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Q9VTK2

- POMT1_DROME

UniProt

Q9VTK2 - POMT1_DROME

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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

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 D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein.

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate-mannose-protein mannosyltransferase activity 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: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

Topology

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

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. 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...)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...

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

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

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:
EMBLi
GenBanki
DDBJi
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_079301.4.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_079301.4.

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

ChiTaRSi rt. fly.
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: 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: November 26, 2014
This is version 98 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