|
|
|
|
|
|
|
|
|
- FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
- CATALYTIC ACTIVITY: Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
- SUBCELLULAR LOCATION: Secreted.
- DEVELOPMENTAL STAGE: Pepsinogens in group I, II, and III where the predominant zymogens at late postnatal stage.
- SIMILARITY: Belongs to the peptidase A1 family [view classification].
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 387 AA [This is the length of the unprocessed precursor] |
Molecular weight: 42071 Da [This is the MW of the unprocessed precursor] |
CRC64: A6EC48F715541A48 [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MKWLLLLGLL ALSECIVHKV PLVRKKSLRK NLIEKGLLQD YLKTHTPNLA TKYFPKETFA
70 80 90 100 110 120
SVSTESLENY LDAEYFGTIS IGTPPQEFTV IFDTGSSNLW VPSTYCSSLA CFLHKRFNPD
130 140 150 160 170 180
DSSTFQATSE TLSITYGTGS MTGILGYDTV KVGNIEDTNQ IFGLSKTEPG ITFLVAPFDG
190 200 210 220 230 240
ILGLAYPSIS ASDATPVFDN MWNEGLVSED LFSVYLSSNG EKGSMVMFGG IDSSYYTGSL
250 260 270 280 290 300
NWVPVSHEGY WQITMDSITI NGETIACADS CQAVVDTGTS LLAGPTSAIS KIQSYIGASK
310 320 330 340 350 360
NLLGENIISC SAIDSLPDIV FTINNVQYPL PASAYILKED DDCLSGFDGM NLDTSYGELW
370 380
ILGDVFIRQY FTVFDRANNQ VGLAAAA
|
P28712 in FASTA format |
|
ExPASy Home page
SIB Switzerland
