Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9VTK2 (POMT1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length886 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentEndoplasmic reticulum
Membrane
   DomainRepeat
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Glycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid glycosylation

Inferred from mutant phenotype Ref.2. Source: UniProtKB

muscle attachment

Inferred from genetic interaction PubMed 17881734. Source: FlyBase

muscle organ development

Inferred from mutant phenotype Ref.6. Source: UniProtKB

protein O-linked mannosylation

Inferred from direct assay Ref.2. Source: FlyBase

regulation of synaptic activity

Inferred from mutant phenotype PubMed 18385336. Source: FlyBase

sarcomere organization

Inferred from genetic interaction PubMed 17881734. Source: FlyBase

somatic muscle development

Inferred from mutant phenotype PubMed 20644630. Source: FlyBase

specification of segmental identity, abdomen

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.6. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from sequence or structural similarity Ref.2. Source: FlyBase

   Molecular_functiondolichyl-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 886886Protein O-mannosyltransferase 1
PRO_0000121487

Regions

Transmembrane256 – 27621Helical; Potential
Transmembrane310 – 33021Helical; Potential
Transmembrane349 – 36921Helical; Potential
Transmembrane398 – 41821Helical; Potential
Transmembrane727 – 74721Helical; Potential
Transmembrane791 – 81121Helical; Potential
Transmembrane835 – 85521Helical; Potential
Domain450 – 51162MIR 1
Domain522 – 57958MIR 2
Domain585 – 64258MIR 3

Amino acid modifications

Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict87 – 904LRGS → APGR in CAA65194. Ref.1
Sequence conflict1841A → T in CAA65194. Ref.1
Sequence conflict228 – 2292QL → TV in CAA65194. Ref.1
Sequence conflict233 – 2353LVS → TGH in CAA65194. Ref.1
Sequence conflict4321S → I in AAL48892. Ref.5
Sequence conflict4431A → T in CAA65194. Ref.1
Sequence conflict458 – 4592QI → KS in CAA65194. Ref.1
Sequence conflict514 – 5185ENLVV → RTWWW in CAA65194. Ref.1
Sequence conflict5941E → K in CAA65194. Ref.1
Sequence conflict6331E → K in CAA65194. Ref.1
Sequence conflict6451T → I in BAD54754. Ref.2
Sequence conflict6551R → P in CAA65194. Ref.1
Sequence conflict8031K → R in AAL48892. Ref.5
Sequence conflict8441V → E in CAA65194. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9VTK2 [UniParc].

Last modified March 1, 2001. Version 2.
Checksum: 5147C832EC5BC275

FASTA886101,194
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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. expand/collapse author list , 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.
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].
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] [Europe PMC] [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.
RefSeqNP_524025.2. NM_079301.3.
UniGeneDm.6018.

3D structure databases

ProteinModelPortalQ9VTK2.
SMRQ9VTK2. Positions 453-644.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

Proteomic databases

PaxDbQ9VTK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076146; FBpp0075877; FBgn0003292.
GeneID39297.
KEGGdme:Dmel_CG6097.

Organism-specific databases

CTD555989.
FlyBaseFBgn0003292. rt.

Phylogenomic databases

eggNOGCOG1928.
GeneTreeENSGT00740000115531.
InParanoidQ9VTK2.
KOK00728.
OMALMESMLL.
OrthoDBEOG79KPDP.
PhylomeDBQ9VTK2.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ9VTK2.

Family and domain databases

InterProIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERPTHR10050. PTHR10050. 1 hit.
PfamPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMSSF82109. SSF82109. 1 hit.
PROSITEPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi39297.
NextBio812934.
PROQ9VTK2.

Entry information

Entry namePOMT1_DROME
AccessionPrimary (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: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase