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UniProtKB/Swiss-Prot entry P20351


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

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Entry information
Entry name T23O_DROME
Primary accession number P20351
Secondary accession number Q9VZ50
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on February 1, 1991 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 70)
Name and origin of the protein
Protein name Tryptophan 2,3-dioxygenase
Synonyms TO
EC 1.13.11.11
Tryptophan pyrrolase
Protein vermilion
Gene name
Name: v
ORFNames: CG5163
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 [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=2108317 [NCBI, ExPASy, EBI, Israel, Japan]
Searles L.L., Ruth R.S., Pret A.-M., Fridell R.A., Ali A.J.;
"Structure and transcription of the Drosophila melanogaster vermilion gene and several mutant alleles.";
Mol. Cell. Biol. 10:1423-1431(1990).
[2]
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).
[3]
GENOME REANNOTATION.
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Head;
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
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
M34147; AAA29014.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014298; AAF47978.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY051478; AAK92902.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A34780; A34780.
RefSeq NP_511113.1; -.
UniGene Dm.7748
3D structure databases
ModBase P20351.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-001405-MON; -.
Organism-specific databases
FlyBase FBgn0003965; v.
Gene expression databases
ArrayExpress P20351; -.
GermOnline CG2155; Drosophila melanogaster.
Ontologies
GO
GO:0004833; Molecular function: tryptophan 2,3-dioxygenase activity (traceable author statement from FlyBase).
GO:0048072; Biological process: compound eye pigmentation (traceable author statement from FlyBase).
GO:0006727; Biological process: ommochrome biosynthetic process (inferred from mutant phenotype from FlyBase).
GO:0006569; Biological process: tryptophan catabolic process (traceable author statement from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR004981; Trp_2_3_dOase.
Graphical view of domain structure.
PANTHER PTHR10138; Trp_2_3_dOase; 1.
Pfam PF03301; Trp_dioxygenase; 1.
Pfam graphical view of domain structure.
BLOCKS P20351.
Genome annotation databases
Ensembl CG2155; Drosophila melanogaster. [Contig view]
GeneID 32026; -.
KEGG dme:Dmel_CG2155; -.
NMPDR fig|7227.3.peg.17334; -.
Other
ProtoNet P20351.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   379  379     Tryptophan 2,3-dioxygenase. PRO_0000065780
Sequence information
Length: 379 AA [This is the length of the unprocessed precursor] Molecular weight: 44421 Da [This is the MW of the unprocessed precursor] CRC64: E9E4C1B1C86D687F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSCPYAGNGN DHDDSAVPLT TEVGKIYGEY LMLDKLLDAQ CMLSEEDKRP VHDEHLFIIT 

        70         80         90        100        110        120 
HQAYELWFKQ IIFEFDSIRD MLDAEVIDET KTLEIVKRLN RVVLILKLLV DQVPILETMT 

       130        140        150        160        170        180 
PLDFMDFRKY LAPASGFQSL QFRLIENKLG VLTEQRVRYN QKYSDVFSDE EARNSIRNSE 

       190        200        210        220        230        240 
KDPSLLELVQ RWLERTPGLE ESGFNFWAKF QESVDRFLEA QVQSAMEEPV EKAKNYRLMD 

       250        260        270        280        290        300 
IEKRREVYRS IFDPAVHDAL VRRGDRRFSH RALQGAIMIT FYRDEPRFSQ PHQLLTLLMD 

       310        320        330        340        350        360 
IDSLITKWRY NHVIMVQRMI GSQQLGTGGS SGYQYLRSTL SDRYKVFLDL FNLSTFLIPR 

       370 
EAIPPLDETI RKKLINKSV 

P20351 in FASTA format

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