Table 3.
Comparison of the aa sequence of NH2- and COOH-terminal domains in human PAG-L/pep polypeptide precursor to various aspartic proteinases.
| Gene Name a | NH2-Domain b | Identity (%) | COOH-Domain b | Identity (%) |
|---|---|---|---|---|
| hPAG-L/pep. | VVFDTGSSNLWV | this study | AIVDTGTSLLTG | this study |
| hPepsinogen A | ............. | 100 | ............ | 100 |
| hCathepsin D | ............ | 100 | .........MV. | 83.3 |
| hPepsinogen C | .L.......... | 91.7 | ...........V | 91.7 |
| hCathepsin E | .I.......... | 91.7 | .........I.. | 91.7 |
| CfPAG-L | .L.......... | 91.7 | G..........V | 83.3 |
| TrNothepsin | ........D... | 91.7 | .........IA. | 83.3 |
| hNapsin A | .A.......... | 91.7 | ..L......I.. | 83.3 |
| pPAG2, 4, 6, 10 | ........D... | 91.7 | ........MLH. | 75 |
| oPAG2 | ........D... | 91.7 | .L.......IH. | 75 |
| bPAG2 | .......A.... | 91.7 | .LL.....MIY. | 58.3 |
| hRenin A | .........V.. | 91.7 | .L....A.YIS. | 58.3 |
| mPepsinogen F | ..L.....V... | 83.3 | G.M......... | 83.3 |
| fPAG | .I......D... | 83.3 | ..I.......I. | 83.3 |
| ePAG | .I.....AD... | 75 | ..........L. | 91.7 |
| zPAG | .I.....AD... | 75 | ..........L. | 91.7 |
| pPAG1, 3, 5 | .I...A..D... | 75 | ..L.S.SAF.L. | 50 |
a aa—Amino acids, b—bovine, e—equine, f—feline, h—human, m—mouse, o—ovine, p—porcine, z—zebra, Tr—pufferfish, Cf—beaver; b Identical aa are dotted and aspartic acid (D) located within domain creating the substrate binding cleft is underlined.