Q9VTK2 (POMT1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein O-mannosyltransferase 1
EC=2.4.1.109

Alternative name(s):
Dolichyl-phosphate-mannose--protein mannosyltransferase 1
Short name=dPOMT1
Protein rotated abdomen

Gene names

Name:	rt
Synonyms:	POMT1
ORF Names:	CG6097

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	886 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Rt/POMT1 and tw/POMT2 function as a protein O-mannosyltransferase in association with each other to generate and maintain normal muscle development. Ref.1 Ref.2 Ref.6
Catalytic activity	Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein. Ref.2
Pathway	Protein modification; protein glycosylation.
Subunit structure	Interacts with tw/POMT2 Probable.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.6.
Tissue specificity	At the cellular blastoderm stage, expression accumulates in the ventrally located mesoderm primordium. At germ band extension, mesoderm expression is seen as stripes of strong expression. A very strong signal is also detected in the invaginating gut. As the germ band retracts, mesodermal expression decays and becomes restricted to somatic muscle precursors. After dorsal closure, expression has disappeared from the mesoderm and remains in the endoderm. Some expression is detected in a few cells of the head and the pharyngeal muscles. Ref.1 Ref.2
Developmental stage	Expressed both maternally and zygotically. Zygotic expression peaks at embryonic stages 8-16. Ref.1 Ref.2 Ref.6
Disruption phenotype	Death during development, the few adult escapers exhibit clockwise rotation of the abdomen and defects in embryonic muscle development. Ref.1 Ref.2
Sequence similarities	Belongs to the glycosyltransferase 39 family. Contains 3 MIR domains.
Sequence caution	The sequence AAL48892.1 differs from that shown. Reason: Intron retention. The sequence CAA65194.1 differs from that shown. Reason: Frameshift at positions 118, 149, 567, 574, 585, 643, 649, 668, 688, 708, 720, 848, 856 and 876.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Repeat Transmembrane Transmembrane helix
Molecular function	Developmental protein Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	lipid glycosylation Inferred from mutant phenotype Ref.2. Source: UniProtKB muscle attachment Inferred from genetic interaction. Source: FlyBase protein O-linked mannosylation Inferred from direct assay Ref.2. Source: FlyBase regulation of synaptic activity Inferred from mutant phenotype. Source: FlyBase sarcomere organization Inferred from genetic interaction. Source: FlyBase somatic muscle development Inferred from mutant phenotype. Source: FlyBase specification of segmental identity, abdomen Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	dolichyl-phosphate-mannose-protein mannosyltransferase activity Inferred from direct assay Ref.2. Source: UniProtKB protein binding Inferred from physical interaction Ref.2Ref.6. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 886	886	Protein O-mannosyltransferase 1		PRO_0000121487
Regions
	Transmembrane	256 – 276	21	Helical; Potential
	Transmembrane	310 – 330	21	Helical; Potential
	Transmembrane	349 – 369	21	Helical; Potential
	Transmembrane	398 – 418	21	Helical; Potential
	Transmembrane	727 – 747	21	Helical; Potential
	Transmembrane	791 – 811	21	Helical; Potential
	Transmembrane	835 – 855	21	Helical; Potential
	Domain	450 – 511	62	MIR 1
	Domain	522 – 579	58	MIR 2
	Domain	585 – 642	58	MIR 3
Amino acid modifications
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	242	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	87 – 90	4	LRGS → APGR in CAA65194. Ref.1
	Sequence conflict	184	1	A → T in CAA65194. Ref.1
	Sequence conflict	228 – 229	2	QL → TV in CAA65194. Ref.1
	Sequence conflict	233 – 235	3	LVS → TGH in CAA65194. Ref.1
	Sequence conflict	432	1	S → I in AAL48892. Ref.5
	Sequence conflict	443	1	A → T in CAA65194. Ref.1
	Sequence conflict	458 – 459	2	QI → KS in CAA65194. Ref.1
	Sequence conflict	514 – 518	5	ENLVV → RTWWW in CAA65194. Ref.1
	Sequence conflict	594	1	E → K in CAA65194. Ref.1
	Sequence conflict	633	1	E → K in CAA65194. Ref.1
	Sequence conflict	645	1	T → I in BAD54754. Ref.2
	Sequence conflict	655	1	R → P in CAA65194. Ref.1
	Sequence conflict	803	1	K → R in AAL48892. Ref.5
	Sequence conflict	844	1	V → E in CAA65194. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VTK2 [UniParc]. Last modified March 1, 2001. Version 2. Checksum: 5147C832EC5BC275	FASTA	886	101,194
	10 20 30 40 50 60 MSATYTNTIT QRRKTAKVRQ QQQHQWTGSD LSGESNERLH FRSRSTNSMQ QHTAISNSPS 70 80 90 100 110 120 PLCCNGARAL TMLNCCVDVN CHLNAPLRGS VNRHTTPTPT PTATPTPVAT PKQASPSPTS 130 140 150 160 170 180 DRSRSLSRSP SPSRSRSLSC QKQIDKNSAG AASAEERKTA NASSQPFTVN LRIDLFSWTL 190 200 210 220 230 240 FLLAFGTRFY KLATPPHIVF DELHYGKYIS MYMRNIFFFD QHPPLGKQLI AGLVSLAGYD 250 260 270 280 290 300 GNYTFTRIGE PYSPEMPIFW FRFLPAMCGS LLAPAVYNLL LEAKLSRWSS ALGGLLVVLD 310 320 330 340 350 360 NSLLTQSRFV LMESMLLLAT TVGIACLLRF QRSRLGSLEW FFTGTAAAVC LGAAGTVKYV 370 380 390 400 410 420 GFLALGLAFY LLCRHLWQLL YDAGLTDRQL WMHAISRLLI FVGIPLAVYL GVFYIHFKTL 430 440 450 460 470 480 HRAGPHDSIM TSAFQASLDG GLASITKGQP LAVVHGSQIT LRHTHGRTCW LHSHAAVYPV 490 500 510 520 530 540 RYPDKRGSSH QQQVTCYSFK DVNNWWLVKR PTKENLVVGD EPDIIRHGEI IQLVHGITSR 550 560 570 580 590 600 ALNSHDVAAA MTPQCQEVSC YIDYEIKMAG ELLWRVEILN RDSEGDIWHA IKSEVRLVHV 610 620 630 640 650 660 STEASLKFSG RQLPEWGFNQ HEVVADREKA IHEDAIWNVE EHRYTQTEDH RERERQMLTA 670 680 690 700 710 720 EMIPTKRTRI SFWAKLLELQ SKMLFQTKSV PNHMYSSMPH EWPLMDKGIA YWLDSQSSAQ 730 740 750 760 770 780 IYLLGNILLW YTATMGILVY AGLLAFYAMR RQRLCFDISE QEWQRFVLAG DTFFMGYVMH 790 800 810 820 830 840 YIPYFCVDRT LFLHNYLPAF VFKLLLLCFV VEHLDYLLRR FCTGRGVHLV RLYRLMLILW 850 860 870 880 LVGVLSIFSK FIPFSYGARK MTLNEVRSLR WKDTWDFVLH KNHHLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in the rotated abdomen locus affect muscle development and reveal an intrinsic asymmetry in Drosophila." Martin-Blanco E., Garcia-Bellido A. Proc. Natl. Acad. Sci. U.S.A. 93:6048-6052(1996) [PubMed: 8650217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. Tissue: Embryo.
[2]	"The twisted abdomen phenotype of Drosophila POMT1 and POMT2 mutants coincides with their heterophilic protein O-mannosyltransferase activity." Ichimiya T., Manya H., Ohmae Y., Yoshida H., Takahashi K., Ueda R., Endo T., Nishihara S. J. Biol. Chem. 279:42638-42647(2004) [PubMed: 15271988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[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: Embryo.
[6]	"The twisted gene encodes Drosophila protein O-mannosyltransferase 2 and genetically interacts with the rotated abdomen gene encoding Drosophila protein O-mannosyltransferase 1." Lyalin D., Koles K., Roosendaal S.D., Repnikova E., Van Wechel L., Panin V.M. Genetics 172:343-353(2006) [PubMed: 16219785] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X95956 mRNA. Translation: CAA65194.1. Frameshift. AB176550 mRNA. Translation: BAD54754.1. AE014296 Genomic DNA. Translation: AAF50046.2. AY071270 mRNA. Translation: AAL48892.1. Sequence problems.
RefSeq	NP_524025.2. NM_079301.2.
UniGene	Dm.6018.
3D structure databases
ProteinModelPortal	Q9VTK2.
SMR	Q9VTK2. Positions 451-648.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9VTK2.
Protein family/group databases
CAZy	GT39. Glycosyltransferase Family 39.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0076146; FBpp0075877; FBgn0003292.
GeneID	39297.
KEGG	dme:Dmel_CG6097.
NMPDR	fig|7227.3.peg.9382.
Organism-specific databases
CTD	555989.
FlyBase	FBgn0003292. rt.
Phylogenomic databases
eggNOG	inNOG07847.
GeneTree	EMGT00050000017292.
InParanoid	Q9VTK2.
OMA	VFDELHY.
OrthoDB	EOG42JM6H.
PhylomeDB	Q9VTK2.
Gene expression databases
Bgee	Q9VTK2.
GermOnline	CG6097. Drosophila melanogaster.
Family and domain databases
InterPro	IPR003342. Glyco_trans_39. IPR003608. MIR. IPR016093. MIR_motif. [Graphical view]
KO	K00728.
Pfam	PF02815. MIR. 1 hit. PF02366. PMT. 1 hit. [Graphical view]
SMART	SM00472. MIR. 3 hits. [Graphical view]
SUPFAM	SSF82109. MIR. 1 hit.
PROSITE	PS50919. MIR. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	812934.

Entry information

Entry name

POMT1_DROME

Accession

Primary (citable) accession number: Q9VTK2
Secondary accession number(s): Q60GL9, Q8SYW7, Q94891

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project