[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1722329 [NCBI, ExPASy, EBI, Israel, Japan] Korner J., Chun J., O'Bryan L., Axel R.; "Prohormone processing in Xenopus oocytes: characterization of cleavage signals and cleavage enzymes."; Proc. Natl. Acad. Sci. U.S.A. 88:11393-11397(1991).

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 von Willebrand factor from their respective precursors.
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential).
TISSUE SPECIFICITY: In all tissues analyzed.
SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M80471; AAA49717.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A41627; A41627.
B41627; B41627.

UniGene

Xl.788

3D structure databases

HSSP

P23188; 1P8J. [HSSP ENTRY / PDB]

SMR

P29119; 107-576.

ModBase

P29119.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006212; Furin_repeat.
IPR000209; Pept_S8_S53.
IPR015500; Peptidase_S8_subtilisin-rel.
IPR002884; PrprotnconvertsP.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.200; Pept_S8_S53; 1.

PANTHER

PTHR10795; SubtilSerProt; 1.

Pfam

PF01483; P_proprotein; 1.
PF00082; Peptidase_S8; 1.
Pfam graphical view of domain structure.

PRINTS

PR00723; SUBTILISIN.

ProDom

PD000717; PrprotnconvertsP; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00261; FU; 2.
SMART graphical view of domain structure.

PROSITE

PS00136; SUBTILASE_ASP; 1.
PS00137; SUBTILASE_HIS; 1.
PS00138; SUBTILASE_SER; 1.

Phylogenomic databases

HOVERGEN

P29119; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cleavage on pair of basic residues; Glycoprotein; Hydrolase; Membrane; Protease; Serine protease; Signal; Transmembrane; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`	`Potential.`
`PROPEP`	`25 105`	`81`	`Potential.`	`PRO_0000027034`
`CHAIN`	`106 783`	`678`	`Furin-1.`	`PRO_0000027035`
`TRANSMEM`	`702 725`	`24`	`Potential.`
`REGION`	`118 418`	`301`	`Catalytic.`
`ACT_SITE`	`151 151`		`Charge relay system (By similarity).`
`ACT_SITE`	`192 192`		`Charge relay system (By similarity).`
`ACT_SITE`	`366 366`		`Charge relay system (By similarity).`
`CARBOHYD`	`385 385`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`551 551`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`209 358`		`By similarity.`
`DISULFID`	`301 331`		`By similarity.`

Sequence information

Length: 783 AA [This is the length of the unprocessed precursor]

Molecular weight: 86444 Da [This is the MW of the unprocessed precursor]

CRC64: 02476FD3247AF2C7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDLSPSLLLM LWTLLSVLVE EITGQKVYTN TWAAHISGGS AEADRLCKKY GFINHGLIFE 

        70         80         90        100        110        120 
DHYHFSHRAV MKRSLTPKRT RQVLLKREPQ VHWLEQQVAK KRKKRDIYTD PTDPKFMQQW 

       130        140        150        160        170        180 
YLLDTNRHDL HVKEAWEQGF TGKGIVVSIL DDGIEKNHPD LQANYDPAAS YDVNDQDPDP 

       190        200        210        220        230        240 
QPRYTQLNDN RHGTRCAGEV AAVANNGICG VGIAYNANIG GVRMLDGEVT DAVEARSLGL 

       250        260        270        280        290        300 
NPNHIHIYSA SWGPEDDGKT VDGPAKLAEE AFYRGVTQGR GGLGSIYVWA SGNGGREHDS 

       310        320        330        340        350        360 
CNCDGYTNSI YTLSISSTTQ MGNVPWYSEA CSSTLATTYS SGNQNEKQIV TTDLRQKCTD 

       370        380        390        400        410        420 
SHTGTSASAP LAAGIIALAL EANKNLTWRD MQHLVVQTSN PAGLNANDWI TNGVGRKVSH 

       430        440        450        460        470        480 
SYGYGLLDAG AMVAMAKTWV TVGPQRKYVI DILSEPKDIG KALEVRRKVE PCAGMSNYIS 

       490        500        510        520        530        540 
TLEHVQARLS LSYNCRGDLA IYLTSPMGTR SCLLAPRPHD YSADGFNDWS FMTTHSWDED 

       550        560        570        580        590        600 
PAGEWVLEIE NVSNNNNYGT LTQFVLVLYG TASEGLSRKF DGDGSRNVAS SQSCIVCEEG 

       610        620        630        640        650        660 
YFLHQKSCIK SCPQGFTSSI QNIHYTLDNN IEPLLVNVCV PCHVSCATCK GTTINDCLTC 

       670        680        690        700        710        720 
PAHSHYNLLD YSCTHQTQRS RESPTLKDSS HDYVARTSNL PFIVAILSCL FIIVVFGSIF 

       730        740        750        760        770        780 
LFLQLRSGGV LGRKRLYMLD SGIISYKGIP SGAWQEEGFS ESETEETAAH SERTAFLKQQ 


STL

P29119 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools