8.A.11.1.4
FKBP8 of 412 aas and TMSs. It is a constitutively inactive PPiase, which becomes active when bound to
calmodulin and calcium. It seems to act as a chaperone for BCL2, targets it
to the mitochondria and modulates its phosphorylation state. The
BCL2/FKBP8/calmodulin/calcium complex probably interferes with the
binding of BCL2 to its targets. The active form of FKBP8 may therefore
play a role in the regulation of apoptosis. It may be involved in the inhibition
of viral infection by influenza A viruses (IAV) (Wang et al. 2017).
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| Accession Number: | Q14318 |
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| Protein Name: | Peptidyl-prolyl cis-trans isomerase FKBP8 |
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| Length: | 412 |
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| Molecular Weight: | 44562.00 |
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| Species: | Homo sapiens (Human) [9606] |
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| Number of TMSs: | 1 |
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| Location1 / Topology2 / Orientation3: |
Mitochondrion membrane1 / Single-pass membrane protein2 / Cytoplasmic side3 |
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| Substrate |
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1: MASCAEPSEP SAPLPAGVPP LEDFEVLDGV EDAEGEEEEE EEEEEEDDLS ELPPLEDMGQ
61: PPAEEAEQPG ALAREFLAAM EPEPAPAPAP EEWLDILGNG LLRKKTLVPG PPGSSRPVKG
121: QVVTVHLQTS LENGTRVQEE PELVFTLGDC DVIQALDLSV PLMDVGETAM VTADSKYCYG
181: PQGRSPYIPP HAALCLEVTL KTAVDGPDLE MLTGQERVAL ANRKRECGNA HYQRADFVLA
241: ANSYDLAIKA ITSSAKVDMT FEEEAQLLQL KVKCLNNLAA SQLKLDHYRA ALRSCSLVLE
301: HQPDNIKALF RKGKVLAQQG EYSEAIPILR AALKLEPSNK TIHAELSKLV KKHAAQRSTE
361: TALYRKMLGN PSRLPAKCPG KGAWSIPWKW LFGATAVALG GVALSVVIAA RN