Q8T3Y0 (SINAL_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable E3 ubiquitin-protein ligase sinah
EC=6.3.2.-

Alternative name(s):
Sina homolog

Gene names

Name:	sinah
ORF Names:	CG13030

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. The adapter phyl is required to direct the degradation of the two isoforms of the transcriptional repressor Tramtrack (Ttk). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates. A phyl-independent mechanism of degradation exists for isoform beta of ttk that involves motifs in the C-terminus of ttk. Ref.4 Ref.5
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with ebi and phyl. Ref.4 Ref.5
Developmental stage	Expressed in pupae and in adults, with a higher expression in males than females. Ref.4
Domain	The RING-type zinc finger domain is essential for ubiquitin ligase activity By similarity. The SBD domain (substrate-binding domain) mediates the homodimerization and the interaction with substrate proteins. It is related to the TRAF family By similarity.
Disruption phenotype	Flies are viable. In combination with a mutation in ebi, flies show an extra dorsal central bristle phenotype. Flies that lack both sina and sinah show visible eye and bristle phenotypes, which can be explained by an inability to degrade the neuronal repressor, Tramtrack. Ref.4
Sequence similarities	Belongs to the SINA (Seven in absentia) family. Contains 1 RING-type zinc finger. Contains 1 SIAH-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteasomal protein catabolic process Inferred from direct assay Ref.5. Source: FlyBase regulation of R7 cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB sensory organ development Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ubiquitin-protein ligase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 351	351	Probable E3 ubiquitin-protein ligase sinah		PRO_0000056178
Regions
	Zinc finger	106 – 141	36	RING-type
	Zinc finger	158 – 218	61	SIAH-type
	Region	155 – 346	192	SBD
Sites
	Metal binding	163	1	Zinc 1 By similarity
	Metal binding	170	1	Zinc 1 By similarity
	Metal binding	182	1	Zinc 1 By similarity
	Metal binding	186	1	Zinc 1 By similarity
	Metal binding	193	1	Zinc 2 By similarity
	Metal binding	200	1	Zinc 2 By similarity
	Metal binding	212	1	Zinc 2 By similarity
	Metal binding	217	1	Zinc 2 By similarity
Experimental info
	Sequence conflict	351	1	N → Y in AAL90183. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8T3Y0 [UniParc]. Last modified April 26, 2004. Version 2. Checksum: 415764CBBD433331	FASTA	351	39,645
	10 20 30 40 50 60 MSVRNSRPQL SWPERVSPQR TIDTPTASGE MLTRRQSAPA LVVPPEETTH VVVVKRQSPD 70 80 90 100 110 120 AAAAGELVPS RRKDSVAVQS GIVATGPLDT TRSGARDDFL MALLECPVCF GYIMPPIMQC 130 140 150 160 170 180 PRGHLICSTC RSKLTICPVC RVFMTNIRSL AMEKVASKLI FPCKHSHFGC RARLSYAEKT 190 200 210 220 230 240 KHEEDCECRP YFCPYPDDKC SWQGPLRDVY QHLMSSHENV ITMEGNDIIF LATNVNLEGA 250 260 270 280 290 300 LDWTMVQSCH GRHFLLSLEK INLGEDCQQY FTACRMIGSM KDAAEFVYNI SLEAYNRTLR 310 320 330 340 350 WQSKPRSIRE NFSSFTNADF LVLNKHTVEL FSEDGNLALN VVIRKVEERT N

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Testis.
[4]	"In vivo function of a novel Siah protein in Drosophila." Cooper S.E. Mech. Dev. 124:584-591(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EBI, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[5]	"Two modes of degradation of the tramtrack transcription factors by Siah homologues." Cooper S.E., Murawsky C.M., Lowe N., Travers A.A. J. Biol. Chem. 283:1076-1083(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PHYL.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014296 Genomic DNA. Translation: AAF49402.3. AY089445 mRNA. Translation: AAL90183.1.
RefSeq	NP_648927.1. NM_140670.2.
UniGene	Dm.29700.
3D structure databases
ProteinModelPortal	Q8T3Y0.
SMR	Q8T3Y0. Positions 97-343.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-17367N.
IntAct	Q8T3Y0. 20 interactions.
MINT	MINT-288495.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0301683; FBpp0290897; FBgn0259794.
GeneID	39885.
KEGG	dme:Dmel_CG13030.
UCSC	CG13030-RB. d. melanogaster.
Organism-specific databases
CTD	39885.
FlyBase	FBgn0259794. sinah.
Phylogenomic databases
eggNOG	NOG308883.
GeneTree	ENSGT00390000005434.
InParanoid	Q8T3Y0.
KO	K04506.
OMA	LMSSHEN.
OrthoDB	EOG4K3JBV.
PhylomeDB	Q8T3Y0.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Bgee	Q8T3Y0.
GermOnline	CG13030. Drosophila melanogaster.
Family and domain databases
Gene3D	3.30.40.10. 1 hit. 3.90.890.10. 1 hit.
InterPro	IPR004162. 7-in-absentia-prot. IPR018121. 7-in-absentia-prot_TRAF-dom. IPR013323. SIAH-type. IPR008974. TRAF-like. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR013010. Znf_SIAH. [Graphical view]
PANTHER	PTHR10315. PTHR10315. 1 hit.
Pfam	PF03145. Sina. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF49599. Traf_like. 1 hit.
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. PS51081. ZF_SIAH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	39885.
NextBio	815894.

Entry information

Entry name

SINAL_DROME

Accession

Primary (citable) accession number: Q8T3Y0
Secondary accession number(s): Q9VVB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project