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Protein

Cytoplasmic FMR1-interacting protein

Gene

Sra-1

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

Functioni

Plays a role in guidance and morphology of central and peripheral axons and in synaptic morphology. Also required for formation of cell membrane protrusions and for bristle development.4 Publications

GO - Molecular functioni

GO - Biological processi

  • axon guidance Source: FlyBase
  • cell adhesion mediated by integrin Source: FlyBase
  • cell morphogenesis Source: FlyBase
  • cell projection assembly Source: FlyBase
  • chaeta development Source: UniProtKB
  • compound eye morphogenesis Source: FlyBase
  • cortical actin cytoskeleton organization Source: FlyBase
  • phagocytosis Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • regulation of synapse organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell shape, Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-DME-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-5663213. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic FMR1-interacting protein
Alternative name(s):
Specifically Rac1-associated protein 1
Short name:
DSra-1
Gene namesi
Name:Sra-1Imported
Synonyms:Cyfip1 Publication
ORF Names:CG4931
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0038320. Sra-1.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Accumulates in central axons and motor neuron terminals.1 Publication

GO - Cellular componenti

  • apical part of cell Source: FlyBase
  • cytoplasm Source: FlyBase
  • SCAR complex Source: UniProtKB
  • synapse Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Flies display pupal lethality with defects in axon growth, branching and pathfinding, synaptic length and organization of the neuromuscular junction. They also display defects in cell morphology with cells exhibiting a starfish-like shape with multiple slender cell extensions and loss of actin filaments at the cell periphery.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12911291Cytoplasmic FMR1-interacting proteinPRO_0000279714Add
BLAST

Proteomic databases

PaxDbiQ9VF87.
PRIDEiQ9VF87.

Expressioni

Tissue specificityi

In the embryo, expressed mainly in the gut and in the developing central nervous system where high levels of expression are found in the CNS neuropile. Expression in the gut diminishes as development proceeds (at protein level). In the adult, expressed specifically in the nervous system.2 Publications

Developmental stagei

Expressed throughout the life cycle with no major peaks of expression. In the embryo, uniquitously and highly expressed at precellular and cellular blastoderm stages.1 Publication

Gene expression databases

BgeeiQ9VF87.
GenevisibleiQ9VF87. DM.

Interactioni

Subunit structurei

Interacts with Fmr1 and Rac1. Component of the WAVE complex composed of Hem/Kette, Scar/Wave and Sra-1/Cyfip where it binds through its C-terminus directly to Hem.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nap1Q241502EBI-116862,EBI-603430

GO - Molecular functioni

Protein-protein interaction databases

BioGridi66924. 2 interactions.
DIPiDIP-33370N.
IntActiQ9VF87. 3 interactions.
MINTiMINT-252304.
STRINGi7227.FBpp0082541.

Family & Domainsi

Sequence similaritiesi

Belongs to the CYFIP family.Sequence analysis

Phylogenomic databases

eggNOGiKOG3534. Eukaryota.
ENOG410XPKW. LUCA.
GeneTreeiENSGT00500000044831.
InParanoidiQ9VF87.
KOiK05749.
OMAiATNRFVK.
OrthoDBiEOG7ZSHS2.
PhylomeDBiQ9VF87.

Family and domain databases

InterProiIPR008081. Cytoplasmic_FMR1-int.
IPR009828. DUF1394.
[Graphical view]
PANTHERiPTHR12195. PTHR12195. 2 hits.
PfamiPF07159. DUF1394. 1 hit.
PF05994. FragX_IP. 1 hit.
[Graphical view]
PIRSFiPIRSF008153. FMR1_interacting. 1 hit.
PRINTSiPR01698. CYTOFMRPINTP.

Sequencei

Sequence statusi: Complete.

Q9VF87-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEKITLADA LSNVEVLDEL SLPDEQPCIE AQPCSIIYKA NFDTNFEDRN
60 70 80 90 100
GFVTGIAKYI EEATTHANLN VLLDEGQKHA VMLYTWRCCS RAIPQPKSNE
110 120 130 140 150
QPNRVEIYEK TVEVLAPEVN KLLNFMYFQR KAIEAFSGEV KRLCHAEKRK
160 170 180 190 200
DFVSEAYLLT LGKFINMFAV LDELKNMKSS VKNDYSTYRR AAQFLKVMSD
210 220 230 240 250
SHTLQESQNL SMFLATQNKI RDTVKDTLEK IVGYEDLLSD VVNICVHMFE
260 270 280 290 300
TKMYLTPEEK HMLVKVMGFG LFLMDSDACN INKLDQKKKI RLDRIDRIFK
310 320 330 340 350
NLEVVPLFGD MQIAPFNYIK RSKHFDSSKW PLSSSNAISP QADLMVHLPQ
360 370 380 390 400
IREDHVKYIS ELARYTNEVT TTVKENPSDA ENRITADLAL RGLQLLSEWT
410 420 430 440 450
SVVTELYSWK LLHPTDHHQN KECPVEAEEY ERATRYNYTS EEKFALIEVI
460 470 480 490 500
AMIKGLQVLM ARIETVLCEA IRRNIYSELQ DFVQLSLREP LRKAVKNKKD
510 520 530 540 550
LIRSIIMSVR ETSADWQKGY EPTDDPVAKG KKDPDGGFRI QVPRLNVGPS
560 570 580 590 600
STQLYMVRTM LESLIADKSG GKRTLRKDID GNCLLQIDTF HKTSFYWSYL
610 620 630 640 650
LNFSDTLQKC CDLSQLWYRE FYLEMTMGRK VNKCLVRHQH NEECKDLITM
660 670 680 690 700
EKRIQFPIEM SMPWILTDHI LQTKEPSMME FVLYPLDLYN DSAYYALTVF
710 720 730 740 750
RKQFLYDEVE AEVNLCFDQF VYKLSEQIFA HYKQLAGSIF LDKRFRLECE
760 770 780 790 800
VLGFNFQSYP RNNRYETLLK QRHVQLLGRS IDLNKLITQR INANMHKSIE
810 820 830 840 850
LAISRFEGND ITGIVELEGL LEANRICHKL LSKYLALDNF DGMVKEANHN
860 870 880 890 900
VLAPYGRITL HVFVELNYDF LVNYCYNAAT NRFIRTKVNL SSSQAIQREK
910 920 930 940 950
PPQMSHYYLW GSKQLNAAYS TQYGQYTGFV GSPHFHAMCR LLGYQGIAVV
960 970 980 990 1000
MDIILKDIVK PLIQGSLLQF TKTLMIAMPK SCKLPRCEYG SPGVLSYYQA
1010 1020 1030 1040 1050
HLTDIVQYPD AKTELFQSFR EFGNSIIFCL LIEQALSQEE VCDLLHAALF
1060 1070 1080 1090 1100
QNIFPRPFCK ENEKPEAKQK RLEAQFANLQ IVSNVEKIGT AKQAMIAREG
1110 1120 1130 1140 1150
DLLTRERLCC GLSIFEVILN RVKSYLDDPV WCGPPPANGI IHVDECSEFH
1160 1170 1180 1190 1200
RLWSALQFVY CIPVRGTEYT IEELFGEGLN WAGCVMIVLL GQQRRFEALD
1210 1220 1230 1240 1250
FCYHILRVQR VDGKDEDVKG IQLKRMVDRI RRFQVLNSQI FSILNKYLKG
1260 1270 1280 1290
GDGEGSNVEH VRCFPPPQHP SVISSSSHYQ DPQKLRQSIN N
Length:1,291
Mass (Da):149,261
Last modified:May 1, 2000 - v1
Checksum:iF3E4254BAD41015B
GO

Sequence cautioni

The sequence AAM52715.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY017343 mRNA. Translation: AAG61254.1.
AY029211 mRNA. Translation: AAK31584.1.
AE014297 Genomic DNA. Translation: AAF55173.1.
BT011115 mRNA. Translation: AAR82782.1.
AY122203 mRNA. Translation: AAM52715.1. Different initiation.
RefSeqiNP_650447.1. NM_142190.3.
UniGeneiDm.3506.

Genome annotation databases

EnsemblMetazoaiFBtr0083085; FBpp0082541; FBgn0038320.
GeneIDi41861.
KEGGidme:Dmel_CG4931.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY017343 mRNA. Translation: AAG61254.1.
AY029211 mRNA. Translation: AAK31584.1.
AE014297 Genomic DNA. Translation: AAF55173.1.
BT011115 mRNA. Translation: AAR82782.1.
AY122203 mRNA. Translation: AAM52715.1. Different initiation.
RefSeqiNP_650447.1. NM_142190.3.
UniGeneiDm.3506.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66924. 2 interactions.
DIPiDIP-33370N.
IntActiQ9VF87. 3 interactions.
MINTiMINT-252304.
STRINGi7227.FBpp0082541.

Proteomic databases

PaxDbiQ9VF87.
PRIDEiQ9VF87.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0083085; FBpp0082541; FBgn0038320.
GeneIDi41861.
KEGGidme:Dmel_CG4931.

Organism-specific databases

CTDi41861.
FlyBaseiFBgn0038320. Sra-1.

Phylogenomic databases

eggNOGiKOG3534. Eukaryota.
ENOG410XPKW. LUCA.
GeneTreeiENSGT00500000044831.
InParanoidiQ9VF87.
KOiK05749.
OMAiATNRFVK.
OrthoDBiEOG7ZSHS2.
PhylomeDBiQ9VF87.

Enzyme and pathway databases

ReactomeiR-DME-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DME-4420097. VEGFA-VEGFR2 Pathway.
R-DME-5663213. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

GenomeRNAii41861.
NextBioi825971.
PROiQ9VF87.

Gene expression databases

BgeeiQ9VF87.
GenevisibleiQ9VF87. DM.

Family and domain databases

InterProiIPR008081. Cytoplasmic_FMR1-int.
IPR009828. DUF1394.
[Graphical view]
PANTHERiPTHR12195. PTHR12195. 2 hits.
PfamiPF07159. DUF1394. 1 hit.
PF05994. FragX_IP. 1 hit.
[Graphical view]
PIRSFiPIRSF008153. FMR1_interacting. 1 hit.
PRINTSiPR01698. CYTOFMRPINTP.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A highly conserved protein family interacting with the fragile X mental retardation protein (FMRP) and displaying selective interactions with FMRP-related proteins FXR1P and FXR2P."
    Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.
    Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "DSra-1 is an effector for DRac1 during Drosophila embryogenesis."
    Langmann C., Harden N.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: BerkeleyImported.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1152.
    Strain: BerkeleyImported.
    Tissue: EmbryoImported.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-1291.
    Strain: BerkeleyImported.
    Tissue: EmbryoImported.
  7. "Abi, Sra1, and Kette control the stability and localization of SCAR/WAVE to regulate the formation of actin-based protrusions."
    Kunda P., Craig G., Dominguez V., Baum B.
    Curr. Biol. 13:1867-1875(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "CYFIP/Sra-1 controls neuronal connectivity in Drosophila and links the Rac1 GTPase pathway to the fragile X protein."
    Schenck A., Bardoni B., Langmann C., Harden N., Mandel J.-L., Giangrande A.
    Neuron 38:887-898(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FMR1 AND RAC1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  9. "WAVE/SCAR, a multifunctional complex coordinating different aspects of neuronal connectivity."
    Schenck A., Qurashi A., Carrera P., Bardoni B., Diebold C., Schejter E., Mandel J.-L., Giangrande A.
    Dev. Biol. 274:260-270(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COMPONENT OF WAVE COMPLEX.
  10. "Sra-1 interacts with Kette and Wasp and is required for neuronal and bristle development in Drosophila."
    Bogdan S., Grewe O., Strunk M., Mertens A., Klaembt C.
    Development 131:3981-3989(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HEM, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCYFIP_DROME
AccessioniPrimary (citable) accession number: Q9VF87
Secondary accession number(s): Q6NP16, Q8MR06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 102 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

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 one 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.