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UniProtKB/Swiss-Prot entry P26016


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FUR11_DROME
Primary accession number P26016
Secondary accession numbers A4V3E2 Q05817 Q27436
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on June 1, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 97)
Name and origin of the protein
Protein name Furin-like protease 1, isoforms 1/1-X/2 [Precursor]
Synonyms Furin-1
EC 3.4.21.75
Kex2-like endoprotease 1
dKLIP-1
Gene name
Name: Fur1
ORFNames: CG10772
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Oregon-R;
TISSUE=Embryo;
DOI=10.1016/0014-5793(91)81052-A; PubMed=1915835 [NCBI, ExPASy, EBI, Israel, Japan]
Roebroek A.J.M., Pauli I.G.L., Zhang Y., van de Ven W.J.M.;
"cDNA sequence of a Drosophila melanogaster gene, Dfur1, encoding a protein structurally related to the subtilisin-like proprotein processing enzyme furin.";
FEBS Lett. 289:133-137(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1-X AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Oregon-R, and Tuebingen;
TISSUE=Embryo;
PubMed=8491178 [NCBI, ExPASy, EBI, Israel, Japan]
Roebroek A.J.M., Creemers J.W.M., Pauli I.G.L., Bogaert T., Van de Ven W.J.M.;
"Generation of structural and functional diversity in furin-like proteins in Drosophila melanogaster by alternative splicing of the DFur1 gene.";
EMBO J. 12:1853-1870(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 von Willebrand factor from their respective precursors.
  • SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein.
  • ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.
    Name1-X
    SynonymsE
    Isoform IDP26016-1
    This is the isoform sequence displayed in this entry.
    Name1
    SynonymsF
    Isoform IDP26016-2
    Features which should be applied to build the isoform sequence: VSP_005424, VSP_008042.
    Name2
    SynonymsC, D, F
    Isoform IDP26016-3
    Features which should be applied to build the isoform sequence: VSP_005424.
    Name1-CRR
    SynonymsA
    Isoform IDP30430-1
    This isoform is stored in UniProtKB/Swiss-Prot entry P30430.
  • 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.
  • DEVELOPMENTAL STAGE: Isoforms 1-X and 2 are expressed in embryos, larvae, pupae and adults. Highest expression is in late embryos.
  • 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
X59384; CAA42027.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12370; AAA28546.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12369; AAA28546.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12370; AAA28547.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12369; AAA28547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12375; AAA28550.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12376; AAA28549.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF56463.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF56464.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAN14052.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAS65215.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAS65216.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY069590; AAL39735.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S17546; S17546.
S35366; S35366.
RefSeq NP_524885.1; -.
NP_733103.1; -.
NP_733104.1; -.
NP_996293.1; -.
NP_996294.1; -.
UniGene Dm.1740
3D structure databases
HSSP P23188; 1P8J. [HSSP ENTRY / PDB]
ModBase P26016.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-013402-MON; -.
Organism-specific databases
FlyBase FBgn0004509; Fur1.
Gene expression databases
ArrayExpress P26016; -.
GermOnline CG10772; Drosophila melanogaster.
Ontologies
GO
GO:0000139; Cellular component: Golgi membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from FlyBase).
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 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]
PROSITE PS00136; SUBTILASE_ASP; 1.
PS00137; SUBTILASE_HIS; 1.
PS00138; SUBTILASE_SER; 1.
BLOCKS P26016.
ProtoNet P26016.
Genome annotation databases
Ensembl CG10772; Drosophila melanogaster. [Contig view]
GeneID 47220; -.
KEGG dme:Dmel_CG10772; -.
NMPDR fig|7227.3.peg.14665; -.
Phylogenomic databases
HOGENOM P26016; -.
Other
NextBio 838963; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cleavage on pair of basic residues; Complete proteome; Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Protease; Serine protease; Signal; Transmembrane; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1      ?        Potential. 
PROPEP   ?    309        Potential. PRO_0000027020
CHAIN   310   1269  960     Furin-like protease 1, isoforms 1/1-X/2. PRO_0000027021
TRANSMEM   119    139  21     Potential. 
TRANSMEM   581    601  21     Potential. 
TRANSMEM   1082   1102  21     Potential. 
TRANSMEM   1233   1253  21     Potential. 
REGION   310    655  346     Serine protease. 
ACT_SITE   372    372        Charge relay system (By similarity). 
ACT_SITE   413    413        Charge relay system (By similarity). 
ACT_SITE   587    587        Charge relay system (By similarity). 
CARBOHYD   15     15        N-linked (GlcNAc...) (Potential). 
CARBOHYD   18     18        N-linked (GlcNAc...) (Potential). 
CARBOHYD   28     28        N-linked (GlcNAc...) (Potential). 
CARBOHYD   108    108        N-linked (GlcNAc...) (Potential). 
CARBOHYD   333    333        N-linked (GlcNAc...) (Potential). 
CARBOHYD   426    426        N-linked (GlcNAc...) (Potential). 
CARBOHYD   606    606        N-linked (GlcNAc...) (Potential). 
CARBOHYD   727    727        N-linked (GlcNAc...) (Potential). 
CARBOHYD   814    814        N-linked (GlcNAc...) (Potential). 
CARBOHYD   857    857        N-linked (GlcNAc...) (Potential). 
CARBOHYD   897    897        N-linked (GlcNAc...) (Potential). 
CARBOHYD   908    908        N-linked (GlcNAc...) (Potential). 
CARBOHYD   994    994        N-linked (GlcNAc...) (Potential). 
DISULFID   430    579        By similarity. 
DISULFID   522    552        By similarity. 
DISULFID   669    695        By similarity. 
VAR_SEQ   776   1152        Missing (in isoform 1 and isoform 2). VSP_005424
VAR_SEQ   1208   1208        Q -> QQYPFPFQ (in isoform 1). VSP_008042
Sequence information
Length: 1269 AA [This is the length of the unprocessed precursor] Molecular weight: 138627 Da [This is the MW of the unprocessed precursor] CRC64: 594E641CFB024C82 [This is a checksum on the sequence]
        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 

P26016 in FASTA format

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View entry in raw text format (no links)
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