Unreviewed, UniProtKB/TrEMBL O97102 (O97102_DROME)

Names and origin

Protein names

Submitted name:
    Smt3 EMBL AAF52470.1
Submitted name:
    LD07775p EMBL AAL28638.1
    Ubiquitin-like protein SMT3 EMBL AAD19219.1

Gene names

Name:	smt3 EMBL AAF52470.1 FlyBase FBgn0026170
Synonyms:	Smt3 EMBL AAF31702.1
ORF Names:	CG4494 FlyBase FBgn0026170, Dmel_CG4494 EMBL AAF52470.1

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

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	90 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Ontologies

Keywords
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phagocytosis, engulfment Inferred from mutant phenotype. Source: FlyBase protein import into nucleus Ref.4 Inferred from genetic interaction. Source: FlyBase protein modification process Ref.4 Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Ref.4 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	O97102-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: E49DA04C24A13CA5	FASTA	90	10,124
	10 20 30 40 50 60 MSDEKKGGET EHINLKVLGQ DNAVVQFKIK KHTPLRKLMN AYCDRAGLSM QVVRFRFDGQ 70 80 90 PINENDTPTS LEMEEGDTIE VYQQQTGGAP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , 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.
[2]	"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. , 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: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., Chavez C., Dorsett V., Farfan D., Frise E., George R., Gonzalez M., Guarin H., Li P., Liao G., Miranda A., Mungall C.J., Nunoo J. , Pacleb J., Paragas V., Park S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: Berkeley EMBL AAL28638.1.
[4]	"A functional interaction between dorsal and components of the Smt3 conjugation machinery." Bhaskar V., Valentine S.A., Courey A.J. J. Biol. Chem. 275:4033-4040(2000) [PubMed: 10660560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[5]	"Identification and characterization of the SMT3 cDNA and gene encoding ubiquitin-like protein from Drosophila melanogaster." Huang H.W., Tsoi S.C., Sun Y.H., Li S.S. Biochem Mol Biol Int 46:775-785(1998) [PubMed: 9844739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[6]	Li S.S.-L., Huang H.W. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF053083 mRNA. Translation: AAD19219.1.
AF218862 mRNA. Translation: AAF31702.1.
AE014134 Genomic DNA. Translation: AAF52470.1.
AY061090 mRNA. Translation: AAL28638.1.

RefSeq

NP_477411.1.

UniGene

Dm.6873

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K1F	NMR	-	A	1-88	[»]

SMR

O97102. Positions 11-90.

ModBase

Search...

Protein-protein interaction databases

IntAct

O97102. 9 interactions.

Proteomic databases

PRIDE

O97102.

Genome annotation databases

Ensembl

FBgn0026170. Drosophila melanogaster. [Contig view]

GeneID

33981.

KEGG

dme:Dmel_CG4494.

NMPDR

fig|7227.3.peg.1172.

Organism-specific databases

FlyBase

FBgn0026170. smt3.

Phylogenomic databases

HOGENOM

O97102.

OMA

O97102. DRQSVDM.

Gene expression databases

ArrayExpress

O97102.

Family and domain databases

InterPro

IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
[Graphical view]

Pfam

PF00240. ubiquitin. 1 hit.
[Graphical view]

SMART

SM00213. UBQ. 1 hit.
[Graphical view]

PROSITE

PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

786256.

Entry information

Entry name

O97102_DROME

Accession

Primary (citable) accession number: O97102

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 1999
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)