UniProtKB/SwissProt variant VAR

Carbonic anhydrase 2
Gene: CA2
Feedback?

Variant information Variant position:

107
Type of variant:

LP/P [Disclaimer]
Residue change:

From Histidine (H) to Tyrosine (Y) at position 107 (H107Y, p.His107Tyr).
Physico-chemical properties:

Change from medium size and polar (H) to large size and aromatic (Y)
BLOSUM score:

2
Variant description:

In OPTB3.
Other resources:

Variant rs118203933 [ dbSNP | Ensembl ]

Sequence information Variant position:

107
Protein sequence length:

260
Location on the sequence:

TYRLIQFHFHWGSLDGQGSE H TVDKKKYAAELHLVHWNTKY
Residue conservation:

Human                         TYRLIQFHFHWGSLD--GQGSEHTVDKKKYAAELHLVHWNTK-Y

Mouse                         SYRLIQFHFHWGSSD--GQGSEHTVNKKKYAAELHLVHWNT

Rat                           SYRLIQFHFHWGSSD--GQGSEHTVNKKKYAAELHLVHWNT

Bovine                        TYRLVQFHFHWGSSD--DQGSEHTVDRKKYAAELHLVHWNT

Rabbit                        TYRLIQFHFHWGSSD--GQGSEHTVNKKKYAAELHLVHWNT

Sheep                         TYRLVQFHFHWGSSD--DQGSEHTVDRKKYAAELHLVHWNT

Chicken                       VYRLVQFHIHWGSCE--GQGSEHTVDGVKYDAELHIVHWNV

Caenorhabditis elegans        RYKLHQISVHFGRADEGEKGSEHTVDRVRFPAEIQLLAYNS

Sequence annotation in neighborhood:

Type	Positions	Description
Chain	2 – 260	Carbonic anhydrase 2
Domain	3 – 259	Alpha-carbonic anhydrase
Binding site	94 – 94
Binding site	96 – 96
Binding site	119 – 119
Site	92 – 92	Involved in the binding of some activators, including histamine and L-histidine
Mutagenesis	94 – 94	H -> CDENQ. Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding.
Mutagenesis	106 – 106	E -> AQ. Strongly reduced CO(2) hydrase activity.
Mutagenesis	106 – 106	E -> D. Normal CO(2) hydrase activity.
Mutagenesis	117 – 117	E -> Q. Strongly reduced activity and sulfonamide affinity.
Mutagenesis	119 – 119	H -> DNQ. Reduced activity.
Mutagenesis	119 – 119	H -> E. Strongly reduced activity.
Mutagenesis	121 – 121	V -> AGILS. Reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities.
Mutagenesis	121 – 121	V -> KR. Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities.
Beta strand	106 – 109

Literature citations
Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His-->Tyr): complete structure of the normal human CA II gene.
Venta P.J.; Welty R.J.; Johnson T.M.; Sly W.S.; Tashian R.E.;
Am. J. Hum. Genet. 49:1082-1090(1991)
Cited for: VARIANT OPTB3 TYR-107; Molecular basis of human carbonic anhydrase II deficiency.
Roth D.E.; Venta P.J.; Tashian R.E.; Sly W.S.;
Proc. Natl. Acad. Sci. U.S.A. 89:1804-1808(1992)
Cited for: VARIANT OPTB3 TYR-107; A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese patients with carbonic anhydrase II deficiency with central nervous system involvement.
Soda H.; Yukizane S.; Yoshida I.; Koga Y.; Aramaki S.; Kato H.;
Hum. Genet. 97:435-437(1996)
Cited for: VARIANT OPTB3 TYR-107; Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype-phenotype correlation.
Shah G.N.; Bonapace G.; Hu P.Y.; Strisciuglio P.; Sly W.S.;
Hum. Mutat. 24:272-272(2004)
Cited for: VARIANTS OPTB3 PRO-92; TYR-94; TYR-107 AND ARG-144; FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00918: Variant p.His107Tyr