 634 type SITE sequence M description Important residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI17 14) chain B residue 646 type SITE sequence T description Important residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI17 15) chain C residue 634 type SITE sequence M description Important residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI17 16) chain C residue 646 type SITE sequence T description Important residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI17 17) chain D residue 741-764 type TOPO_DOM sequence KPGMAFNT description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 825-829 type TOPO_DOM sequence EIPAH description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 895-901 type TOPO_DOM sequence QDPFSSP description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 923-934 type TOPO_DOM sequence LEPYLRNELAHP description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 21) chain C residue 741-764 type TOPO_DOM sequence KPGMAFNT description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 22) chain C residue 825-829 type TOPO_DOM sequence EIPAH description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 895-901 type TOPO_DOM sequence QDPFSSP description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 24) chain C residue 923-934 type TOPO_DOM sequence LEPYLRNELAHP description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 25) chain D residue 825-829 type TOPO_DOM sequence EIPAH description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 26) chain D residue 895-901 type TOPO_DOM sequence QDPFSSP description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 27) chain D residue 923-934 type TOPO_DOM sequence LEPYLRNELAHP description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 741-764 type TOPO_DOM sequence KPGMAFNT description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 825-829 type TOPO_DOM sequence EIPAH description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 895-901 type TOPO_DOM sequence QDPFSSP description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 923-934 type TOPO_DOM sequence LEPYLRNELAHP description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 741-764 type TOPO_DOM sequence KPGMAFNT description Extracellular => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI2 33) chain D residue 765-785 type TRANSMEM sequence TNSYLIKTCMILVFLSSIFGY description Helical; Name=2 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 765-785 type TRANSMEM sequence TNSYLIKTCMILVFLSSIFGY description Helical; Name=2 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI3 35) chain B residue 765-785 type TRANSMEM sequence TNSYLIKTCMILVFLSSIFGY description Helical; Name=2 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI3 36) chain C residue 765-785 type TRANSMEM sequence TNSYLIKTCMILVFLSSIFGY description Helical; Name=2 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI3 37) chain C residue 851-873 type TOPO_DOM sequence QRFENCGIFIVMLEVILKTLLRS description Cytoplasmic => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI4 38) chain D residue 851-873 type TOPO_DOM sequence QRFENCGIFIVMLEVILKTLLRS description Cytoplasmic => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI4 39) chain A residue 851-873 type TOPO_DOM sequence QRFENCGIFIVMLEVILKTLLRS description Cytoplasmic => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI4 40) chain B residue 851-873 type TOPO_DOM sequence QRFENCGIFIVMLEVILKTLLRS description Cytoplasmic => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI4 41) chain D residue 804-824 type TRANSMEM sequence SNVLEWIIYTTGIIFVLPLFV description Helical; Name=3 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI5 42) chain A residue 804-824 type TRANSMEM sequence SNVLEWIIYTTGIIFVLPLFV description Helical; Name=3 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI5 43) chain B residue 804-824 type TRANSMEM sequence SNVLEWIIYTTGIIFVLPLFV description Helical; Name=3 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI5 44) chain C residue 804-824 type TRANSMEM sequence SNVLEWIIYTTGIIFVLPLFV description Helical; Name=3 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI5 45) chain D residue 830-850 type TRANSMEM sequence LQWQCGAIAVYFYWMNFLLYL description Helical; Name=4 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI6 46) chain A residue 830-850 type TRANSMEM sequence LQWQCGAIAVYFYWMNFLLYL description Helical; Name=4 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI6 47) chain B residue 830-850 type TRANSMEM sequence LQWQCGAIAVYFYWMNFLLYL description Helical; Name=4 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI6 48) chain C residue 830-850 type TRANSMEM sequence LQWQCGAIAVYFYWMNFLLYL description Helical; Name=4 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI6 49) chain D residue 874-894 type TRANSMEM sequence TVVFIFLLLAFGLSFYILLNL description Helical; Name=5 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI7 50) chain A residue 874-894 type TRANSMEM sequence TVVFIFLLLAFGLSFYILLNL description Helical; Name=5 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI7 51) chain B residue 874-894 type TRANSMEM sequence TVVFIFLLLAFGLSFYILLNL description Helical; Name=5 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI7 52) chain C residue 874-894 type TRANSMEM sequence TVVFIFLLLAFGLSFYILLNL description Helical; Name=5 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI7 53) chain D residue 902-922 type INTRAMEM sequence LLSIIQTFSMMLGDINYRESF description Pore-forming => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI8 54) chain A residue 902-922 type INTRAMEM sequence LLSIIQTFSMMLGDINYRESF description Pore-forming => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI8 55) chain B residue 902-922 type INTRAMEM sequence LLSIIQTFSMMLGDINYRESF description Pore-forming => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI8 56) chain C residue 902-922 type INTRAMEM sequence LLSIIQTFSMMLGDINYRESF description Pore-forming => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI8 57) chain D residue 935-956 type TRANSMEM sequence VLSFAQLVSFTIFVPIVLMNLL description Helical; Name=6 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI9 58) chain A residue 935-956 type TRANSMEM sequence VLSFAQLVSFTIFVPIVLMNLL description Helical; Name=6 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI9 59) chain B residue 935-956 type TRANSMEM sequence VLSFAQLVSFTIFVPIVLMNLL description Helical; Name=6 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI9 60) chain C residue 935-956 type TRANSMEM sequence VLSFAQLVSFTIFVPIVLMNLL description Helical; Name=6 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI9 61) chain D residue 468-480 type prosite sequence DISDTRLLNEGDL description EF_HAND_1 EF-hand calcium-binding domain. DISDTRLLNegDL source prosite : PS00018 62) chain D residue 621 type BINDING sequence C description covalent; Cys highly reactive => ECO:0000250|UniProtKB:Q8BLA8, ECO:0000305|PubMed:17164327, ECO:0000305|PubMed:27241698 source Swiss-Prot : SWS_FT_FI11 63) chain A residue 621 type BINDING sequence C description covalent; Cys highly reactive => ECO:0000250|UniProtKB:Q8BLA8, ECO:0000305|PubMed:17164327, ECO:0000305|PubMed:27241698 source Swiss-Prot : SWS_FT_FI11 64) chain B residue 621 type BINDING sequence C description covalent; Cys highly reactive => ECO:0000250|UniProtKB:Q8BLA8, ECO:0000305|PubMed:17164327, ECO:0000305|PubMed:27241698 source Swiss-Prot : SWS_FT_FI11 65) chain C residue 621 type BINDING sequence C description covalent; Cys highly reactive => ECO:0000250|UniProtKB:Q8BLA8, ECO:0000305|PubMed:17164327, ECO:0000305|PubMed:27241698 source Swiss-Prot : SWS_FT_FI11 66) chain D residue 641 type BINDING sequence C description covalent => ECO:0000305|PubMed:17164327 source Swiss-Prot : SWS_FT_FI12 67) chain D residue 710 type BINDING sequence K description covalent => ECO:0000305|PubMed:17164327 source Swiss-Prot : SWS_FT_FI12 68) chain A residue 641 type BINDING sequence C description covalent => ECO:0000305|PubMed:17164327 source Swiss-Prot : SWS_FT_FI12 69) chain A residue 710 type BINDING sequence K description covalent => ECO:0000305|PubMed:17164327 source Swiss-Prot : SWS_FT_FI12 70) chain B residue 641 type BINDING sequence C description covalent => ECO:0000305|PubMed:17164327 source Swiss-Prot : SWS_FT_FI12 71) chain B residue 710 type BINDING sequence K description covalent => ECO:0000305|PubMed:17164327 source Swiss-Prot : SWS_FT_FI12 72) chain C residue 641 type BINDING sequence C description covalent => ECO:0000305|PubMed:17164327 source Swiss-Prot : SWS_FT_FI12 73) chain C residue 710 type BINDING sequence K description covalent => ECO:0000305|PubMed:17164327 source Swiss-Prot : SWS_FT_FI12 74) chain D residue 720-740 type TRANSMEM sequence MMNLGSYCLGLIPMTILVVNI description Helical; Name=1 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI1 75) chain A residue 720-740 type TRANSMEM sequence MMNLGSYCLGLIPMTILVVNI description Helical; Name=1 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 720-740 type TRANSMEM sequence MMNLGSYCLGLIPMTILVVNI description Helical; Name=1 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI1 77) chain C residue 720-740 type TRANSMEM sequence MMNLGSYCLGLIPMTILVVNI description Helical; Name=1 => ECO:0000305|PubMed:25855297 source Swiss-Prot : SWS_FT_FI1 78) chain D residue 747 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI20 79) chain A residue 747 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI20 80) chain B residue 747 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI20 81) chain C residue 747 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI20 82) chain D residue 622 type SITE sequence P description Key residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI16 83) chain A residue 622 type SITE sequence P description Key residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI16 84) chain B residue 622 type SITE sequence P description Key residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI16 85) chain C residue 622 type SITE sequence P description Key residue for activation by the scorpion wasabi receptor toxin => ECO:0000269|PubMed:31447178 source Swiss-Prot : SWS_FT_FI16 86) chain D residue 633 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH); transient; in hyperoxia => ECO:0000305|PubMed:21873995 source Swiss-Prot : SWS_FT_FI19 87) chain D residue 856 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH); transient; in hyperoxia => ECO:0000305|PubMed:21873995 source Swiss-Prot : SWS_FT_FI19 88) chain A residue 633 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH); transient; in hyperoxia => ECO:0000305|PubMed:21873995 source Swiss-Prot : SWS_FT_FI19 89) chain A residue 856 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH); transient; in hyperoxia => ECO:0000305|PubMed:21873995 source Swiss-Prot : SWS_FT_FI19 90) chain B residue 633 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH); transient; in hyperoxia => ECO:0000305|PubMed:21873995 source Swiss-Prot : SWS_FT_FI19 91) chain B residue 856 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH); transient; in hyperoxia => ECO:0000305|PubMed:21873995 source Swiss-Prot : SWS_FT_FI19 92) chain C residue 633 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH); transient; in hyperoxia => ECO:0000305|PubMed:21873995 source Swiss-Prot : SWS_FT_FI19 93) chain C residue 856 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH); transient; in hyperoxia => ECO:0000305|PubMed:21873995 source Swiss-Prot : SWS_FT_FI19

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