▁q 3 2 . 1 ▁and ▁consists ▁of ▁ 4 ▁ex ons ▁that ▁code ▁for ▁a ▁protein ▁of ▁ 1 2 1 0 ▁am ino ▁ac ids ▁( 1 3 7 ▁k Da ). ▁ ▁Little ▁is ▁known ▁about ▁the ▁characteristics ▁and ▁function ▁of ▁the ▁encoded ▁protein . ▁However , ▁the ▁protein ▁sequence ▁codes ▁for ▁a ▁domain ▁characteristic ▁of ▁a ▁classical ▁C 2 H 2 - type ▁z inc ▁finger ▁near ▁the ▁N - term inal ▁end . ▁ ▁Inter actions ▁ ▁Z NF 8 0 4 A ▁bind s ▁to ▁the ▁N - ter minus ▁of ▁AT X N 1 . ▁ ▁Binding ▁of ▁DNA ▁ ▁The ▁t ert i ary ▁structure ▁of ▁the ▁C 2 H 2 ▁finger ▁consists ▁of ▁a ▁beta ▁hair pin ▁fol ded ▁against ▁an ▁alpha ▁hel ix . ▁The ▁fol ding ▁occurs ▁via ▁a ▁z inc ( II ) ▁ion ▁that ▁coordinates ▁to ▁two ▁c yst e ine ▁resid ues ▁( one ▁on ▁each ▁beta ▁sheet ) ▁and ▁two ▁hist id ine ▁resid ues ▁( both ▁on ▁the ▁α - hel ix ). ▁Z NF 8 0 4 A ▁might ▁use ▁its ▁z inc ▁finger ▁to ▁bind ▁DNA ▁in ▁a ▁sequence - specific ▁manner . ▁For ▁example , ▁Carl ▁P ab o ▁and ▁his ▁colle agues ▁in ▁ 1 9 9 1 ▁discovered ▁that ▁mouse ▁trans cription ▁factor ▁Z if 2 6 8 ▁bind s ▁DNA ▁using ▁three ▁linked ▁C 2 H 2 ▁z inc ▁fingers . ▁A min o ▁acid ▁resid ues ▁stick ing ▁out ▁from