Q9XYP8 (GCP3_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gamma-tubulin complex component 3 homolog

Alternative name(s):
Gamma-ring complex protein 91 kDa
Short name=d91p
Short name=dGrip91

Gene names

Name:	l(1)dd4
ORF Names:	CG10988

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

General annotation (Comments)

Subunit structure	Gamma-tubulin small complex (Gamma TuSC) is a heterotetrameric complex which contains two molecules of gamma-tubulin, and one molecule each of Dgrip84 and Dgrip91. The gamma-tubulin in this complex binds preferentially to GDP over GTP.
Subcellular location	Cytoplasm › cytoskeleton › centrosome Potential.
Sequence similarities	Belongs to the GCP family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	anaphase Inferred from mutant phenotype. Source: FlyBase centrosome organization Inferred from mutant phenotype. Source: FlyBase meiosis I Inferred from mutant phenotype. Source: FlyBase microtubule nucleation Inferred from direct assay Ref.1. Source: UniProtKB mitotic spindle organization Inferred from mutant phenotype. Source: FlyBase
Cellular component	gamma-tubulin small complex Inferred from direct assay Ref.1. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW spindle pole Inferred from electronic annotation. Source: InterPro
Molecular function	gamma-tubulin binding Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 917	917	Gamma-tubulin complex component 3 homolog		PRO_0000078121
Experimental info
	Sequence conflict	79	1	N → Y in AAD27817. Ref.1
	Sequence conflict	118	1	M → I in AAD27817. Ref.1
	Sequence conflict	413	1	L → F in AAD27817. Ref.1
	Sequence conflict	479	1	L → F in AAD27817. Ref.1
	Sequence conflict	583	1	G → A in AAD27817. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9XYP8 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: 6AEE88C211D256BB	FASTA	917	103,707
	10 20 30 40 50 60 MSQDRIAGID VATNSTDISN IINEMIICIK GKQMPEVHEK AMDHLSKMIA ANSRVIRDSN 70 80 90 100 110 120 MLTERECVQK IMKLLSARNK KEEGKTVSDH FNELYRKLTL TKCDPHMRHS LMTHLLTMTD 130 140 150 160 170 180 NSDAEKAVAS EDPRTQCDNL TQILVSRLNS ISSSIASLNE MGVVNGNGVG AAAVTGAAAV 190 200 210 220 230 240 TGAAAVTGAA AVTGAAASHS YDATQSSIGL RKQSLPNYLD ATKMLPESRH DIVMSAIYSF 250 260 270 280 290 300 TGVQGKYLKK DVVTGRFKLD QQNIKFLTTG QAGMLLRLSE LGYYHDRVVK FSDVSTGFNA 310 320 330 340 350 360 IGSMGQALIS KLKEELANFH GQVAMLHDEM QRFRQASVNG IANKGKKDSG PDAGDEMTLF 370 380 390 400 410 420 KLLAWYIKPL HRMQWLTKIA DACQVKKGGD LASTVYDFLD NGNDMVNKLV EDLLTAICGP 430 440 450 460 470 480 LVRMISKWIL EGGISDMHRE FFVKSIKDVG VDRLWHDKFR LRLPMLPKFV PMDMANKILM 490 500 510 520 530 540 TGKSINFLRE ICEEQGMMKE RDELMKVMES SASQIFSYTP DTSWHAAVET CYQQTSKHVL 550 560 570 580 590 600 DIMVGPHKLL DHLHGMRRYL LLGQGDFISI LIENMKNELE RPGLDIYAND LTSMLDSALR 610 620 630 640 650 660 CTNAQYDDPD ILNHLDVIVQ RPFNGDIGWN IISLQYIVHG PLAAMLESTM PTYKVLFKPL 670 680 690 700 710 720 WRMKHMEFVL SMKIWKEQMG NAKALRTMKS EIGKASHRLN LFTSEIMHFI HQMQYYVLFE 730 740 750 760 770 780 VIECNWVELQ KKMQKATTLD EILEAHEKFL QTILVGCFVS NKASVEHSLE VVYENIIELE 790 800 810 820 830 840 KWQSSFYKDC FKELNARKEL SKIVEKSEKK GVYGLTNKMI LQRDQEAKIF AEKMDIACRG 850 860 870 880 890 900 LEVIATDYEK AVSTFLMSLN SSDDPNLQLF GTRLDFNEYY KKRDTNLSKP LTFEHMRMSN 910 VFAVNSRFVI CTPSTQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of two related Drosophila gamma-tubulin complexes that differ in their ability to nucleate microtubules." Oegema K., Wiese C., Martin O.C., Milligan R.A., Iwamatsu A., Mitchison T.J., Zheng Y. J. Cell Biol. 144:721-733(1999) [PubMed: 10037793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-36; 85-90; 202-227; 250-257; 277-302; 541-548; 616-626; 664-671; 799-804; 810-817 AND 863-880.
[2]	"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.
[3]	"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.
[4]	"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: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF118380 mRNA. Translation: AAD27817.1. AE014298 Genomic DNA. Translation: AAF48309.1. AY069292 mRNA. Translation: AAL39437.1.
RefSeq	NP_524919.2. NM_080180.3.
3D structure databases
ProteinModelPortal	Q9XYP8.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-19100N.
IntAct	Q9XYP8. 1 interaction.
MINT	MINT-864294.
STRING	Q9XYP8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0073841; FBpp0073672; FBgn0001612.
GeneID	48481.
KEGG	dme:Dmel_CG10988.
NMPDR	fig|7227.3.peg.17744.
Organism-specific databases
FlyBase	FBgn0001612. l(1)dd4.
Phylogenomic databases
eggNOG	inNOG08234.
GeneTree	EMGT00050000005230.
InParanoid	Q9XYP8.
OMA	TRPRREG.
OrthoDB	EOG44QRG1.
PhylomeDB	Q9XYP8.
Gene expression databases
ArrayExpress	Q9XYP8.
Bgee	Q9XYP8.
GermOnline	CG10988. Drosophila melanogaster.
Family and domain databases
InterPro	IPR015697. GCP3. IPR007259. Spc97_Spc98. [Graphical view]
PANTHER	PTHR19302:SF14. GCP3. 1 hit. PTHR19302. Spc97_Spc98. 1 hit.
Pfam	PF04130. Spc97_Spc98. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	839436.

Entry information

Entry name

GCP3_DROME

Accession

Primary (citable) accession number: Q9XYP8
Secondary accession number(s): Q9VY94

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	June 6, 2002
Last modified:	January 25, 2012
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project