Reviewed, UniProtKB/Swiss-Prot Q9VM92 (TTL3B_DROME)

Names and origin

Protein names

Recommended name:
    Tubulin glycylase 3B
      Short name=dmTTLL3B
    EC=6.3.2.-

Gene names

Name:	TTLL3B
ORF Names:	CG11201

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

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	756 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential glycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates alpha-tubulin by adding a single glycine chain to generate monoglycine side chains, but is not involved in elongation step to generate polyglycine side chains on alpha-tubulin. Has the ability to both mono- and polyglycylate non-tubulin proteins such as up (Troponin T). Required for early steps of spermatogenesis. Ref.4
Subcellular location	Cytoplasm › cytoskeleton. Nucleus.
Sequence similarities	Contains 1 TTL domain.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	axoneme assembly Ref.4 Inferred from mutant phenotype. Source: UniProtKB cilium assembly Ref.4 Inferred from mutant phenotype. Source: UniProtKB protein polyglycylation Ref.4 Inferred from direct assay. Source: UniProtKB sperm individualization Ref.4 Inferred from mutant phenotype. Source: FlyBase
Cellular component	cilium axoneme Ref.4 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleus Ref.4 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct protein-glycine ligase activity, elongating Ref.4 Inferred from direct assay. Source: UniProtKB protein-glycine ligase activity, initiating Ref.4 Inferred from direct assay. Source: UniProtKB tubulin-tyrosine ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CG9232	Q9VMA2	1	EBI-137205,EBI-92316

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 756	756	Tubulin glycylase 3B		PRO_0000381796
Regions
	Domain	272 – 629	358	TTL
	Compositional bias	711 – 714	4	Poly-Lys

Sequences

	Sequence		Length	Mass (Da)
	Q9VM92-1 [UniParc]. Last modified March 3, 2009. Version 2. Checksum: 62BD02138F624E27	FASTA	756	86,109
	10 20 30 40 50 60 MTTQNTTPAG FTGNRNRYYN PVSKIQSLIH NLDAELVQLC KQCSVQKPLT SLNNSTSLGS 70 80 90 100 110 120 HFSNFGALGG GSGSKTMGGS SSMGSNNFSP DSIGNLLARV RASTPLPRTV TSSPTAPEAQ 130 140 150 160 170 180 KRQMRNVYRT RVIDAYRNRR IFTVYGNYHT VRRALMRRGW LEKLPASRHA KLQSMSEDAL 190 200 210 220 230 240 LEHARRGNDY EAVVISKMIN HFPAFFIWQG KGQRDLCAEV RPFRNRVRRS QFLDFSTKVG 250 260 270 280 290 300 LVGCAEQERW YREDGVCGMS YPRFYRLGGN NLEERMAFIE DYQQTQARSL LLYVREHQPA 310 320 330 340 350 360 ELISENGTIF STTLDFALGK VKKMVRHAEH YSLDDARIKP PTPAEIVENQ TFMVQSTDVL 370 380 390 400 410 420 KSNAKFKVSE KVMAEYARLA GLYLDQIESL RPDYRWDGSR NLWILKPGYQ SRGIGIVIRS 430 440 450 460 470 480 SLDDILQWTS NNQNKKYIVQ KYIERPLLIY RTKFDIRQYM LLTITDTKVS IWTYRDCYLR 490 500 510 520 530 540 FSSQEFTMDD LRESIHLTNN SVQKRYKNKT NRDSRLPKNN MWSLDQFKNY LRIMGAPDGS 550 560 570 580 590 600 WSKTYNGFKQ NLVAVVMASL DETELLQNAF ELYGCDFMLD EHYNPILIEI NSTPDLSPST 610 620 630 640 650 660 EITARICPMV LKDCIRVVVD LPKNPTAATG LFELAFEVNY SINKGADGKP LELNGKQMTL 670 680 690 700 710 720 FENMPRMRNS PRTRLLRKIL NNVKTSTTKK VEKVVEAPAK NVKNPTAKIT KKKKLSASAG 730 740 750 SSTAASAQPS TQNLTTKLIL NPATRENLAL QYTAPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	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 (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[4]	"Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation." Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C. Cell 137:1076-1087(2009) [PubMed: 19524510] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014134 Genomic DNA. Translation: AAF52431.2. BT021443 mRNA. Translation: AAX33591.1.
RefSeq	NP_609068.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VM92. 2 interactions.
Proteomic databases
PRIDE	Q9VM92.
Genome annotation databases
Ensembl	FBtr0300056; FBpp0289333; FBgn0031853; Drosophila melanogaster. [Genome view]
GeneID	33946.
KEGG	dme:Dmel_CG11201.
UCSC	CG11201-RB. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0031853. CG11201.
Phylogenomic databases
OrthoDB	EOG92NJ67
Gene expression databases
ArrayExpress	Q9VM92.
Bgee	Q9VM92.
Family and domain databases
InterPro	IPR004344. Tub_tyr_ligase. [Graphical view]
PANTHER	PTHR12241. Tub_tyr_ligase. 1 hit.
Pfam	PF03133. TTL. 1 hit. [Graphical view]
PROSITE	PS51221. TTL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TTL3B_DROME

Accession

Primary (citable) accession number: Q9VM92
Secondary accession number(s): Q5BHY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 1, 2009
Last sequence update:	March 3, 2009
Last modified:	November 24, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project