eF-site ID 1hvg-A PDB Code 1hvg Chain A click to enlarge Title STRUCTURAL AND ELECTROPHYSIOLOGICAL ANALYSIS OF ANNEXIN V MUTANTS. MUTAGENESIS OF HUMAN ANNEXIN V, AN IN VITRO VOLTAGE-GATED CALCIUM CHANNEL, PROVIDES INFORMATION ABOUT THE STRUCTURAL FEATURES OF THE ION PATHWAY, THE VOLTAGE SENSOR AND THE ION SELECTIVITY FILTER Classification CALCIUM/PHOSPHOLIPID BINDING Compound ANNEXIN V Source (ANXA5_HUMAN) Sequence A:  VLRGTVTDFPGFDERADAETLRKAMKGLGTDEESILTLLT SRSNAQRQEISAAFKTLFGRDLLDDLKSELTGKFQKLIVA LMKPSRLYDAYELKHALKGAGTNEKVLTEIIASRTPEELR AIKQVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRDP DAGIDEAQVEQDAQALFQAGELKWGTDEEKFITIFGTRSV SHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAVVKS IRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLFN IRKEFRKNFATSLYSMIKGDTSGDYKKALLLLC Description Functional site 1) chain A residue 32-84 type prosite sequence GTDEESILTLLTSRSNAQRQEISAAFKTLFGRDLLDDLKS ELTGKFQKLIVAL description ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfqklIvaL source prosite : PS00223 2) chain A residue 104-156 type prosite sequence GTNEKVLTEIIASRTPEELRAIKQVYEEEYGSSLEDDVVG DTSGYYQRMLVVL description ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfqklIvaL source prosite : PS00223 3) chain A residue 188-240 type prosite sequence GTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDR ETSGNLEQLLLAV description ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfqklIvaL source prosite : PS00223 4) chain A residue 263-315 type prosite sequence GTDDHTLIRVMVSRSEIDLFNIRKEFRKNFATSLYSMIKG DTSGDYKKALLLL description ANNEXIN_1 Annexin repeat signature. GTdeesiltlLtsRsnaQrqEisaaFktlfgrdLlddLkseltGkfqklIvaL source prosite : PS00223 5) chain A residue 30 type CROSSLNK sequence G description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 6) chain A residue 38 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P48036 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 71 type MOD_RES sequence S description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 8) chain A residue 77 type MOD_RES sequence F description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 80 type MOD_RES sequence L description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 98 type MOD_RES sequence H description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 102 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:16916647 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 291 type MOD_RES sequence N description N6-succinyllysine => ECO:0000250|UniProtKB:P48036 source Swiss-Prot : SWS_FT_FI5

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