Q9VM92 (TTL3B_DROME) Reviewed, UniProtKB/Swiss-Prot

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)

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.
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 Ref.4.
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 Reference proteome
Gene Ontology (GO)
Biological process	axoneme assembly Inferred from mutant phenotype Ref.4. Source: UniProtKB cilium assembly Inferred from mutant phenotype Ref.4. Source: UniProtKB protein polyglycylation Inferred from direct assay Ref.4. Source: UniProtKB sperm individualization Inferred from mutant phenotype Ref.4. Source: FlyBase
Cellular component	cilium axoneme Inferred from direct assay Ref.4. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay Ref.4. Source: UniProtKB
Molecular function	protein-glycine ligase activity, elongating Inferred from direct assay Ref.4. Source: UniProtKB protein-glycine ligase activity, initiating Inferred from direct assay Ref.4. Source: UniProtKB tubulin-tyrosine ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 [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. Strain: Berkeley.
[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
EMBL GenBank DDBJ	AE014134 Genomic DNA. Translation: AAF52431.2. BT021443 mRNA. Translation: AAX33591.1.
RefSeq	NP_609068.2. NM_135224.2.
UniGene	Dm.18758.
3D structure databases
ProteinModelPortal	Q9VM92.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VM92. 1 interaction.
MINT	MINT-777438.
STRING	Q9VM92.
Proteomic databases
PRIDE	Q9VM92.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0300056; FBpp0289333; FBgn0031853.
GeneID	33946.
KEGG	dme:Dmel_CG11201.
UCSC	CG11201-RB. d. melanogaster.
Organism-specific databases
CTD	33946.
FlyBase	FBgn0031853. TTLL3B.
Phylogenomic databases
eggNOG	inNOG06215.
GeneTree	EMGT00050000006867.
InParanoid	Q9VM92.
OrthoDB	EOG4VT4C7.
PhylomeDB	Q9VM92.
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...
Other
NextBio	786066.

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:	January 25, 2012
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project