|
|
|
|
|
|
[1]
|
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2266110 [NCBI, ExPASy, EBI, Israel, Japan]
Hatsuzawa K.,
Hosaka M.,
Nakagawa T.,
Nagase M.,
Shoda A.,
Murakami K.,
Nakayama K.;
"Structure and expression of mouse furin, a yeast Kex2-related protease. Lack of processing of coexpressed prorenin in GH4C1 cells.";
J. Biol. Chem. 265:22075-22078(1990).
|
[2]
|
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Creemers J.W.M.,
Roebroek A.J.M.,
van den Ouweland A.M.W.,
van Duijnhoven H.L.P.,
van de Ven W.J.M.;
"Cloning and functional expression of a 4.3 kbp mouse fur cDNA: evidence for differential expression.";
Life Sci. Adv. (Mol. Biol.) 11:127-138(1992).
|
[3]
|
INTERACTION WITH FLNA.
DOI=10.1083/jcb.139.7.1719; PubMed=9412467 [NCBI, ExPASy, EBI, Israel, Japan]
Liu G.,
Thomas L.,
Warren R.A.,
Enns C.A.,
Cunningham C.C.,
Hartwig J.H.,
Thomas G.;
"Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway.";
J. Cell Biol. 139:1719-1733(1997).
|
[4]
|
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 108-578 IN COMPLEX WITH INHIBITOR.
DOI=10.1038/nsb941; PubMed=12794637 [NCBI, ExPASy, EBI, Israel, Japan]
Henrich S.,
Cameron A.,
Bourenkov G.P.,
Kiefersauer R.,
Huber R.,
Lindberg I.,
Bode W.,
Than M.E.;
"The crystal structure of the proprotein processing proteinase furin explains its stringent specificity.";
Nat. Struct. Biol. 10:520-526(2003).
|
|
|
|
- FUNCTION: Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.
- CATALYTIC ACTIVITY: Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.
- COFACTOR: Binds 2 calcium ions per subunit.
- ENZYME REGULATION: Could be inhibited by the not secondly cleaved propeptide.
- SUBUNIT: Interacts with FLNA (By similarity). Binds to PACS1 which mediates TGN localization and connection to clathrin adapters (By similarity).
- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein. Note=Shuttles between the trans-Golgi network and the cell surface. Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin (By similarity).
- TISSUE SPECIFICITY: Seems to be expressed ubiquitously.
- DOMAIN: Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface.
- PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and furin activation (By similarity).
- PTM: Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms (By similarity).
- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily [view classification].
- SIMILARITY: Contains 1 homo B/P domain.
|
|
|
|
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Length: 793 AA [This is the length of the unprocessed precursor] |
Molecular weight: 86804 Da [This is the MW of the unprocessed precursor] |
CRC64: 5F121C3DE2E1A42D [This is a checksum on the sequence] |
|
10 20 30 40 50 60
MELRSWLLWV VAAAGAVVLL AADAQGQKIF TNTWAVHIPG GPAVADRVAQ KHGFHNLGQI
70 80 90 100 110 120
FGDYYHFWHR AVTKRSLSPH RPRHSRLQRE PQVKWLEQQV AKRRAKRDVY QEPTDPKFPQ
130 140 150 160 170 180
QWYLSGVTQR DLNVKEAWAQ GFTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP
190 200 210 220 230 240
DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL
250 260 270 280 290 300
GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH
310 320 330 340 350 360
DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC
370 380 390 400 410 420
TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNADD WATNGVGRKV
430 440 450 460 470 480
SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IVEILVEPKD IGKRLEVRKA VTACLGEPNH
490 500 510 520 530 540
ITRLEHVQAR LTLSYNRRGD LAIHLISPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD
550 560 570 580 590 600
EDPAGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLST PPESSGCKTL TSSQACVVCE
610 620 630 640 650 660
EGYSLHQKSC VQHCPPGFIP QVLDTHYSTE NDVEIIRASV CTPCHASCAT CQGPAPTDCL
670 680 690 700 710 720
SCPSHASLDP VEQTCSRQSQ SSRESRPQQQ PPALRPEVEM EPRLQAGLAS HLPEVLAGLS
730 740 750 760 770 780
CLIIVLIFGI VFLFLHRCSG FSFRGMKVYT MDRGLISYKG LPPEAWQEEC PSDSEEDEGR
790
GERTAFIKDQ SAL
|
P23188 in FASTA format |
|
ExPASy Home page
CBR Canada
