UniProt functional annotation for P06870

UniProt code: P06870.

Organism: Homo sapiens (Human).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
 
Function: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
 
Catalytic activity: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl- bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|- Xaa.; EC=3.4.21.35;
Tissue specificity: Isoform 2 is expressed in pancreas, salivary glands, kidney, colon, prostate gland, testis, spleen and the colon adenocarcinoma cell line T84. {ECO:0000269|PubMed:7749372}.
Ptm: The O-linked polysaccharides on Ser-93, Ser-104 and Ser-167 are probably the mucin type linked to GalNAc. In PubMed:3163150, GalNAc was detected with the corresponding peptides but not located. {ECO:0000269|PubMed:15651049, ECO:0000269|PubMed:3163150}.
Polymorphism: Genetic variations in KLK1 are the cause of a decreased in urinary kallikrein activity [MIM:615953]. The His-77 mutation dramatically reduces the activity of the enzyme in the urine. There is a 50 to 60% reduction in urinary kallikrein activity in His-77 individuals, but renal and hormonal adaptation to dietary changes in sodium and potassium are unaffected. However, in studies of brachial artery function, His-77 individuals consistently exhibited an increase in wall shear stress and a paradoxical reduction in artery diameter and lumen compared to Arg-77 individuals. This partial genetic deficiency in kallikrein activity is associated with a form of arterial dysfunction involving inappropriate inward remodeling of the brachial artery despite a chronic increase in shear stress. {ECO:0000269|PubMed:11912256, ECO:0000269|PubMed:15765151}.
Similarity: Belongs to the peptidase S1 family. Kallikrein subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.

Annotations taken from UniProtKB at the EBI.