Q9U1K1 (SPIR_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein spire

Gene names

Name:	spir
Synonyms:	p150-Spir
ORF Names:	CG10076

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1020 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton. Ref.1 Ref.2 Ref.7 Ref.10 Ref.11
Subunit structure	Interacts with bsk, Rho1, Rac1, Cdc42 and wash. Interacts with capu. Ref.1 Ref.2 Ref.9 Ref.10
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › perinuclear region. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note: Punctate spots in perinuclear region and cytoplasm. Ref.2 Ref.10
Developmental stage	Expressed both maternally and zygotically. Ref.1
Domain	Binds to actin monomers via the WH2 domain. Ref.1 The Spir-box targets binding to intracellular membrane structures By similarity. UniProtKB Q08AE8
Post-translational modification	Phosphorylated by Jnk kinase (bsk). Ref.2
Disruption phenotype	Flies display premature microtubule-dependent cytoplasmic streaming; failure in the orientation of microtubule plus ends towards the posterior pole. Ref.1
Sequence similarities	Belongs to the spire family. Contains 1 KIND domain. Contains 2 WH2 domains.
RNA editing	Edited at position 734. Partially edited. Target of Adar. Ref.5 Ref.8

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing RNA editing
Domain	Repeat
Ligand	Actin-binding
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin nucleation Inferred from direct assay PubMed 16518391. Source: FlyBase chorion-containing eggshell formation Inferred from mutant phenotype PubMed 1783295. Source: FlyBase karyosome formation Inferred from mutant phenotype PubMed 15979065. Source: FlyBase pole plasm oskar mRNA localization Traceable author statement PubMed 11700288. Source: FlyBase protein transport Inferred from electronic annotation. Source: UniProtKB-KW vesicle-mediated transport Traceable author statement PubMed 12877999. Source: FlyBase
Cellular_component	cell cortex Inferred from direct assay PubMed 16518391. Source: FlyBase cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	actin binding Traceable author statement PubMed 11700288. Source: FlyBase microtubule binding Inferred from mutant phenotype PubMed 16518391. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
bsk	P92208	1	EBI-91672,EBI-74487
CG14579	Q9VRF5	1	EBI-91672,EBI-99956
sax	Q7JQ36	1	EBI-91672,EBI-121415

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform A Ref.2 (identifier: Q9U1K1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B Ref.1 (identifier: Q9U1K1-2)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     585-614: MEPAKQVPPPEEPSFTKDEYHKFYDTALES → T

Isoform C Ref.3 (identifier: Q9U1K1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     2-96: TEHQAEEQAD...EQCVTLHDIL → EARPAKRSTA...KPRQAIRSSK
     97-491: Missing.

Note: No experimental confirmation available.

Isoform D Ref.1 (identifier: Q9U1K1-4)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     338-338: Missing.
     585-586: ME → SI
     587-1020: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1020

1020

Protein spire

PRO_0000309573

Regions

Domain

90 – 327

238

KIND

Domain

399 – 417

19

WH2 1

Domain

463 – 480

18

WH2 2

Region

705 – 725

21

Spir-box

Compositional bias

205 – 220

16

His-rich

Compositional bias

792 – 877

86

Ser-rich

Natural variations

Alternative sequence

2 – 96

95

TEHQA…LHDIL → EARPAKRSTAASVFRSHHMP RESDLVDIGSDASLYCGSDG ESSQAQSTSTSTPNPQTSSD QDLDQPQPTPRAAPRASASN NPPTPKPRQAIRSSK in isoform C. Ref.3

VSP_052599

Alternative sequence

97 – 491

395

Missing in isoform C. Ref.3

VSP_052600

Alternative sequence

338

1

Missing in isoform D. Ref.1

VSP_052601

Alternative sequence

585 – 614

30

MEPAK…TALES → T in isoform B. Ref.1

VSP_052602

Alternative sequence

585 – 586

2

ME → SI in isoform D. Ref.1

VSP_052603

Alternative sequence

587 – 1020

434

Missing in isoform D. Ref.1

VSP_052604

Natural variant

734

1

K → R in RNA edited version. Ref.8

Experimental info

Mutagenesis

232

1

Y → K: Abolishes interaction with capu. Ref.10

Sequence conflict

53

1

L → M in AAF23615. Ref.1

Sequence conflict

53

1

L → M in AAF23616. Ref.1

Sequence conflict

885

1

V → A in AAF23615. Ref.1

Secondary structure

1

.

.

.

1020

Helix Strand Turn

Details...

Helix

463 – 473

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 010CD024F9ABC078	FASTA	1,020	114,867
	10 20 30 40 50 60 MTEHQAEEQA DTPPTKVKAT PTPTPSGKFK DAKEDAFLST SPDSANGDAQ HKLPADQLAM 70 80 90 100 110 120 SSSAHPQQAG QARPLILQAF HRCSSPEQCV TLHDILDSFK APLSEDQAWA LIHQFAGLYH 130 140 150 160 170 180 QVAVQAHTCA ADYEAALPTG FELHFHRDGS VHFSGPDQLT PKEQLQQEQI PLPPQHDVIV 190 200 210 220 230 240 DQPDHSASSS GDSSVINRAF DNSNHHHHHQ HHHPPLVVSH RKIISELAEI VYTALDYNLP 250 260 270 280 290 300 EDEECQVSQE LENLFNFMTA DETDDDCIDE GIDEGDKRWD DESEEERNDT KELEHIIETC 310 320 330 340 350 360 RNHIKTTLPE NHYRAVCRAL VTETIELRVF LQQVLNNEAG AEKLIKASES SATTQQELAK 370 380 390 400 410 420 LGFNDWARFW VQVIDELRRG VRLKKSNHER TPIEYELTPY EILMGDIRAK KYQLRKVMVN 430 440 450 460 470 480 GDIPPRVKKD AHAMILEFIR SRPPLKKASD RQLGPPRMCE PSPREQLMES IRKGKELKQI 490 500 510 520 530 540 TPPEAPTLRE RVLPSANSTL SRSRQRLIKV DFSKFQDDDL FYDENSISSS HSTAATHQHH 550 560 570 580 590 600 PHFAEMHRCS QPKMPPYPFG GYMVPSQARQ DCRETASLMR PRRTMEPAKQ VPPPEEPSFT 610 620 630 640 650 660 KDEYHKFYDT ALESYDLATQ CESRRASLRR HTIVGCQSNL DETHSMPPTR PESRQSDDVS 670 680 690 700 710 720 KETPKRSPAE QTHPSDEGSS TSSLGPWNKS FMDKQTWMER GDDRLSVTLA EIVHIRSVMT 730 740 750 760 770 780 KAELEGLPMD VRVKEDVEKR RVCFLCLRTR FSFFGPWGIQ CKLCQRTVCA KCYTKMRIPS 790 800 810 820 830 840 EHFRNVPLVL ISPSLLSSPA SSSTPSPSHH AQQAHSSSTG NIMDDQFPKS LIERLLRSES 850 860 870 880 890 900 DRKTRSTVGS APSSPKHQRS NMSTPGISVG PGASSSSAAA TGQAVEALHD QATMSSSYSA 910 920 930 940 950 960 AMRPSGVHQQ QKQHYNNAMS RSMEGPRSLP VHSPAYRPLS NNSTLERKSR FSRGFNLFSS 970 980 990 1000 1010 1020 GSHLAQTQEQ KENLRGEQVT VCNDCQGLVN EITSSVKQKR SSARNRTIQN LTLDLTPVWK
	Isoform B (Long) [UniParc]. Checksum: 5A39B9F07136E212	FASTA	991	111,475
	10 20 30 40 50 60 MTEHQAEEQA DTPPTKVKAT PTPTPSGKFK DAKEDAFLST SPDSANGDAQ HKLPADQLAM 70 80 90 100 110 120 SSSAHPQQAG QARPLILQAF HRCSSPEQCV TLHDILDSFK APLSEDQAWA LIHQFAGLYH 130 140 150 160 170 180 QVAVQAHTCA ADYEAALPTG FELHFHRDGS VHFSGPDQLT PKEQLQQEQI PLPPQHDVIV 190 200 210 220 230 240 DQPDHSASSS GDSSVINRAF DNSNHHHHHQ HHHPPLVVSH RKIISELAEI VYTALDYNLP 250 260 270 280 290 300 EDEECQVSQE LENLFNFMTA DETDDDCIDE GIDEGDKRWD DESEEERNDT KELEHIIETC 310 320 330 340 350 360 RNHIKTTLPE NHYRAVCRAL VTETIELRVF LQQVLNNEAG AEKLIKASES SATTQQELAK 370 380 390 400 410 420 LGFNDWARFW VQVIDELRRG VRLKKSNHER TPIEYELTPY EILMGDIRAK KYQLRKVMVN 430 440 450 460 470 480 GDIPPRVKKD AHAMILEFIR SRPPLKKASD RQLGPPRMCE PSPREQLMES IRKGKELKQI 490 500 510 520 530 540 TPPEAPTLRE RVLPSANSTL SRSRQRLIKV DFSKFQDDDL FYDENSISSS HSTAATHQHH 550 560 570 580 590 600 PHFAEMHRCS QPKMPPYPFG GYMVPSQARQ DCRETASLMR PRRTTYDLAT QCESRRASLR 610 620 630 640 650 660 RHTIVGCQSN LDETHSMPPT RPESRQSDDV SKETPKRSPA EQTHPSDEGS STSSLGPWNK 670 680 690 700 710 720 SFMDKQTWME RGDDRLSVTL AEIVHIRSVM TKAELEGLPM DVRVKEDVEK RRVCFLCLRT 730 740 750 760 770 780 RFSFFGPWGI QCKLCQRTVC AKCYTKMRIP SEHFRNVPLV LISPSLLSSP ASSSTPSPSH 790 800 810 820 830 840 HAQQAHSSST GNIMDDQFPK SLIERLLRSE SDRKTRSTVG SAPSSPKHQR SNMSTPGISV 850 860 870 880 890 900 GPGASSSSAA ATGQAVEALH DQATMSSSYS AAMRPSGVHQ QQKQHYNNAM SRSMEGPRSL 910 920 930 940 950 960 PVHSPAYRPL SNNSTLERKS RFSRGFNLFS SGSHLAQTQE QKENLRGEQV TVCNDCQGLV 970 980 990 NEITSSVKQK RSSARNRTIQ NLTLDLTPVW K
	Isoform C [UniParc]. Checksum: 6B020E5746568D77	FASTA	625	69,401
	10 20 30 40 50 60 MEARPAKRST AASVFRSHHM PRESDLVDIG SDASLYCGSD GESSQAQSTS TSTPNPQTSS 70 80 90 100 110 120 DQDLDQPQPT PRAAPRASAS NNPPTPKPRQ AIRSSKVLPS ANSTLSRSRQ RLIKVDFSKF 130 140 150 160 170 180 QDDDLFYDEN SISSSHSTAA THQHHPHFAE MHRCSQPKMP PYPFGGYMVP SQARQDCRET 190 200 210 220 230 240 ASLMRPRRTM EPAKQVPPPE EPSFTKDEYH KFYDTALESY DLATQCESRR ASLRRHTIVG 250 260 270 280 290 300 CQSNLDETHS MPPTRPESRQ SDDVSKETPK RSPAEQTHPS DEGSSTSSLG PWNKSFMDKQ 310 320 330 340 350 360 TWMERGDDRL SVTLAEIVHI RSVMTKAELE GLPMDVRVKE DVEKRRVCFL CLRTRFSFFG 370 380 390 400 410 420 PWGIQCKLCQ RTVCAKCYTK MRIPSEHFRN VPLVLISPSL LSSPASSSTP SPSHHAQQAH 430 440 450 460 470 480 SSSTGNIMDD QFPKSLIERL LRSESDRKTR STVGSAPSSP KHQRSNMSTP GISVGPGASS 490 500 510 520 530 540 SSAAATGQAV EALHDQATMS SSYSAAMRPS GVHQQQKQHY NNAMSRSMEG PRSLPVHSPA 550 560 570 580 590 600 YRPLSNNSTL ERKSRFSRGF NLFSSGSHLA QTQEQKENLR GEQVTVCNDC QGLVNEITSS 610 620 VKQKRSSARN RTIQNLTLDL TPVWK
	Isoform D (Short) [UniParc]. Checksum: 8F2F09E9AB96CF7F	FASTA	585	66,418
	10 20 30 40 50 60 MTEHQAEEQA DTPPTKVKAT PTPTPSGKFK DAKEDAFLST SPDSANGDAQ HKLPADQLAM 70 80 90 100 110 120 SSSAHPQQAG QARPLILQAF HRCSSPEQCV TLHDILDSFK APLSEDQAWA LIHQFAGLYH 130 140 150 160 170 180 QVAVQAHTCA ADYEAALPTG FELHFHRDGS VHFSGPDQLT PKEQLQQEQI PLPPQHDVIV 190 200 210 220 230 240 DQPDHSASSS GDSSVINRAF DNSNHHHHHQ HHHPPLVVSH RKIISELAEI VYTALDYNLP 250 260 270 280 290 300 EDEECQVSQE LENLFNFMTA DETDDDCIDE GIDEGDKRWD DESEEERNDT KELEHIIETC 310 320 330 340 350 360 RNHIKTTLPE NHYRAVCRAL VTETIELRVF LQQVLNNAGA EKLIKASESS ATTQQELAKL 370 380 390 400 410 420 GFNDWARFWV QVIDELRRGV RLKKSNHERT PIEYELTPYE ILMGDIRAKK YQLRKVMVNG 430 440 450 460 470 480 DIPPRVKKDA HAMILEFIRS RPPLKKASDR QLGPPRMCEP SPREQLMESI RKGKELKQIT 490 500 510 520 530 540 PPEAPTLRER VLPSANSTLS RSRQRLIKVD FSKFQDDDLF YDENSISSSH STAATHQHHP 550 560 570 580 HFAEMHRCSQ PKMPPYPFGG YMVPSQARQD CRETASLMRP RRTSI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Spire contains actin binding domains and is related to ascidian posterior end mark-5." Wellington A., Emmons S., James B., Calley J., Grover M., Tolias P., Manseau L. Development 126:5267-5274(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND D), FUNCTION, INTERACTION WITH RHO1; RAC1 AND CDC42, DEVELOPMENTAL STAGE, ACTIN-BINDING, DISRUPTION PHENOTYPE. Tissue: Ovary.
[2]	"The p150-Spir protein provides a link between c-Jun N-terminal kinase function and actin reorganization." Otto I.M., Raabe T., Rennefahrt U.E.E., Bork P., Rapp U.R., Kerkhoff E. Curr. Biol. 10:345-348(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH BSK, SUBCELLULAR LOCATION, PHOSPHORYLATION. Tissue: Embryo.
[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: 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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND D), RNA EDITING OF POSITION 734. Strain: Berkeley. Tissue: Embryo and Head.
[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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-1020 (ISOFORM B). Strain: Berkeley. Tissue: Embryo.
[7]	"Drosophila Spire is an actin nucleation factor." Quinlan M.E., Heuser J.E., Kerkhoff E., Mullins R.D. Nature 433:382-388(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"RNA editing in Drosophila melanogaster: new targets and functional consequences." Stapleton M., Carlson J.W., Celniker S.E. RNA 12:1922-1932(2006) [PubMed] [Europe PMC] [Abstract] Cited for: RNA EDITING OF POSITION 734.
[9]	"Wash functions downstream of Rho and links linear and branched actin nucleation factors." Liu R., Abreu-Blanco M.T., Barry K.C., Linardopoulou E.V., Osborn G.E., Parkhurst S.M. Development 136:2849-2860(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WASH.
[10]	"Structure and function of the interacting domains of Spire and Fmn-family formins." Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W., Quinlan M.E., Eck M.J. Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CAPU, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-232.
[11]	"Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation." Ducka A.M., Joel P., Popowicz G.M., Trybus K.M., Schleicher M., Noegel A.A., Huber R., Holak T.A., Sitar T. Proc. Natl. Acad. Sci. U.S.A. 107:11757-11762(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 448-485 IN COMPLEX WITH ACTIN, FUNCTION.
[12]	"Multiple forms of Spire-actin complexes and their functional consequences." Chen C.K., Sawaya M.R., Phillips M.L., Reisler E., Quinlan M.E. J. Biol. Chem. 287:10684-10692(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 428-485 IN COMPLEX WITH ACTIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF184975 mRNA. Translation: AAF23615.1.
AF184976 mRNA. Translation: AAF23616.1.
AJ238876 mRNA. Translation: CAB62901.1.
AE014134 Genomic DNA. Translation: AAF53884.2.
AE014134 Genomic DNA. Translation: AAN11070.1.
AE014134 Genomic DNA. Translation: AAN11071.1.
AE014134 Genomic DNA. Translation: AAN11072.2.
AY075586 mRNA. Translation: AAL68390.1.
AY089503 mRNA. Translation: AAL90241.1.
BT016094 mRNA. Translation: AAV36979.1.

RefSeq

NP_001246102.1. NM_001259173.1.
NP_524854.2. NM_080115.3.
NP_724254.1. NM_165323.2.
NP_724255.1. NM_165324.2.
NP_724256.2. NM_165325.2.

UniGene

Dm.3356.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MN5	X-ray	1.50	S	448-485	[»]
3MN7	X-ray	2.00	S	441-479	[»]
3UE5	X-ray	2.76	B	428-485	[»]
4EFH	X-ray	2.48	B	428-485	[»]

ProteinModelPortal

Q9U1K1.

SMR

Q9U1K1. Positions 222-331.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17301N.

IntAct

Q9U1K1. 3 interactions.

MINT

MINT-295231.

Proteomic databases

PaxDb

Q9U1K1.

PRIDE

Q9U1K1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0081352; FBpp0080884; FBgn0003475.

GeneID

45931.

KEGG

dme:Dmel_CG10076.

UCSC

CG10076-RA. d. melanogaster.

Organism-specific databases

CTD

45931.

FlyBase

FBgn0003475. spir.

Phylogenomic databases

eggNOG

NOG69783.

GeneTree

ENSGT00390000003058.

InParanoid

Q9U1K1.

KO

K02098.

OMA

WALIYQF.

OrthoDB

EOG44TMQP.

PhylomeDB

Q9U1K1.

Gene expression databases

Bgee

Q9U1K1.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR011019. KIND.
IPR003124. WH2_dom.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

SMART

SM00750. KIND. 1 hit.
SM00246. WH2. 2 hits.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS51377. KIND. 1 hit.
PS51082. WH2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

spir. drosophila.

EvolutionaryTrace

Q9U1K1.

GenomeRNAi

45931.

NextBio

838510.

Entry information

Entry name

SPIR_DROME

Accession

Primary (citable) accession number: Q9U1K1
Secondary accession number(s): Q5U0Z8 , Q8INV3, Q8INV4, Q8INV5, Q8SXP3, Q8T8P8, Q9U4F0, Q9U4F1, Q9VIN3, Q9VIN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project