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Q9V853 (SMUF1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
E3 ubiquitin-protein ligase Smurf1
EC=6.3.2.-
Alternative name(s):
Lethal with a checkpoint kinase protein
SMAD ubiquitination regulatory factor 1 homolog
Short name=DSmurf
Gene names
Name:lack
Synonyms:Smurf, Smurf1
ORF Names:CG4943
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length1061 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Down-regulates Dpp signaling after gastrulation by promoting MAD ubiquitination and subsequent degradation. Ref.1 Ref.2

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with phosphorylated MAD. Ref.1 Ref.2

Developmental stage

Uniformly expressed at blastoderm stage. Weakly but broadly expressed at later stages of embryogenesis. Ref.1

Disruption phenotype

Flies exhibit lethal defects in hindgut morphogenesis. Ref.1

Sequence similarities

Contains 1 C2 domain.

Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.

Contains 3 WW domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

fuP236475EBI-133520,EBI-165536
tkvQ95SI02EBI-133520,EBI-3401975

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10611061E3 ubiquitin-protein ligase Smurf1
PRO_0000120330

Regions

Domain14 – 9784C2
Domain167 – 20034WW 1
Domain513 – 54634WW 2
Domain561 – 59434WW 3
Domain723 – 1061339HECT
Region513 – 60290Interaction with MAD
Compositional bias486 – 4949Poly-Gly
Compositional bias645 – 6539Poly-Thr

Sites

Active site10291Glycyl thioester intermediate

Amino acid modifications

Modified residue2621Phosphoserine Ref.7
Modified residue4121Phosphothreonine Ref.7
Modified residue4161Phosphoserine Ref.7

Experimental info

Mutagenesis5411W → F: Abolishes interaction with MAD; when associated with A-544. Ref.2
Mutagenesis5441P → A: Abolishes interaction with MAD; when associated with F-541. Ref.2
Mutagenesis10291C → A: Abolishes enzymatic activity; no change in interaction with MAD. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9V853 [UniParc].

Last modified October 1, 2002. Version 3.
Checksum: 6BBCC550F5129163

FASTA1,061115,676
        10         20         30         40         50         60 
MNKLDYPRRN GTHKVRITIL CARNLARKDL FRLPDPFAKV QVDGTGQVYS TEISKSSLDP 

        70         80         90        100        110        120 
KWNAHYDLFL GIGDAITITV WNQRKIHKGS GFLGCVRIPA FNIQSLKGAG FQRLDLGKLS 

       130        140        150        160        170        180 
PDDDELVRGQ IIISLLSKDG PSSGNPLAIV GPSGDVRGPS EDDSSEDSLP EGWEERRTDN 

       190        200        210        220        230        240 
GRVYYVNHAT KSTQWDRPRQ PGVVGSSHAT SPQQRHNTHN GNSGDRQAPA GPTRSTTCTN 

       250        260        270        280        290        300 
LMNNGHRSRD LSVTASDERR HSTEILSSVG KENTSPTTPV SATTTPGKKT SSSNSSSAGG 

       310        320        330        340        350        360 
RTLEQRPTNE PATPTSSTTS ASVRLHSNDN HVKTPKHQTN GHAPPESTPT SPTGQQNYVN 

       370        380        390        400        410        420 
GNAQNGSTSG NGSGQAAQPQ SASNGWTQED AATTTSPSTT TSPPRHSQSP PTPNISPPAS 

       430        440        450        460        470        480 
VTPSANGNVH SPNANSTPAG SGGGSRSYTA ATPGQRSQRR SSRQQGEESS TRRRSSRGTR 

       490        500        510        520        530        540 
NGGTSGGGGG GGSGQRYASA AIAAANQAAR PFLDLPPGYE MRTTQQGQVY FYHIPTGVST 

       550        560        570        580        590        600 
WHDPRIPRDF DTQHLTLDAI GPLPSGWEQR KTASGRVYFV DHNNRTTQFT DPRLSGSILQ 

       610        620        630        640        650        660 
MIRRGTVPPT SAANAGTPAP PSATPATPSA AAAVPPQATP ASNATPTTLT TTTNPPHRIV 

       670        680        690        700        710        720 
PDLPQGLLEG ADLLPKYRRD LVGKLRALRT ELQTMQPQSG HCRLEVSRNE IFEESYRLIM 

       730        740        750        760        770        780 
KMRAKDMRKR LMVKFKGEEG LDYGGVAREW LHLLSREMLN PQYGLFQYSR DDHYTLQINP 

       790        800        810        820        830        840 
DSGVNPDHLS YFHFVGRTLG IAVFHGHCLD GGFTTPFYKQ LLNKPITLGD IEGVDPDLHR 

       850        860        870        880        890        900 
SLTWMLESNI SGIIESTFSV ENNSFGALVV HELKPGGASI PVTEENKREY VKLYVNYRFM 

       910        920        930        940        950        960 
RGIEQQFLAL QKGFCELIPS HLLRPFDERE LELVIGGISS IDVNDWRNNT RLKHCTNETT 

       970        980        990       1000       1010       1020 
QVLWFWQVVE SYSSEMRARL LQFVTGSSRV PLQGFRALQG STGAVGPRLF TIHLTADVPT 

      1030       1040       1050       1060 
QNLPKAHTCF NRIDLPPYET YQLLCDKLTQ AVEETCGFAV E

« Hide

References

« Hide 'large scale' references
[1]"The DSmurf ubiquitin-protein ligase restricts BMP signaling spatially and temporally during Drosophila embryogenesis."
Podos S.D., Hanson K.K., Wang Y.-C., Ferguson E.L.
Dev. Cell 1:567-578(2001) [PubMed: 11703946] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MAD, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[2]"DSmurf selectively degrades decapentaplegic-activated MAD, and its overexpression disrupts imaginal disc development."
Liang Y.-Y., Lin X., Liang M., Brunicardi F.C., ten Dijke P., Chen Z., Choi K.-W., Feng X.-H.
J. Biol. Chem. 278:26307-26310(2003) [PubMed: 12754252] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MAD, MUTAGENESIS OF TRP-541; PRO-544 AND CYS-1029.
[3]"Molecular cloning of a type E3 Ubiquitin ligase."
Laurencon A., Hawley S.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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.
[5]"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.
Strain: Berkeley.
[6]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].
Strain: Berkeley.
Tissue: Embryo.
[7]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262; THR-412 AND SER-416, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF416571 mRNA. Translation: AAL09691.1.
AF464851 mRNA. Translation: AAM09646.1.
AF216521 mRNA. Translation: AAF21125.1.
AE013599 Genomic DNA. Translation: AAF57824.3.
BT021410 mRNA. Translation: AAX33558.1.
RefSeqNP_523779.1. NM_079055.2.
UniGeneDm.2783.

3D structure databases

ProteinModelPortalQ9V853.
SMRQ9V853. Positions 11-139, 169-201, 514-1055.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9V853. 3 interactions.
MINTMINT-4080844.
STRINGQ9V853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0086833; FBpp0086011; FBgn0029006.
GeneID36999.
KEGGdme:Dmel_CG4943.
NMPDRfig|7227.3.peg.5997.

Organism-specific databases

CTD36999.
FlyBaseFBgn0029006. lack.

Phylogenomic databases

eggNOGinNOG09206.
GeneTreeEMGT00050000000712.
InParanoidQ9V853.
OMAANQAARP.
OrthoDBEOG4QNKB3.
PhylomeDBQ9V853.

Gene expression databases

BgeeQ9V853.
GermOnlineCG4943. Drosophila melanogaster.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR000569. HECT.
IPR001202. WW_Rsp5_WWP.
[Graphical view]
Gene3DG3DSA:2.20.70.10. G3DSA:2.20.70.10. 3 hits.
KOK04678.
PfamPF00168. C2. 1 hit.
PF00632. HECT. 1 hit.
PF00397. WW. 3 hits.
[Graphical view]
SMARTSM00239. C2. 1 hit.
SM00119. HECTc. 1 hit.
SM00456. WW. 3 hits.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF56204. HECT. 1 hit.
SSF51045. WW_Rsp5_WWP. 3 hits.
PROSITEPS50004. C2. 1 hit.
PS50237. HECT. 1 hit.
PS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio801434.

Entry information

Entry nameSMUF1_DROME
AccessionPrimary (citable) accession number: Q9V853
Secondary accession number(s): Q9U3W2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents