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Reviewed, UniProtKB/Swiss-Prot P54360 (FOJO_DROME)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein four-jointed
Cleaved into the following chain:
    1- Recommended name:
            Protein four-jointed, secreted isoform
Gene names
Name: fj
ORF Names: CG10917
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required for intermediate growth in the proximal-distal axis. Acts in ommatidial polarity determination as a secondary signal downstream of Notch, JAK/STAT and wingless. Also necessary for the initiation, up-regulation or maintenance of Notch ligand, Serrate (Ser) expression in legs, thereby participating in a feedback loop with N signaling. Sufficient for joint formation and growth in the leg. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein. Note: Golgi apparatus, in the wing pouch. Ref.7 Ref.8

Protein four-jointed, secreted isoform: Secreted. Ref.7 Ref.8

Tissue specificity

In the eye disk, expressed in a gradient ahead of the morphogenetic furrow, high at the equator and low at the poles of the eye. In the leg disk, expressed in concentric rings, possibly corresponding to segmental boundaries. In the wing disk, expression is localized in the wing pouch; low in peripheral regions and high towards the center. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8

Post-translational modification

Proteolytically cleaved to yield a secreted protein. Ref.8

Disruption phenotype

Mutants show reduced growth and altered differentiation only within restricted sectors of the proximal-distal (PD) axis in the leg and wing. Ref.1

Sequence similarities

Belongs to the FJX1/FJ family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 583583Protein four-jointed
PRO_0000087324
Chain? – 583Protein four-jointed, secreted isoformPRO_0000292347

Regions

Topological domain1 – 7878Cytoplasmic Potential
Transmembrane79 – 9921Signal-anchor for type II membrane protein Potential
Topological domain100 – 583484Extracellular Potential

Amino acid modifications

Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation3791N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict481P → S Ref.1
Sequence conflict481P → S Ref.2
Sequence conflict1261S → T in AAA69524. Ref.1
Sequence conflict1931L → M in AAA69524. Ref.1
Sequence conflict2251F → L Ref.1
Sequence conflict2251F → L Ref.2
Sequence conflict2881R → P in AAA69524. Ref.1
Sequence conflict3301A → R in AAA69524. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54360-1 [UniParc].

Last modified May 24, 2005. Version 2.
Checksum: 8AADC85FC85D09A4

FASTA58365,490
        10         20         30         40         50         60 
MYDIKRLEAG QQKLQQAQQP LGLDLSGQQQ QLTCSVITAP EHRANPNPSS ISQSNPSEAT 

        70         80         90        100        110        120 
HMTLLTLRRR RSLQRRACLL SILAAFVFGM ALGVVVPMFG LPRHQDSPPD LPEEQIQMVA 

       130        140        150        160        170        180 
VEPLSSYRVE FIKETDELSA EQVFRNAFHL EQDKDAPDSM VVKKLDTNDG SIKEFHVQRT 

       190        200        210        220        230        240 
ASGRYRKGPE RRLSKKMPER VQPQETSRSP TTSPTNPTSE HQAGFIEEDV YWGPTVEQAL 

       250        260        270        280        290        300 
PKGFAAKDQV SWERFVGEQG RVVRLEQGCG RMQNRMVVFA DGTRACARYR QNTDQIQGEI 

       310        320        330        340        350        360 
FSYYLGQLLN ISNLAPSAAT VVDTSTPNWA AALGDITQAQ WKERRPVVLT RWLSDLEPAG 

       370        380        390        400        410        420 
IPQPFQPLER HLNKHDVWNL TRHMQSERQA QSQPHGLLKR LGAASSPGSA HQSNAIEETG 

       430        440        450        460        470        480 
TGTETANGAL VQRLIELAQW SDLIVFDYLI ANLDRVVNNL YNFQWNADIM AAPAHNLARQ 

       490        500        510        520        530        540 
SASQLLVFLD NESGLLHGYR LLKKYEAYHS LLLDNLCVFR RPTIDALRRL RAAGAGRRLR 

       550        560        570        580 
DLFERTTSAG VRDVLPSLPD KSVKILVERI DRVLGQVQKC QGS 

« Hide

References

« Hide 'large scale' references
[1]"four-jointed is required for intermediate growth in the proximal-distal axis in Drosophila."
Villano J.L., Katz F.N.
Development 121:2767-2777(1995) [PubMed: 7555705] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
Tissue: Eye imaginal disk.
[2]"Positional information along the dorsal-ventral axis of the Drosophila eye: graded expression of the four-jointed gene."
Brodsky M.H., Steller H.
Dev. Biol. 173:428-446(1996) [PubMed: 8606003] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Strain: Canton-S.
[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.
[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].
Strain: Berkeley.
Tissue: Embryo.
[6]"The four-jointed gene is required in the Drosophila eye for ommatidial polarity specification."
Zeidler M.P., Perrimon N., Strutt D.I.
Curr. Biol. 9:1363-1372(1999) [PubMed: 10607560] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[7]"Four-jointed interacts with dachs, abelson and enabled and feeds back onto the Notch pathway to affect growth and segmentation in the Drosophila leg."
Buckles G.R., Rauskolb C., Villano J.L., Katz F.N.
Development 128:3533-3542(2001) [PubMed: 11566858] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Cleavage and secretion is not required for four-jointed function in Drosophila patterning."
Strutt H., Mundy J., Hofstra K., Strutt D.
Development 131:881-890(2004) [PubMed: 14757640] [Abstract]
Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

U28837 mRNA. Translation: AAA69524.1.
U44904 mRNA. Translation: AAB01809.1.
AE013599 Genomic DNA. Translation: AAF57724.2.
AY071147 mRNA. Translation: AAL48769.1.
RefSeqNP_477483.1.
UniGeneDm.4763

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP54360. 3 interactions.

Genome annotation databases

EnsemblFBgn0000658. Drosophila melanogaster. [Contig view]
GeneID37089.
KEGGdme:Dmel_CG10917.
NMPDRfig|7227.3.peg.6125.

Organism-specific databases

FlyBaseFBgn0000658. fj.

Phylogenomic databases

HOGENOMP54360.
OMAP54360. TRACARY.

Gene expression databases

ArrayExpressP54360.
GermOnlineCG10917. Drosophila melanogaster.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio801889.

Entry information

Entry nameFOJO_DROME
AccessionPrimary (citable) accession number: P54360
Secondary accession number(s): Q24176, Q8SZ37, Q9V8E3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 24, 2005
Last modified: June 16, 2009
This is version 69 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

SIMILARITY comments

Index of protein domains and families

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