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Q9VTK2

- POMT1_DROME

UniProt

Q9VTK2 - POMT1_DROME

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Protein

Protein O-mannosyltransferase 1

Gene
rt, POMT1, CG6097
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Rt/POMT1 and tw/POMT2 function as a protein O-mannosyltransferase in association with each other to generate and maintain normal muscle development.3 Publications

Catalytic activityi

Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.1 Publication

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: UniProtKB
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. lipid glycosylation Source: UniProtKB
  2. muscle attachment Source: FlyBase
  3. muscle organ development Source: UniProtKB
  4. protein O-linked mannosylation Source: FlyBase
  5. regulation of synaptic activity Source: FlyBase
  6. sarcomere organization Source: FlyBase
  7. somatic muscle development Source: FlyBase
  8. specification of segmental identity, abdomen Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Names & Taxonomyi

Protein namesi
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 namesi
Name:rt
Synonyms:POMT1
ORF Names:CG6097
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0003292. rt.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei256 – 27621Helical; Reviewed predictionAdd
BLAST
Transmembranei310 – 33021Helical; Reviewed predictionAdd
BLAST
Transmembranei349 – 36921Helical; Reviewed predictionAdd
BLAST
Transmembranei398 – 41821Helical; Reviewed predictionAdd
BLAST
Transmembranei727 – 74721Helical; Reviewed predictionAdd
BLAST
Transmembranei791 – 81121Helical; Reviewed predictionAdd
BLAST
Transmembranei835 – 85521Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Death during development, the few adult escapers exhibit clockwise rotation of the abdomen and defects in embryonic muscle development.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 886886Protein O-mannosyltransferase 1PRO_0000121487Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi161 – 1611N-linked (GlcNAc...) Reviewed prediction
Glycosylationi242 – 2421N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9VTK2.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Zygotic expression peaks at embryonic stages 8-16.3 Publications

Gene expression databases

BgeeiQ9VTK2.

Interactioni

Subunit structurei

Interacts with tw/POMT2 Inferred.

Structurei

3D structure databases

ProteinModelPortaliQ9VTK2.
SMRiQ9VTK2. Positions 453-644.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini450 – 51162MIR 1Add
BLAST
Domaini522 – 57958MIR 2Add
BLAST
Domaini585 – 64258MIR 3Add
BLAST

Sequence similaritiesi

Contains 3 MIR domains.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1928.
GeneTreeiENSGT00740000115531.
InParanoidiQ9VTK2.
KOiK00728.
OMAiLMESMLL.
OrthoDBiEOG79KPDP.
PhylomeDBiQ9VTK2.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VTK2-1 [UniParc]FASTAAdd to Basket

« Hide

MSATYTNTIT QRRKTAKVRQ QQQHQWTGSD LSGESNERLH FRSRSTNSMQ    50
QHTAISNSPS PLCCNGARAL TMLNCCVDVN CHLNAPLRGS VNRHTTPTPT 100
PTATPTPVAT PKQASPSPTS DRSRSLSRSP SPSRSRSLSC QKQIDKNSAG 150
AASAEERKTA NASSQPFTVN LRIDLFSWTL FLLAFGTRFY KLATPPHIVF 200
DELHYGKYIS MYMRNIFFFD QHPPLGKQLI AGLVSLAGYD GNYTFTRIGE 250
PYSPEMPIFW FRFLPAMCGS LLAPAVYNLL LEAKLSRWSS ALGGLLVVLD 300
NSLLTQSRFV LMESMLLLAT TVGIACLLRF QRSRLGSLEW FFTGTAAAVC 350
LGAAGTVKYV GFLALGLAFY LLCRHLWQLL YDAGLTDRQL WMHAISRLLI 400
FVGIPLAVYL GVFYIHFKTL HRAGPHDSIM TSAFQASLDG GLASITKGQP 450
LAVVHGSQIT LRHTHGRTCW LHSHAAVYPV RYPDKRGSSH QQQVTCYSFK 500
DVNNWWLVKR PTKENLVVGD EPDIIRHGEI IQLVHGITSR ALNSHDVAAA 550
MTPQCQEVSC YIDYEIKMAG ELLWRVEILN RDSEGDIWHA IKSEVRLVHV 600
STEASLKFSG RQLPEWGFNQ HEVVADREKA IHEDAIWNVE EHRYTQTEDH 650
RERERQMLTA EMIPTKRTRI SFWAKLLELQ SKMLFQTKSV PNHMYSSMPH 700
EWPLMDKGIA YWLDSQSSAQ IYLLGNILLW YTATMGILVY AGLLAFYAMR 750
RQRLCFDISE QEWQRFVLAG DTFFMGYVMH YIPYFCVDRT LFLHNYLPAF 800
VFKLLLLCFV VEHLDYLLRR FCTGRGVHLV RLYRLMLILW LVGVLSIFSK 850
FIPFSYGARK MTLNEVRSLR WKDTWDFVLH KNHHLY 886
Length:886
Mass (Da):101,194
Last modified:March 1, 2001 - v2
Checksum:i5147C832EC5BC275
GO

Sequence cautioni

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 904LRGS → APGR in CAA65194. 1 Publication
Sequence conflicti184 – 1841A → T in CAA65194. 1 Publication
Sequence conflicti228 – 2292QL → TV in CAA65194. 1 Publication
Sequence conflicti233 – 2353LVS → TGH in CAA65194. 1 Publication
Sequence conflicti432 – 4321S → I in AAL48892. 1 Publication
Sequence conflicti443 – 4431A → T in CAA65194. 1 Publication
Sequence conflicti458 – 4592QI → KS in CAA65194. 1 Publication
Sequence conflicti514 – 5185ENLVV → RTWWW in CAA65194. 1 Publication
Sequence conflicti594 – 5941E → K in CAA65194. 1 Publication
Sequence conflicti633 – 6331E → K in CAA65194. 1 Publication
Sequence conflicti645 – 6451T → I in BAD54754. 1 Publication
Sequence conflicti655 – 6551R → P in CAA65194. 1 Publication
Sequence conflicti803 – 8031K → R in AAL48892. 1 Publication
Sequence conflicti844 – 8441V → E in CAA65194. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X95956 mRNA. Translation: CAA65194.1. Frameshift.
AB176550 mRNA. Translation: BAD54754.1.
AE014296 Genomic DNA. Translation: AAF50046.2.
AY071270 mRNA. Translation: AAL48892.1. Sequence problems.
RefSeqiNP_524025.2. NM_079301.3.
UniGeneiDm.6018.

Genome annotation databases

EnsemblMetazoaiFBtr0076146; FBpp0075877; FBgn0003292.
GeneIDi39297.
KEGGidme:Dmel_CG6097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X95956 mRNA. Translation: CAA65194.1 . Frameshift.
AB176550 mRNA. Translation: BAD54754.1 .
AE014296 Genomic DNA. Translation: AAF50046.2 .
AY071270 mRNA. Translation: AAL48892.1 . Sequence problems.
RefSeqi NP_524025.2. NM_079301.3.
UniGenei Dm.6018.

3D structure databases

ProteinModelPortali Q9VTK2.
SMRi Q9VTK2. Positions 453-644.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Proteomic databases

PaxDbi Q9VTK2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0076146 ; FBpp0075877 ; FBgn0003292 .
GeneIDi 39297.
KEGGi dme:Dmel_CG6097.

Organism-specific databases

CTDi 555989.
FlyBasei FBgn0003292. rt.

Phylogenomic databases

eggNOGi COG1928.
GeneTreei ENSGT00740000115531.
InParanoidi Q9VTK2.
KOi K00728.
OMAi LMESMLL.
OrthoDBi EOG79KPDP.
PhylomeDBi Q9VTK2.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

GenomeRNAii 39297.
NextBioi 812934.
PROi Q9VTK2.

Gene expression databases

Bgeei Q9VTK2.

Family and domain databases

InterProi IPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view ]
PANTHERi PTHR10050. PTHR10050. 1 hit.
Pfami PF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view ]
SMARTi SM00472. MIR. 3 hits.
[Graphical view ]
SUPFAMi SSF82109. SSF82109. 1 hit.
PROSITEi PS50919. MIR. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. 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.

Entry informationi

Entry nameiPOMT1_DROME
AccessioniPrimary (citable) accession number: Q9VTK2
Secondary accession number(s): Q60GL9, Q8SYW7, Q94891
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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