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Protein

Nucleotide exchange factor SIL1

Gene

CG10420

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for an ER lumenal chaperone of HSP70 family (By similarity).By similarity

GO - Biological processi

  1. SRP-dependent cotranslational protein targeting to membrane, translocation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleotide exchange factor SIL1
Gene namesi
ORF Names:CG10420
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0039296. CG10420.

Subcellular locationi

GO - Cellular componenti

  1. endomembrane system Source: FlyBase
  2. endoplasmic reticulum Source: UniProtKB
  3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 429405Nucleotide exchange factor SIL1PRO_0000223358Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9VBV5.
PRIDEiQ9VBV5.

Expressioni

Gene expression databases

BgeeiQ9VBV5.

Interactioni

Protein-protein interaction databases

BioGridi67953. 13 interactions.
IntActiQ9VBV5. 1 interaction.
STRINGi7227.FBpp0084244.

Structurei

3D structure databases

ProteinModelPortaliQ9VBV5.
SMRiQ9VBV5. Positions 203-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili104 – 13532Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi426 – 4294Prevents secretion from ERSequence Analysis

Sequence similaritiesi

Belongs to the SIL1 family.Curated

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG310365.
GeneTreeiENSGT00510000048102.
InParanoidiQ9VBV5.
KOiK14001.
OMAiQGWCEIT.
OrthoDBiEOG72G176.
PhylomeDBiQ9VBV5.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9VBV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGKQVVILL GSVLILGCLQ VAAATETDNK TNDFVATDEW QTIAEGQAIP
60 70 80 90 100
RGLHVRINLQ TGLKEAKLLD ESERGTSLQS QPDDQNARES HDDNEPLALD
110 120 130 140 150
YKPDIIEESI RRVKEQKKSY AELRKAYKEF QKNFRTDGEL IVQLIDQFRN
160 170 180 190 200
FSRTPLESEM RSKLDCLENL EYLLHQIDNA LMFIDNGGLD DVLLPIVVND
210 220 230 240 250
TSTSLRVSAM RVLGSLASNN PKAQIKVFEK NFGSHLAQIL TSSGNVGEIS
260 270 280 290 300
AALHAFGALL RKFPLAQQRV LSTSGTQALI KVLQSPDVEL RSKAKVVTLI
310 320 330 340 350
SDLVLEKRSV LDVSKDDPEA SSTMAQYVLL DFESWLKTPG YCAAVDTVLT
360 370 380 390 400
KEFLLLLEQP EVVEQFATAL ETTEDMCTST WSQSSGLRHA LLTVRNRYAN
410 420
STDEYRLEVS QILAKLCERL FNKPKHTEL
Length:429
Mass (Da):47,943
Last modified:May 1, 2000 - v1
Checksum:i476349B0C0CD8EE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF56422.1.
AY058471 mRNA. Translation: AAL13700.1.
RefSeqiNP_651356.1. NM_143099.4.
UniGeneiDm.1330.

Genome annotation databases

EnsemblMetazoaiFBtr0084870; FBpp0084244; FBgn0039296.
GeneIDi43034.
KEGGidme:Dmel_CG10420.
UCSCiCG10420-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF56422.1.
AY058471 mRNA. Translation: AAL13700.1.
RefSeqiNP_651356.1. NM_143099.4.
UniGeneiDm.1330.

3D structure databases

ProteinModelPortaliQ9VBV5.
SMRiQ9VBV5. Positions 203-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67953. 13 interactions.
IntActiQ9VBV5. 1 interaction.
STRINGi7227.FBpp0084244.

Proteomic databases

PaxDbiQ9VBV5.
PRIDEiQ9VBV5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084870; FBpp0084244; FBgn0039296.
GeneIDi43034.
KEGGidme:Dmel_CG10420.
UCSCiCG10420-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0039296. CG10420.

Phylogenomic databases

eggNOGiNOG310365.
GeneTreeiENSGT00510000048102.
InParanoidiQ9VBV5.
KOiK14001.
OMAiQGWCEIT.
OrthoDBiEOG72G176.
PhylomeDBiQ9VBV5.

Miscellaneous databases

GenomeRNAii43034.
NextBioi831896.
PROiQ9VBV5.

Gene expression databases

BgeeiQ9VBV5.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiSIL1_DROME
AccessioniPrimary (citable) accession number: Q9VBV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.