Variant position: 143 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 354 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 GNPNDPHGSEHTVSGQHFAA ELHIVHYNSDLYPDASTASNK
Mouse GNRNDPHGSEHTVSGKHFAA ELHIVHYNSDLYPDFSTASDK
Rabbit GNRNDPYGSEHTVGGKQFAA ELHIVHYNSDSYPDISTASNK
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.
Loss of carbonic anhydrase XII function in individuals with elevated sweat chloride concentration and pulmonary airway disease.
Lee M.; Vecchio-Pagan B.; Sharma N.; Waheed A.; Li X.; Raraigh K.S.; Robbins S.; Han S.T.; Franca A.L.; Pellicore M.J.; Evans T.A.; Arcara K.M.; Nguyen H.; Luan S.; Belchis D.; Hertecant J.; Zabner J.; Sly W.S.; Cutting G.R.;
Hum. Mol. Genet. 25:1923-1933(2016)
Cited for: FUNCTION; CATALYTIC ACTIVITY; TISSUE SPECIFICITY; SUBCELLULAR LOCATION; VARIANT HYCHL GLN-121; CHARACTERIZATION OF VARIANTS HYCHL GLN-121 AND LYS-143;
Hyperchlorhidrosis caused by homozygous mutation in CA12, encoding carbonic anhydrase XII.
Feldshtein M.; Elkrinawi S.; Yerushalmi B.; Marcus B.; Vullo D.; Romi H.; Ofir R.; Landau D.; Sivan S.; Supuran C.T.; Birk O.S.;
Am. J. Hum. Genet. 87:713-720(2010)
Cited for: VARIANT HYCHL LYS-143; INVOLVEMENT IN HYCHL; BIOPHYSICOCHEMICAL PROPERTIES;
Autosomal recessive hyponatremia due to isolated salt wasting in sweat associated with a mutation in the active site of carbonic cnhydrase 12.
Muhammad E.; Leventhal N.; Parvari G.; Hanukoglu A.; Hanukoglu I.; Chalifa-Caspi V.; Feinstein Y.; Weinbrand J.; Jacoby H.; Manor E.; Nagar T.; Beck J.C.; Sheffield V.C.; Hershkovitz E.; Parvari R.;
Hum. Genet. 129:397-405(2011)
Cited for: VARIANT HYCHL LYS-143;
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