Q9VF87 (CYFIP_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytoplasmic FMR1-interacting protein

Alternative name(s):
Specifically Rac1-associated protein 1
Short name=DSra-1

Gene names

Name:	Sra-1
Synonyms:	Cyfip
ORF Names:	CG4931

Organism

Drosophila melanogaster (Fruit fly)

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	1291 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.8 Ref.9 Ref.10
Subunit structure	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. Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm. Note: Accumulates in central axons and motor neuron terminals. Ref.8
Tissue specificity	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. Ref.8 Ref.10
Developmental stage	Expressed throughout the life cycle with no major peaks of expression. In the embryo, uniquitously and highly expressed at precellular and cellular blastoderm stages. Ref.8
Disruption phenotype	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. Ref.7 Ref.8 Ref.10
Sequence similarities	Belongs to the CYFIP family.
Sequence caution	The sequence AAM52715.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell shape Differentiation Neurogenesis
Cellular component	Cytoplasm
Molecular function	Developmental protein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Inferred from mutant phenotype Ref.8. Source: FlyBase cell projection assembly Inferred from mutant phenotype Ref.7. Source: FlyBase chaeta development Inferred from mutant phenotype Ref.10. Source: UniProtKB cortical actin cytoskeleton organization Inferred from mutant phenotype Ref.7. Source: FlyBase phagocytosis, engulfment Inferred from mutant phenotype. Source: FlyBase regulation of cell shape Inferred from mutant phenotype Ref.7. Source: FlyBase regulation of synapse organization Inferred from mutant phenotype Ref.8. Source: FlyBase
Cellular component	SCAR complex Inferred from direct assay Ref.9. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Nap1	Q24150	2	EBI-116862,EBI-603430

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1291	1291	Cytoplasmic FMR1-interacting protein		PRO_0000279714

Sequences

	Sequence		Length	Mass (Da)
	Q9VF87 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: F3E4254BAD41015B	FASTA	1,291	149,261
	10 20 30 40 50 60 MTEKITLADA LSNVEVLDEL SLPDEQPCIE AQPCSIIYKA NFDTNFEDRN GFVTGIAKYI 70 80 90 100 110 120 EEATTHANLN VLLDEGQKHA VMLYTWRCCS RAIPQPKSNE QPNRVEIYEK TVEVLAPEVN 130 140 150 160 170 180 KLLNFMYFQR KAIEAFSGEV KRLCHAEKRK DFVSEAYLLT LGKFINMFAV LDELKNMKSS 190 200 210 220 230 240 VKNDYSTYRR AAQFLKVMSD SHTLQESQNL SMFLATQNKI RDTVKDTLEK IVGYEDLLSD 250 260 270 280 290 300 VVNICVHMFE TKMYLTPEEK HMLVKVMGFG LFLMDSDACN INKLDQKKKI RLDRIDRIFK 310 320 330 340 350 360 NLEVVPLFGD MQIAPFNYIK RSKHFDSSKW PLSSSNAISP QADLMVHLPQ IREDHVKYIS 370 380 390 400 410 420 ELARYTNEVT TTVKENPSDA ENRITADLAL RGLQLLSEWT SVVTELYSWK LLHPTDHHQN 430 440 450 460 470 480 KECPVEAEEY ERATRYNYTS EEKFALIEVI AMIKGLQVLM ARIETVLCEA IRRNIYSELQ 490 500 510 520 530 540 DFVQLSLREP LRKAVKNKKD LIRSIIMSVR ETSADWQKGY EPTDDPVAKG KKDPDGGFRI 550 560 570 580 590 600 QVPRLNVGPS STQLYMVRTM LESLIADKSG GKRTLRKDID GNCLLQIDTF HKTSFYWSYL 610 620 630 640 650 660 LNFSDTLQKC CDLSQLWYRE FYLEMTMGRK VNKCLVRHQH NEECKDLITM EKRIQFPIEM 670 680 690 700 710 720 SMPWILTDHI LQTKEPSMME FVLYPLDLYN DSAYYALTVF RKQFLYDEVE AEVNLCFDQF 730 740 750 760 770 780 VYKLSEQIFA HYKQLAGSIF LDKRFRLECE VLGFNFQSYP RNNRYETLLK QRHVQLLGRS 790 800 810 820 830 840 IDLNKLITQR INANMHKSIE LAISRFEGND ITGIVELEGL LEANRICHKL LSKYLALDNF 850 860 870 880 890 900 DGMVKEANHN VLAPYGRITL HVFVELNYDF LVNYCYNAAT NRFIRTKVNL SSSQAIQREK 910 920 930 940 950 960 PPQMSHYYLW GSKQLNAAYS TQYGQYTGFV GSPHFHAMCR LLGYQGIAVV MDIILKDIVK 970 980 990 1000 1010 1020 PLIQGSLLQF TKTLMIAMPK SCKLPRCEYG SPGVLSYYQA HLTDIVQYPD AKTELFQSFR 1030 1040 1050 1060 1070 1080 EFGNSIIFCL LIEQALSQEE VCDLLHAALF QNIFPRPFCK ENEKPEAKQK RLEAQFANLQ 1090 1100 1110 1120 1130 1140 IVSNVEKIGT AKQAMIAREG DLLTRERLCC GLSIFEVILN RVKSYLDDPV WCGPPPANGI 1150 1160 1170 1180 1190 1200 IHVDECSEFH RLWSALQFVY CIPVRGTEYT IEELFGEGLN WAGCVMIVLL GQQRRFEALD 1210 1220 1230 1240 1250 1260 FCYHILRVQR VDGKDEDVKG IQLKRMVDRI RRFQVLNSQI FSILNKYLKG GDGEGSNVEH 1270 1280 1290 VRCFPPPQHP SVISSSSHYQ DPQKLRQSIN N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11438699] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"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: GENOME REANNOTATION. Strain: Berkeley.
[5]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1152. Strain: Berkeley. Tissue: Embryo.
[6]	"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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-1291. Strain: Berkeley. Tissue: Embryo.
[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: 14588242] [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: 12818175] [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: 15385157] [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: 15269173] [Abstract] Cited for: FUNCTION, INTERACTION WITH HEM, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
RefSeq	NP_650447.1. NM_142190.2.
UniGene	Dm.3506.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-33370N.
IntAct	Q9VF87. 1 interaction.
MINT	MINT-252304.
STRING	Q9VF87.
Proteomic databases
PRIDE	Q9VF87.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0083085; FBpp0082541; FBgn0038320.
GeneID	41861.
KEGG	dme:Dmel_CG4931.
NMPDR	fig|7227.3.peg.12961.
Organism-specific databases
CTD	41861.
FlyBase	FBgn0038320. Sra-1.
Phylogenomic databases
eggNOG	inNOG04619.
GeneTree	EMGT00050000016790.
InParanoid	Q9VF87.
OMA	EFHKQSF.
OrthoDB	EOG4905QS.
PhylomeDB	Q9VF87.
Gene expression databases
Bgee	Q9VF87.
Family and domain databases
InterPro	IPR008081. Cytoplasmic_FMR1-int. IPR016536. Cytoplasmic_FMR1-int_sub. IPR009828. DUF1394. [Graphical view]
KO	K05749.
PANTHER	PTHR12195. FragX_IP. 1 hit.
Pfam	PF07159. DUF1394. 1 hit. PF05994. FragX_IP. 1 hit. [Graphical view]
PIRSF	PIRSF008153. FMR1_interacting. 1 hit.
PRINTS	PR01698. CYTOFMRPINTP.
ProtoNet	Search...
Other
NextBio	825971.

Entry information

Entry name

CYFIP_DROME

Accession

Primary (citable) accession number: Q9VF87
Secondary accession number(s): Q6NP16, Q8MR06

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project