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Reviewed, UniProtKB/Swiss-Prot P26016 (FUR11_DROME)

Last modified June 16, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Furin-like protease 1, isoforms 1/1-X/2
      Short name=Furin-1
    EC=3.4.21.75
Alternative name(s):
    Kex2-like endoprotease 1
    dKLIP-1
Gene names
Name: Fur1
ORF Names: CG10772
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity.

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

Golgi apparatus membrane; Multi-pass membrane protein. Ref.2

Tissue specificity

In adults, isoform 1-X is expressed in CNS, fat body and female reproductive tissues, and in embryos, in CNS, tracheal pits, hindgut, posterior spiracles and anal pads. Ref.2

Developmental stage

Isoforms 1-X and 2 are expressed in embryos, larvae, pupae and adults. Highest expression is in late embryos. Ref.2

Sequence similarities

Belongs to the peptidase S8 family. Furin subfamily.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay. Source: FlyBase

   Molecular functionserine-type endopeptidase activity

Inferred from direct assay. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1-X (identifier: P26016-1)

Also known as: E;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P26016-2)

Also known as: F;

The sequence of this isoform differs from the canonical sequence as follows:
     776-1152: Missing.
     1208-1208: Q → QQYPFPFQ
Isoform 2 (identifier: P26016-3)

Also known as: C; D; F;

The sequence of this isoform differs from the canonical sequence as follows:
     776-1152: Missing.
Isoform 1-CRR (identifier: P30430-1)

Also known as: A;

The sequence of this isoform can be found in the external entry P30430-1.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ? Potential
Propeptide? – 309 PotentialPRO_0000027020
Chain310 – 1269960Furin-like protease 1, isoforms 1/1-X/2
PRO_0000027021

Regions

Transmembrane119 – 13921 Potential
Transmembrane581 – 60121 Potential
Transmembrane1082 – 110221 Potential
Transmembrane1233 – 125321 Potential
Region310 – 655346Serine protease

Sites

Active site3721Charge relay system By similarity
Active site4131Charge relay system By similarity
Active site5871Charge relay system By similarity

Amino acid modifications

Glycosylation151N-linked (GlcNAc...) Potential
Glycosylation181N-linked (GlcNAc...) Potential
Glycosylation281N-linked (GlcNAc...) Potential
Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential
Glycosylation6061N-linked (GlcNAc...) Potential
Glycosylation7271N-linked (GlcNAc...) Potential
Glycosylation8141N-linked (GlcNAc...) Potential
Glycosylation8571N-linked (GlcNAc...) Potential
Glycosylation8971N-linked (GlcNAc...) Potential
Glycosylation9081N-linked (GlcNAc...) Potential
Glycosylation9941N-linked (GlcNAc...) Potential
Disulfide bond430 ↔ 579 By similarity
Disulfide bond522 ↔ 552 By similarity
Disulfide bond669 ↔ 695 By similarity

Natural variations

Alternative sequence776 – 1152377Missing in isoform 1 and isoform 2.
VSP_005424
Alternative sequence12081Q → QQYPFPFQ in isoform 1.
VSP_008042

Sequences

Sequence LengthMass (Da)Tools
Isoform 1-X (E) [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 594E641CFB024C82

FASTA1,269138,627
        10         20         30         40         50         60 
MKNDVVRWSR QPTSNTTNSS SSSRSDSNST HKHRSKSNKL NARQLGSNAA RSCQQRSSVA 

        70         80         90        100        110        120 
TTLEDEQQTI IECDIGNFNF DCNLFKTSFL TQHKQKRSGK SSSKSKSNRS RPLAKTKAVF 

       130        140        150        160        170        180 
LLALQFSAVV FLCNINVGFV AGSVATAASS AGGSSPAAPS SAPSSPPTVA VPPPPPPSSA 

       190        200        210        220        230        240 
LKVDPNGQSP VLPPYVLDYE TGGKAKLTPN NGKFGQSGSS GSNNNHIVGH YTHTWAVHIP 

       250        260        270        280        290        300 
NGDNGMADAV AKDHGFVNLG KIFDDHYHFA HHKVSKRSLS PATHHQTRLD DDDRVHWAKQ 

       310        320        330        340        350        360 
QRAKSRSKRD FIRMRPSRTS SRAMSMVDAM SFNDSKWPQM WYLNRGGGLD MNVIPAWKMG 

       370        380        390        400        410        420 
ITGKGVVVTI LDDGLESDHP DIQDNYDPKA SYDVNSHDDD PMPHYDMTDS NRHGTRCAGE 

       430        440        450        460        470        480 
VAATANNSFC AVGIAYGASV GGVRMLDGDV TDAVEARSLS LNPQHIDIYS ASWGPDDDGK 

       490        500        510        520        530        540 
TVDGPGELAS RAFIEGTTKG RGGKGSIFIW ASGNGGREQD NCNCDGYTNS IWTLSISSAT 

       550        560        570        580        590        600 
EEGHVPWYSE KCSSTLATTY SSGGQGEKQV VTTDLHHSCT VSHTGTSASA PLAAGIAALV 

       610        620        630        640        650        660 
LQSNQNLTWR DLQHIVVRTA KPANLKDPSW SRNGVGRRVS HSFGYGLMDA AEMVRVARNW 

       670        680        690        700        710        720 
KAVPEQQRCE INAPHVDKVI PPRTHITLQL TVNHCRSVNY LEHVQAKITL TSQRRGDIQL 

       730        740        750        760        770        780 
FLRSPANTSV TLLTPRIHDN SRSGFNQWPF MSVHTWGESP QGNWQLEIHN EGRYMGHALL 

       790        800        810        820        830        840 
REWSLIFYGT TQSIGPNDPI SVPKPSGSEA TTPNSSSTTS NLHQAYSPQY PRIPPNNFGS 

       850        860        870        880        890        900 
SPSGGSKLPL GKVPPPNKSS YVTNNPLLNS APPKQGYQQI SATYGVILGK ANGKSNNNSK 

       910        920        930        940        950        960 
EKTNNKGNKS NNGNKGKSGG SSGNRKEQTT QSTIIQTSTS KNKYYRISQQ QQQKNNKQDR 

       970        980        990       1000       1010       1020 
NGVQTQRPKA NSGEKSYDEK SRKVVGEITT NSGNGSIKAA KQVKESTTTS SNSRIPKLFE 

      1030       1040       1050       1060       1070       1080 
RYEKIQAIFP ELEPYENSSP KGKPKQAKQG KQFEVDLFKP TNGGNSRQGN TKKSPSVPPP 

      1090       1100       1110       1120       1130       1140 
SQTMATLSIL PILPAGGSSF LPDQKILKKQ QLLMAAAGVM APAQVEVEME EVHATPDYEA 

      1150       1160       1170       1180       1190       1200 
RKDQRKEVNG PNAQITQWDM IFYGTETPAQ PDDVANPSQS NQFNLYGNDM AHNDVEYDST 

      1210       1220       1230       1240       1250       1260 
GQWRNMQQVG EVGMTRDHSN TAACLKWSDR KCLGLSLLFF MIMQVFFLNF KHANDNNNKN 


KNNIIKCIR 

« Hide

Isoform 1 (F).

Checksum: 0D800C3495DB918C
Show »

FASTA89998,797
Isoform 2 (C) (D) (F).

Checksum: 66D5C5B288C47895
Show »

FASTA89297,889
Isoform 1-CRR (A).

See P30430.

FASTA

References

« Hide 'large scale' references
[1]"cDNA sequence of a Drosophila melanogaster gene, Dfur1, encoding a protein structurally related to the subtilisin-like proprotein processing enzyme furin."
Roebroek A.J.M., Pauli I.G.L., Zhang Y., van de Ven W.J.M.
FEBS Lett. 289:133-137(1991) [PubMed: 1915835] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Oregon-R.
Tissue: Embryo.
[2]"Generation of structural and functional diversity in furin-like proteins in Drosophila melanogaster by alternative splicing of the DFur1 gene."
Roebroek A.J.M., Creemers J.W.M., Pauli I.G.L., Bogaert T., Van de Ven W.J.M.
EMBO J. 12:1853-1870(1993) [PubMed: 8491178] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1-X AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Oregon-R and Tuebingen.
Tissue: Embryo.
[3]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: Berkeley.
Tissue: Embryo.

Cross-references

Sequence databases

X59384 mRNA. Translation: CAA42027.1.
L12370, L12369 Genomic DNA. Translation: AAA28546.1.
L12370, L12369 Genomic DNA. Translation: AAA28547.1.
L12375 mRNA. Translation: AAA28550.1.
L12376 mRNA. Translation: AAA28549.1.
AE014297 Genomic DNA. Translation: AAF56463.2.
AE014297 Genomic DNA. Translation: AAF56464.1.
AE014297 Genomic DNA. Translation: AAN14052.1.
AE014297 Genomic DNA. Translation: AAS65215.1.
AE014297 Genomic DNA. Translation: AAS65216.1.
AY069590 mRNA. Translation: AAL39735.1.
PIRS17546.
S35366.
RefSeqNP_524885.1.
NP_733103.1.
NP_733104.1.
NP_996293.1.
NP_996294.1.
UniGeneDm.1740

3D structure databases

HSSPHSSP built from PDB template 1P8J based on UniProtKB P23188.
ModBaseSearch...

Genome annotation databases

EnsemblFBgn0004509. Drosophila melanogaster. [Contig view]
GeneID47220.
KEGGdme:Dmel_CG10772.
NMPDRfig|7227.3.peg.14665.

Organism-specific databases

FlyBaseFBgn0004509. Fur1.

Phylogenomic databases

HOGENOMP26016.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-013402-MON.
BRENDA3.4.21.75. 48.

Gene expression databases

ArrayExpressP26016.
GermOnlineCG10772. Drosophila melanogaster.

Family and domain databases

InterProIPR000209. Pept_S8_S53.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
[Graphical view]
Gene3DG3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
PANTHERPTHR10795. SubtilSerProt. 1 hit.
PfamPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
ProDomPD000717. PrprotnconvertsP. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio838963.

Entry information

Entry nameFUR11_DROME
AccessionPrimary (citable) accession number: P26016
Secondary accession number(s): A4V3E2, Q05817, Q27436
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents