P29119 (FURI1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Furin-1
EC=3.4.21.75

Alternative name(s):
Dibasic-processing enzyme
Paired basic amino acid residue-cleaving enzyme
Short name=PACE

Gene names

Name:

furin

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	783 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Tissue specificity	In all tissues analyzed.
Sequence similarities	Belongs to the peptidase S8 family. Furin subfamily.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Propeptide	25 – 105	81	Potential		PRO_0000027034
	Chain	106 – 783	678	Furin-1		PRO_0000027035
Regions
	Transmembrane	702 – 725	24	Helical; Potential
	Region	118 – 418	301	Catalytic
Sites
	Active site	151	1	Charge relay system By similarity
	Active site	192	1	Charge relay system By similarity
	Active site	366	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	385	1	N-linked (GlcNAc...) Potential
	Glycosylation	551	1	N-linked (GlcNAc...) Potential
	Disulfide bond	209 ↔ 358		By similarity
	Disulfide bond	301 ↔ 331		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29119 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 02476FD3247AF2C7	FASTA	783	86,444
	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

References

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	M80471 mRNA. Translation: AAA49717.1.
PIR	A41627. B41627.
UniGene	Xl.788.
3D structure databases
ProteinModelPortal	P29119.
SMR	P29119. Positions 108-572.
ModBase	Search...
Protein family/group databases
MEROPS	S08.071.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG008705.
Family and domain databases
InterPro	IPR006212. Furin_repeat. IPR008979. Galactose-bd-like. IPR009030. Growth_fac_rcpt. IPR000209. Peptidase_S8/S53. IPR023827. Peptidase_S8_Asp-AS. IPR022398. Peptidase_S8_His-AS. IPR023828. Peptidase_S8_Ser-AS. IPR015500. Peptidase_S8_subtilisin-rel. IPR009020. Prot_inh_propept. IPR002884. PrprotnconvertsP. [Graphical view]
Gene3D	G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
PANTHER	PTHR10795. SubtilSerProt. 1 hit.
Pfam	PF01483. P_proprotein. 1 hit. PF00082. Peptidase_S8. 1 hit. [Graphical view]
PRINTS	PR00723. SUBTILISIN.
SMART	SM00261. FU. 2 hits. [Graphical view]
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF57184. Grow_fac_recept. 1 hit. SSF52743. Pept_S8_S53. 1 hit. SSF54897. Prot_inh_propept. 1 hit.
PROSITE	PS00136. SUBTILASE_ASP. 1 hit. PS00137. SUBTILASE_HIS. 1 hit. PS00138. SUBTILASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FURI1_XENLA

Accession

Primary (citable) accession number: P29119

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	November 16, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program