Variant position: 92 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 260 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human DSQDKAVLK--GGP-LDGTYRLI QFHFHWGSLD--GQGSEHTVDKK
Mouse DSQDNAVLK--GGP-LSDSYRLI QFHFHWGSSD--GQGSEH
Rat DSQDFAVLK--EGP-LSGSYRLI QFHFHWGSSD--GQGSEH
Bovine DSQDKAVLK--DGP-LTGTYRLV QFHFHWGSSD--DQGSEH
Rabbit DSHDKTVLK--EGP-LEGTYRLI QFHFHWGSSD--GQGSEH
Sheep DSQDKAVLK--DGP-LTGTYRLV QFHFHWGSSD--DQGSEH
Chicken DSSDKSVLQ--GGA-LDGVYRLV QFHIHWGSCE--GQGSEH
Caenorhabditis elegans DLPNRPTINITGGPTMPYRYKLH QISVHFGRADEGEKGSEH
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
2 – 260 Carbonic anhydrase 2
3 – 259 Alpha-carbonic anhydrase
94 – 94 Zinc; catalytic
96 – 96 Zinc; catalytic
92 – 92 Activator
94 – 94 H -> CDENQ. Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding.
106 – 106 E -> AQ. Strongly reduced CO(2) hydrase activity.
106 – 106 E -> D. Normal CO(2) hydrase activity.
88 – 97
Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis.
Hu P.Y.; Lim E.J.; Ciccolella J.; Strisciuglio P.; Sly W.S.;
Hum. Mutat. 9:383-387(1997)
Cited for: VARIANT OPTB3 PRO-92;
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; CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144;
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.