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Q28193 (FURIN_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Furin
EC=3.4.21.75
Alternative name(s):
Dibasic-processing enzyme
Paired basic amino acid residue-cleaving enzyme
Short name=PACE
Trans Golgi network protease furin
Gene names
Name:FURIN
Synonyms:FUR, PACE
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length797 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 vWF from their respective precursors.

Cofactor

Calcium By similarity.

Enzyme regulation

Could be inhibited by the not secondly cleaved propeptide.

Subunit structure

Interacts with FLNA. 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.

Tissue specificity

Seems to be expressed ubiquitously.

Domain

Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface.

Post-translational modification

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.

Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms By similarity.

Sequence similarities

Belongs to the peptidase S8 family. Furin subfamily.

Contains 1 homo B/P domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 10783Inhibition peptide By similarity
PRO_0000027026
Chain108 – 797690Furin
PRO_0000027027

Regions

Transmembrane719 – 74123Helical; Potential
Region762 – 7654Cell surface signal
Motif498 – 5003Cell attachment site Potential
Motif776 – 7827Trans Golgi network signal
Compositional bias556 – 708153Cys-rich
Compositional bias690 – 6989Poly-Pro

Sites

Active site1531Charge relay system By similarity
Active site1941Charge relay system By similarity
Active site3681Charge relay system By similarity
Metal binding1151Calcium 1 By similarity
Metal binding1621Calcium 1 By similarity
Metal binding2081Calcium 1 By similarity
Metal binding2581Calcium 2 By similarity
Metal binding3011Calcium 2 By similarity
Metal binding3311Calcium 2 By similarity
Site75 – 762Cleavage, second; by autolysis By similarity
Site107 – 1082Cleavage, first; by autolysis By similarity

Amino acid modifications

Modified residue7761Phosphoserine; by CK2 By similarity
Modified residue7781Phosphoserine; by CK2 By similarity
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Glycosylation5531N-linked (GlcNAc...) Potential
Disulfide bond211 ↔ 360 By similarity
Disulfide bond303 ↔ 333 By similarity
Disulfide bond450 ↔ 474 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28193 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 466F28EC0246C3D2

FASTA79787,251
        10         20         30         40         50         60 
MELRPWLFWV VAAAGALVLL VADARGEKVF TNTWAVHIPG GPAVADRVAR KHGFLNLGQI 

        70         80         90        100        110        120 
FGDYYHFWHR AVTKRSLSPH RLGHNRLQRE PQVKWLEQQV AKRRAKRDIY QEPTDPKFPQ 

       130        140        150        160        170        180 
QWYLSGVTQR DLNVKEAWAQ GYTGRGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP 

       190        200        210        220        230        240 
DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL 

       250        260        270        280        290        300 
GLNPNHIHIY SASWGPEDDG KTVDGPAHLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH 

       310        320        330        340        350        360 
DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC 

       370        380        390        400        410        420 
TESHTGTSAF APLAAGIIAL TLEANKNLTW RDMQHLVVRT SKPAHLNAND WATNGVGRKV 

       430        440        450        460        470        480 
SHSYGYGLLD AGAMVALAQN WTTVAPQRKC TIDILTEPKD IGKRLEVRKT VTACLGEPSH 

       490        500        510        520        530        540 
ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD 

       550        560        570        580        590        600 
EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPT PPESIGCKTL TSSQACVVCE 

       610        620        630        640        650        660 
EGFSLHQKNC VQHCPPGFAP QVLDTHYSTE NDVEIIRASV CTPCHASCAT CQGPAPTDCL 

       670        680        690        700        710        720 
SCPSHASLDP VEQTCSRQSQ SSRESHQQQP PPPPRPPPAE VATEPRLRAD LLPSHLPEVV 

       730        740        750        760        770        780 
AGLSCAFIVL VFVTVFLVLQ LRSGFSFRGV KVYTMDRGLI SYKGLPPEAW QEECPSDSEE 

       790 
DEGRGERTAF IKDQSAL

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References

[1]"Maturation of the trans-Golgi network protease furin: compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation."
Vey M., Schaefer W., Berghoefer S., Klenk H., Garten W.
J. Cell Biol. 127:1829-1842(1994) [PubMed: 7806563] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEOLYTIC PROCESSING.
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X75956 mRNA. Translation: CAA53569.1.
IPIIPI00685701.
PIRI46044.
RefSeqNP_776561.1. NM_174136.2.
UniGeneBt.21338.

3D structure databases

ProteinModelPortalQ28193.
SMRQ28193. Positions 110-575.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ28193.

Protein family/group databases

MEROPSS08.071.

Proteomic databases

PRIDEQ28193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281374.
KEGGbta:281374.

Organism-specific databases

CTD5045.

Phylogenomic databases

eggNOGmaNOG16185.
GeneTreeENSGT00600000084064.
HOVERGENHBG008705.
InParanoidQ28193.
OrthoDBEOG4ZW59M.
PhylomeDBQ28193.

Family and domain databases

InterProIPR006212. Furin_repeat.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt.
IPR000209. Peptidase_S8/S53.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
IPR002884. PrprotnconvertsP.
[Graphical view]
Gene3DG3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
KOK01349.
PANTHERPTHR10795. SubtilSerProt. 1 hit.
PfamPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
SMARTSM00261. FU. 2 hits.
[Graphical view]
SUPFAMSSF49785. Gal_bind_like. 1 hit.
SSF57184. Grow_fac_recept. 1 hit.
SSF52743. Pept_S8_S53. 1 hit.
SSF54897. Prot_inh_propept. 1 hit.
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. False negative.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBQ28193.

Entry information

Entry nameFURIN_BOVIN
AccessionPrimary (citable) accession number: Q28193
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 16, 2011
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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