Q07436 (EXPA_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein expanded

Gene names

Name:	ex
ORF Names:	CG4114

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	1427 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. Ex acts synergistically along with Mer and Kibra to regulate the Hippo signaling pathway. Involved in the control of cell proliferation in imaginal disks. May bind to certain proteins of signal transduction pathways by interaction with their SH3 domains. Ref.7
Subunit structure	Forms a complex with Kibra and Mer. Interacts (via RXPPXY motif) with Kibra (via domain WW 1). Interacts with Mer and Hpo (via SARAH domain). Ref.7
Subcellular location	Apical cell membrane. Note: Apical surface of disk cells. Ref.7
Disruption phenotype	Hyperplasmia of the imaginal disk resulting in wing overgrowth. This overgrowth is limited to specific regions along the 2 wing axs. Defects also in eyes, head, thorax and limbs where duplication and bulging often occur. Ref.1
Sequence similarities	Contains 1 FERM domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cell membrane Membrane
Domain	SH3-binding
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle arrest Inferred from genetic interaction. Source: FlyBase compound eye photoreceptor cell differentiation Inferred from mutant phenotype. Source: FlyBase decapentaplegic signaling pathway Inferred from genetic interaction. Source: FlyBase endocytic recycling Inferred from genetic interaction. Source: FlyBase hippo signaling cascade Inferred from genetic interaction. Source: FlyBase negative regulation of cell proliferation Inferred from mutant phenotype. Source: FlyBase negative regulation of imaginal disc growth Inferred from mutant phenotype. Source: FlyBase positive regulation of phosphorylation Inferred from genetic interaction. Source: FlyBase regulation of apoptotic process Inferred from genetic interaction. Source: FlyBase regulation of cell differentiation Inferred from genetic interaction. Source: FlyBase regulation of exit from mitosis Inferred from mutant phenotype. Source: FlyBase regulation of hippo signaling cascade Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apical plasma membrane Inferred from direct assay. Source: FlyBase cytoskeleton Inferred from electronic annotation. Source: InterPro zonula adherens Traceable author statement. Source: FlyBase
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1427	1427	Protein expanded		PRO_0000219443
Regions
	Domain	26 – 399	374	FERM
	Motif	842 – 847	6	RXPPXY motif
	Motif	1008 – 1020	13	SH3-binding Potential
	Motif	1149 – 1157	9	SH3-binding Potential
	Compositional bias	409 – 412	4	Poly-Glu
	Compositional bias	782 – 788	7	Poly-Pro
	Compositional bias	952 – 955	4	Poly-His
	Compositional bias	1002 – 1005	4	Poly-Pro
	Compositional bias	1011 – 1017	7	Poly-Pro
	Compositional bias	1081 – 1084	4	Poly-Pro
	Compositional bias	1149 – 1154	6	Poly-Pro
	Compositional bias	1158 – 1168	11	Poly-Ala
	Compositional bias	1170 – 1174	5	Poly-Ser
	Compositional bias	1199 – 1205	7	Poly-Pro
	Compositional bias	1416 – 1422	7	Poly-Gln
Amino acid modifications
	Modified residue	1181	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	160 – 161	2	EQ → DE in AAB39774. Ref.1
	Sequence conflict	194	1	S → L in AAB39774. Ref.1
	Sequence conflict	347	1	F → S in AAB39774. Ref.1
	Sequence conflict	563	1	I → T in AAB39774. Ref.1
	Sequence conflict	671	1	A → D in AAB39774. Ref.1
	Sequence conflict	693	1	Q → S in AAB39774. Ref.1
	Sequence conflict	1293 – 1294	2	SM → FN in AAB39774. Ref.1
	Sequence conflict	1422	1	Q → QQQ in AAB39774. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q07436 [UniParc]. Last modified June 21, 2005. Version 3. Checksum: 3CC1AD0B4D900EB2	FASTA	1,427	153,644
	10 20 30 40 50 60 MRAFCTVSAP LEVCASSAEQ LSPGSRFLAL RLLGQQQPKT LYFLVDAKSR VREVYTQTCL 70 80 90 100 110 120 HFATQGMLDT ELFGLAVLID GEYMFADPES KLSKYGPKSW RSSHTHGLDA NGRPLLELHF 130 140 150 160 170 180 RVQFYIESPF MLKDETSRHN YYLQLRHNIL QRDLPREQAE QALVFLAGLA LQADLGDAPP 190 200 210 220 230 240 GTSNSKDDSG EETSASPSNG GRGLSATTTL PKISKRANER MLRLSTYVAS TSKRETIPLP 250 260 270 280 290 300 PSLPPNGADY YRIEDYLPSG LHTPWARSAM RACHREHLGM ATAEAELLYI QQACSLHETI 310 320 330 340 350 360 NAHTYRMRLA KSEQGSGSAW FVVYAKGIKI LGGESTNSSS NPETTTFLWP NITKLSFERK 370 380 390 400 410 420 KFEIRSGESR ITLYAASDEK NKLLLTLCKD THQWSMKLAA RLKEVSKREE EEAAESQRLH 430 440 450 460 470 480 ASYACSRSLL LPYKSKNEQR ISVISSTSSN TTSGIVSDRV HSEDELEIMI NTPPAPLAAP 490 500 510 520 530 540 STESLALAHL LDRPSVSRQT SSVGQMSLKD LEEQLAALSV RPQDASSNGA TIVTNSSVQR 550 560 570 580 590 600 NSMGTTANDS STATDSPSSQ HNIGSQCSST CSTVVVTSPV NGAGASSSGA PIPVHSTSSS 610 620 630 640 650 660 LELGFSHTAQ NSALSETSPD DFLSTSAREE TESVSGASGV YTLAHGAPPT ETSGVYTMHS 670 680 690 700 710 720 SELTGQSSEI AESEKSSHYG MFQPQKLEET HVQHSDSVDG KKKEDFRPRS DSNVSTGSSF 730 740 750 760 770 780 RGDGSDPTDN KHSLLSAEEL TNLIVGRGTY PSRKTVSSSL HSDCDYVTLP LGDQGEEEVD 790 800 810 820 830 840 QPPAPPPPYS ARHEKTGLCG PPIAKPIPKP IAVVAPKPDS PPCSPPVPPA PIPAPPPAIR 850 860 870 880 890 900 RRDPPPYSIS SKPRPTSLIS VSSSAHPAPS AAGSMSSLKS EEVTARFITT RPQISILKAH 910 920 930 940 950 960 TSLIPDGAKP SYAAPHHCSS VASSNGSVCS HQLSQQSLHN SNYAGGSQAS LHHHHVPSHH 970 980 990 1000 1010 1020 RHSGSAAIGI VPYGLHKSTA SLHHQQSCVL LPVIKPRQFL APPPPSLPRQ PPPPPPPNHP 1030 1040 1050 1060 1070 1080 HLASHLYERE MARKQLELYQ QQLYSDVDYV IYPIQDPAVS QQEYLDAKQG SLLAAMAQAA 1090 1100 1110 1120 1130 1140 PPPPHHPYLA MQVSPAIYRS TPYLPLTLST HSRYASTQNL SDTYVQLPGP GYSPLYSPSM 1150 1160 1170 1180 1190 1200 ASLCSSYEPP PPPPLHPAAL AAAAAAGAGS SSSSMFARSR SDDNILNSLD LLPKGKRLPP 1210 1220 1230 1240 1250 1260 PPPPPYVNRR LKKPPMPAPS EKPPPIPSKP IPSRMSPIPP RKPPTLNPHH ANSPLTKTSS 1270 1280 1290 1300 1310 1320 GAQWAGERPR PDLGLGLGLN RGNNSILAQL QASMVAQSHA QAQAQALDIA LLREKSKHLD 1330 1340 1350 1360 1370 1380 LPLISALCND RSLLKQTKVV INPKTGQEMP TSSAQPSGAT TNGVANSSAG AGTLSKARKG 1390 1400 1410 1420 STVSHRHPQD KLPPLPVQQL AEANNYVIDP AVMMKQQQQQ QQHNKTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expanded: a gene involved in the control of cell proliferation in imaginal discs." Boedigheimer M., Laughon A. Development 118:1291-1301(1993) [PubMed: 8269855] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE. Tissue: Imaginal disk.
[2]	Boedigheimer M. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[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]	"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]. Strain: Berkeley. Tissue: Head.
[6]	"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-1181, MASS SPECTROMETRY. Tissue: Embryo.
[7]	"Kibra functions as a tumor suppressor protein that regulates Hippo signaling in conjunction with Merlin and Expanded." Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D. Dev. Cell 18:288-299(2010) [PubMed: 20159598] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIBRA; MER AND HPO.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L14768 mRNA. Translation: AAB39774.1. AE014134 Genomic DNA. Translation: AAF51495.1. AY069068 mRNA. Translation: AAL39213.1.
PIR	T13720.
RefSeq	NP_476840.2. NM_057492.3.
UniGene	Dm.247.
3D structure databases
ProteinModelPortal	Q07436.
ModBase	Search...
Protein-protein interaction databases
STRING	Q07436.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0078059; FBpp0077719; FBgn0004583.
GeneID	33218.
KEGG	dme:Dmel_CG4114.
NMPDR	fig|7227.3.peg.98.
UCSC	CG4114-RA. d. melanogaster.
Organism-specific databases
CTD	110023.
FlyBase	FBgn0004583. ex.
Phylogenomic databases
eggNOG	inNOG05687.
GeneTree	EMGT00050000000169.
InParanoid	Q07436.
OMA	WRSSHTH.
OrthoDB	EOG44TMPQ.
PhylomeDB	Q07436.
Gene expression databases
Bgee	Q07436.
GermOnline	CG4114. Drosophila melanogaster.
Family and domain databases
InterPro	IPR019749. Band_41_domain. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR000299. FERM_domain. IPR018980. FERM_PH-like_C. IPR011993. PH_type. [Graphical view]
Gene3D	G3DSA:1.20.80.10. ACBP. 2 hits. G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF09380. FERM_C. 1 hit. PF00373. FERM_M. 1 hit. [Graphical view]
SMART	SM00295. B41. 1 hit. [Graphical view]
SUPFAM	SSF47031. FERM_3-hlx. 1 hit.
PROSITE	PS00660. FERM_1. False negative. PS00661. FERM_2. False negative. PS50057. FERM_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	782491.

Entry information

Entry name

EXPA_DROME

Accession

Primary (citable) accession number: Q07436
Secondary accession number(s): Q9VPQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	June 21, 2005
Last modified:	January 25, 2012
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project