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Q9VTK2

- POMT1_DROME

UniProt

Q9VTK2 - POMT1_DROME

Protein

Protein O-mannosyltransferase 1

Gene

rt

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (01 Mar 2001)
      Previous versions | rss
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    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.

    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

    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:rtImported
    Synonyms:POMT1Imported
    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 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

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

    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...)Sequence Analysis
    Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis

    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.Curated

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VTK2.
    SMRiQ9VTK2. Positions 453-644.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

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

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Belongs to the glycosyltransferase 39 family.Sequence Analysis
    Contains 3 MIR domains.PROSITE-ProRule annotation

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 904LRGS → APGR in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti184 – 1841A → T in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti228 – 2292QL → TV in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti233 – 2353LVS → TGH in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti432 – 4321S → I in AAL48892. (PubMed:12537569)Curated
    Sequence conflicti443 – 4431A → T in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti458 – 4592QI → KS in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti514 – 5185ENLVV → RTWWW in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti594 – 5941E → K in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti633 – 6331E → K in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti645 – 6451T → I in BAD54754. (PubMed:15271988)Curated
    Sequence conflicti655 – 6551R → P in CAA65194. (PubMed:8650217)Curated
    Sequence conflicti803 – 8031K → R in AAL48892. (PubMed:12537569)Curated
    Sequence conflicti844 – 8441V → E in CAA65194. (PubMed:8650217)Curated

    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

    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: Berkeley1 Publication.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BerkeleyImported.
      Tissue: Embryo1 Publication.
    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: October 1, 2014
    This is version 96 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