P30432 (FUR2_DROME) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 120.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Furin-like protease 2 Short name=Furin-2 EC=3.4.21.75 | ||||
| Gene names |
| ||||
| Organism | Drosophila melanogaster (Fruit fly) | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora |
Protein attributes
| Sequence length | 1679 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 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 | Membrane; Single-pass membrane protein Potential. |
| Tissue specificity | Transient expression in a subset of central nervous system neurons during embryonic stages 12-13. Expression in developing tracheal tree from stage 13 to end of embryonic development. |
| Developmental stage | Expressed both maternally and zygotically. |
| Sequence similarities | Belongs to the peptidase S8 family. Furin subfamily. |
| Sequence caution | The sequence AAL48024.1 differs from that shown. Reason: Erroneous initiation. The sequence AAX33562.1 differs from that shown. Reason: Intron retention. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat Signal Transmembrane Transmembrane helix |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor protein tyrosine kinase signaling pathwayInferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activityInferred from direct assay Ref.1. Source: FlyBase transmembrane receptor protein tyrosine kinase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform D (identifier: P30432-1) Also known as: E; F; G; 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 A (identifier: P30432-2) Also known as: B; C; The sequence of this isoform differs from the canonical sequence as follows: 386-386: L → LVSK | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – ? | Potential | |||||||||
| Propeptide | ? – 318 | Potential | PRO_0000027024 | ||||||||
| Chain | 319 – 1679 | 1361 | Furin-like protease 2 | PRO_0000027025 | |||||||
Regions | |||||||||||
| Transmembrane | 1512 – 1532 | 21 | Helical; Potential | ||||||||
| Topological domain | 1533 – 1679 | 147 | Cytoplasmic Potential | ||||||||
| Repeat | 961 – 1006 | 46 | 1 | ||||||||
| Repeat | 1007 – 1056 | 50 | 2 | ||||||||
| Repeat | 1057 – 1103 | 47 | 3 | ||||||||
| Repeat | 1104 – 1152 | 49 | 4 | ||||||||
| Repeat | 1153 – 1204 | 52 | 5 | ||||||||
| Repeat | 1205 – 1253 | 49 | 6 | ||||||||
| Repeat | 1254 – 1298 | 45 | 7 | ||||||||
| Repeat | 1299 – 1345 | 47 | 8 | ||||||||
| Repeat | 1346 – 1392 | 47 | 9 | ||||||||
| Repeat | 1393 – 1443 | 51 | 10 | ||||||||
| Region | 961 – 1443 | 483 | 10 X tandem repeats, Cys-rich | ||||||||
Sites | |||||||||||
| Active site | 417 | 1 | Charge relay system By similarity | ||||||||
| Active site | 456 | 1 | Charge relay system By similarity | ||||||||
| Active site | 637 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 3 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 109 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 130 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 205 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 442 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 480 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 927 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1060 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1181 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1274 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1277 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1439 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 473 ↔ 629 | By similarity | |||||||||
| Disulfide bond | 565 ↔ 595 | By similarity | |||||||||
| Disulfide bond | 720 ↔ 748 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 386 | 1 | L → LVSK in isoform A. | VSP_009365 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 152 – 153 | 2 | Missing in AAA28551. Ref.1 | ||||||||
| Sequence conflict | 177 | 1 | V → F in AAA28551. Ref.1 | ||||||||
| Sequence conflict | 213 | 1 | V → VDQL in AAA28551. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and functional expression of Dfurin2, a subtilisin-like proprotein processing enzyme of Drosophila melanogaster with multiple repeats of a cysteine motif." Roebroek A.J.M., Creemers J.W.M., Pauli I.G.L., Kurzik-Dumke U., Rentrop M., Gateff E.A.F., Leunissen J.A.M., van de Ven W.J.M. J. Biol. Chem. 267:17208-17215(1992) [PubMed: 1512259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D). Strain: Iso-1, Oregon-R and Tuebingen. Tissue: Embryo. |
| [2] | "The Dfur2 gene of Drosophila melanogaster: genetic organization, expression during embryogenesis, and pro-protein processing activity of its translational product Dfurin2." Roebroek A.J.M., Ayoubi T.A.Y., Creemers J.W.M., Pauli I.G.L., van de Ven W.J.M. DNA Cell Biol. 14:223-234(1995) [PubMed: 7880443] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Iso-1. |
| [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. 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. Lewis S.E.Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley. |
| [5] | Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D). Strain: Berkeley. Tissue: Embryo. |
| [6] | "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] OF 305-1679 (ISOFORM A). Strain: Berkeley. Tissue: Embryo. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M94375 mRNA. Translation: AAA28551.1. L33831 Genomic DNA. Translation: AAA69860.1. AE014298 Genomic DNA. Translation: AAF48598.2. AE014298 Genomic DNA. Translation: AAF48599.2. AE014298 Genomic DNA. Translation: AAN09399.1. AE014298 Genomic DNA. Translation: AAN09400.1. AE014298 Genomic DNA. Translation: AAN09401.1. AE014298 Genomic DNA. Translation: AAN09402.1. AE014298 Genomic DNA. Translation: AAS65387.1. BT021414 mRNA. Translation: AAX33562.1. Sequence problems. AY070553 mRNA. Translation: AAL48024.1. Different initiation. |
| PIR | A43434. |
| RefSeq | NP_523368.2. NM_078644.3. NP_727963.1. NM_167506.2. NP_727964.1. NM_167507.2. NP_727965.1. NM_167508.2. NP_727966.1. NM_167509.2. NP_727967.1. NM_167510.2. NP_996486.1. NM_206763.1. |
| UniGene | Dm.6383. |
3D structure databases | |
| ProteinModelPortal | P30432. |
| SMR | P30432. Positions 239-311, 375-852, 965-1411. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P30432. 1 interaction. |
| MINT | MINT-918283. |
| STRING | P30432. |
Protein family/group databases | |
| MEROPS | S08.049. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | FBtr0074262; FBpp0074039; FBgn0004598. FBtr0074264; FBpp0074041; FBgn0004598. FBtr0074266; FBpp0074043; FBgn0004598. FBtr0074267; FBpp0089399; FBgn0004598. |
| GeneID | 32604. |
| KEGG | dme:Dmel_CG18734. |
Organism-specific databases | |
| CTD | 32604. |
| FlyBase | FBgn0004598. Fur2. |
Phylogenomic databases | |
| eggNOG | inNOG07052. |
| GeneTree | EMGT00050000008995. |
| InParanoid | P30432. |
| OMA | FKPWYLE. |
| OrthoDB | EOG4MPG51. |
| PhylomeDB | P30432. |
Gene expression databases | |
| Bgee | P30432. |
| GermOnline | CG18734. Drosophila melanogaster. |
Family and domain databases | |
| InterPro | IPR006210. EGF-like. IPR006211. Furin-like_Cys-rich_dom. 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. |
| KO | K01349. |
| PANTHER | PTHR10795. SubtilSerProt. 1 hit. |
| Pfam | PF00757. Furin-like. 1 hit. PF01483. P_proprotein. 1 hit. PF00082. Peptidase_S8. 1 hit. [Graphical view] |
| PRINTS | PR00723. SUBTILISIN. |
| SMART | SM00181. EGF. 1 hit. SM00261. FU. 10 hits. [Graphical view] |
| SUPFAM | SSF49785. Gal_bind_like. 1 hit. SSF57184. Grow_fac_recept. 4 hits. 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... |
Other | |
| NextBio | 779394. |
Entry information
| Entry name | FUR2_DROME | ||||||||
| Accession | Primary (citable) accession number: P30432 Secondary accession number(s): A4V4M0 Q8SZS2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Drosophila annotation project | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with