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- 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.
- PTM: Each pepsinogen is converted to corresponding pepsin at pH 2.0 in part as a result of the release of a 47 AA activation segment and in part as a result of stepwise proteolytic cleavage via an intermediate form(s).
- MISCELLANEOUS: The expression of pepsinogen genes is regulated by hormones and related substances.
- SIMILARITY: Belongs to the peptidase A1 family [view classification].
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 388 AA [This is the length of the unprocessed precursor] |
Molecular weight: 41955 Da [This is the MW of the unprocessed precursor] |
CRC64: A2923AB1F7FCDEB9 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MKWLLLLGLV ALSECIIYKV PLVRKKSLRR NLSEHGLLKD FLKKHNLNPA SKYFPQAEAP
70 80 90 100 110 120
TLIDEQPLEN YLDVEYFGTI GIGTPAQNFT VVFDTGSSNL WVPSVYCYSL ACMDHNLFNP
130 140 150 160 170 180
QDSSTYRATS KTVSITYGTG SMTGILGYDT VKVGGISDTN QIFGLSETEP GFFLYFAPFD
190 200 210 220 230 240
GILGLAYPSI SSSGATPVFD NIWNQRLVSQ DLFSVYLSAD DQSGSVVIFG GIDSSYYTGS
250 260 270 280 290 300
LNWVPVSVEG YWQISVDSIT MNGKTIACAK GCQAIVDTGT SLLTGPTSPI ANIQSDIGAS
310 320 330 340 350 360
ENSDGEMVVS CSAISSLPDI VFTINGVQYP LPPSAYILQS QGSCTSGFQG MDVPTESGEL
370 380
WILGDVFIRQ YFTVFDRANN QVGLAPVA
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P27678 in FASTA format |
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