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UniProtKB/Swiss-Prot entry P30430


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

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Entry information
Entry name FUR1C_DROME
Primary accession number P30430
Secondary accession numbers Q27235 Q9VBR5
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on June 1, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 92)
Name and origin of the protein
Protein name Furin-like protease 1, isoform 1-CRR [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].
STRAIN=Oregon-R;
TISSUE=Head;
PubMed=1545235 [NCBI, ExPASy, EBI, Israel, Japan]
Hayflick J.S., Wolfgang W.J., Forte M.A., Thomas G.;
"A unique Kex2-like endoprotease from Drosophila melanogaster is expressed in the central nervous system during early embryogenesis.";
J. Neurosci. 12:705-717(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, 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).
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-CRR
    SynonymsA
    Isoform IDP30430-1
    This is the isoform sequence displayed in this entry.
    Name1
    SynonymsF
    Isoform IDP26016-2
    This isoform is stored in UniProtKB/Swiss-Prot entry P26016.
    Name1-X
    SynonymsE
    Isoform IDP26016-1
    This isoform is stored in UniProtKB/Swiss-Prot entry P26016.
    Name2
    SynonymsC, D, F
    Isoform IDP26016-3
    This isoform is stored in UniProtKB/Swiss-Prot entry P26016.
  • TISSUE SPECIFICITY: In adults, P26016-2'>isoform 1-CRR is expressed in CNS, fat body, and female reproductive tissues, and in embryos, in anal pads, hindgut, developing antennomaxillary complex, oenocytes, clipeolabrum, pharynx, trachea, CNS and developing posterior spiracles.
  • DEVELOPMENTAL STAGE: P26016-2'>Isoform 1-CRR is expressed in embryos, larvae, pupae and adults.
  • 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
M81431; AAA28467.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12370; AAA28545.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12369; AAA28545.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L12372; AAA28548.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAN14051.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_733102.1; -.
UniGene Dm.1740
3D structure databases
HSSP P23188; 1P8J. [HSSP ENTRY / PDB]
ModBase P30430.
Protein family/group databases
MEROPS S08.048; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-013401-MON; -.
Organism-specific databases
FlyBase FBgn0004509; Fur1.
Gene expression databases
ArrayExpress P30430; -.
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 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.
BLOCKS P30430.
ProtoNet P30430.
Genome annotation databases
Ensembl CG10772; Drosophila melanogaster. [Contig view]
GeneID 47220; -.
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_0000027022
CHAIN   310   1101  792     Furin-like protease 1, isoform 1-CRR. PRO_0000027023
TRANSMEM   119    139  21     Potential. 
TRANSMEM   1014   1034  21     Potential. 
REGION   310    655  346     Catalytic. 
COMPBIAS   847    982  136     Cys-rich. 
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   859    859        N-linked (GlcNAc...) (Potential). 
CARBOHYD   978    978        N-linked (GlcNAc...) (Potential). 
DISULFID   430    579        By similarity. 
DISULFID   522    552        By similarity. 
DISULFID   669    695        By similarity. 
CONFLICT   1014   1014        T -> I (in Ref. 1; AAA28467). 
Sequence information
Length: 1101 AA [This is the length of the unprocessed precursor] Molecular weight: 120993 Da [This is the MW of the unprocessed precursor] CRC64: 90DC38E2CACB71A0 [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 EGRYMAQITQ 

       790        800        810        820        830        840 
WDMIFYGTET PAQPDDVANP SQSNQFNLYG NDMAHNDVEY DSTGQWRNMQ QVGEVGMTRD 

       850        860        870        880        890        900 
HSNTAACLKW SDRKCLECND SAYMFEDQCY DVCPVHTYPL DKFQAEEDEQ DDEVTRGPVN 

       910        920        930        940        950        960 
PYSSSPMDHS LLMSNSLDDK QDPLQAEDRR RRSSLTQLVE VPSRVCAACD RSCLECYGAL 

       970        980        990       1000       1010       1020 
ASQCSTCSPG SQLRKILNET FCYAYVVRST GMASVVDISK MDDRDTQQYM TGTTVLLLVS 

      1030       1040       1050       1060       1070       1080 
VIFTLMGVAV AGGIVYHRRA MARSNELYSR VSLVPGDESD SDEDELFTAH FPARKSGVNI 

      1090       1100 
YRDEAPSEKI FEEDEISHLV P 

P30430 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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