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Q9W5D4

- POMT2_DROME

UniProt

Q9W5D4 - POMT2_DROME

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Protein

Protein O-mannosyl-transferase 2

Gene

tw

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.2 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

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. sarcomere organization Source: FlyBase
  6. somatic muscle development Source: FlyBase
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-mannosyl-transferase 2 (EC:2.4.1.109)
Alternative name(s):
Dolichyl-phosphate-mannose--protein mannosyltransferase 2
Short name:
DmPOMT2
Short name:
dPOMT2
Protein twisted
Gene namesi
Name:tw
Synonyms:Pomt2
ORF Names:CG12311
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0086368. tw.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 765765Protein O-mannosyl-transferase 2PRO_0000121490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi751 – 7511N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9W5D4.
PRIDEiQ9W5D4.

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.1 Publication

Developmental stagei

Expressed throughout development; expression peaks at embryonic stages 8-16.2 Publications

Gene expression databases

BgeeiQ9W5D4.

Interactioni

Subunit structurei

Interacts with Rt/POMT1.Curated

Structurei

3D structure databases

ProteinModelPortaliQ9W5D4.
SMRiQ9W5D4. Positions 320-496.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei35 – 5521HelicalSequence AnalysisAdd
BLAST
Transmembranei128 – 14821HelicalSequence AnalysisAdd
BLAST
Transmembranei175 – 19521HelicalSequence AnalysisAdd
BLAST
Transmembranei206 – 22621HelicalSequence AnalysisAdd
BLAST
Transmembranei228 – 24821HelicalSequence AnalysisAdd
BLAST
Transmembranei268 – 28821HelicalSequence AnalysisAdd
BLAST
Transmembranei566 – 58621HelicalSequence AnalysisAdd
BLAST
Transmembranei667 – 68721HelicalSequence AnalysisAdd
BLAST
Transmembranei689 – 70921HelicalSequence AnalysisAdd
BLAST
Transmembranei719 – 73921HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini318 – 37457MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini384 – 44057MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini445 – 50157MIR 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.
InParanoidiQ9W5D4.
KOiK00728.
OMAiWLCISRF.
OrthoDBiEOG79KPDP.
PhylomeDBiQ9W5D4.

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.

Q9W5D4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAASVVKTPK CPRRGSVKDV AQNAPRTAPT SSKEANWNWW LLLATVFLVT
60 70 80 90 100
FATRFYKVTE PDHICWDETH FGKMGSWYIN RTFFFDVHPP LGKMLIGLSG
110 120 130 140 150
YLTGYNGTFP FEKPGDKYNE TRYQGMRYFC TTLGALIMPM GFDTVYDLTR
160 170 180 190 200
SHEAALLAAA YLIFDVGLLT LNQYILLDPI LLFFMMASVW GMVKVSKSTA
210 220 230 240 250
SGGSYGLRWW LWLFLTGTML SCTISVKFVG LFVVLLVGLH TATELWLILG
260 270 280 290 300
DLGQPILETV KQLACRAITL IVWPVLLYIL FFYIHLSVLN RSGNGDGFYS
310 320 330 340 350
SAFQSRLIGN SLYNASMPRD VAYGSLVTIK NHKTGGGYLH SHHHLYPKGS
360 370 380 390 400
GARQQQVTTY THKDENNKWL IRPHNKPGPP KGKVQILRHG DLVRLTHMAT
410 420 430 440 450
RRNLHSHNEP APMTKKHLQV TGYGELGLGD ANDVWRVLIV GGKVNETVHT
460 470 480 490 500
VTSRLKFIHL LQNCALTSSG KQLPKWGFEQ QEVSCNPNVR DKNSQWNVED
510 520 530 540 550
NEHKLMPSVS FSVYAPGFFA RFLESHAVML QGNAGLKPKE GEVTSRPWQW
560 570 580 590 600
PINYRGQFFS GSSYRIYLLG NPLIWWSNLV FLALFVTVFL CNAVVQQRRA
610 620 630 640 650
GFARSAAQNQ AQVPDSETVA QDEESEHSTT DICSCCTPAK EIVPKAVPSG
660 670 680 690 700
SPEAPNPAQS LRAAAWLFLG WMLHYLPFWA MGRVLYFHHY FPALIFNSLL
710 720 730 740 750
TGVMYNYILR VLPKWIHHVI LGLVLSILVY SFAAFSPLAY GMSGPLANEP
760
NSTMYNLKWL STWEF
Length:765
Mass (Da):86,250
Last modified:May 1, 2000 - v1
Checksum:i250CC8486330CB94
GO

Sequence cautioni

The sequence CAA20897.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591T → GS in allele tw[1].

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB176551 mRNA. Translation: BAD54755.1.
AE014298 Genomic DNA. Translation: AAF45548.1.
AL031583 Genomic DNA. Translation: CAA20897.1. Sequence problems.
AY095525 mRNA. Translation: AAM12256.1.
PIRiT13483.
RefSeqiNP_001259102.1. NM_001272173.1.
NP_569858.1. NM_130502.3.
UniGeneiDm.12266.

Genome annotation databases

EnsemblMetazoaiFBtr0070139; FBpp0070134; FBgn0086368.
GeneIDi31024.
KEGGidme:Dmel_CG12311.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB176551 mRNA. Translation: BAD54755.1 .
AE014298 Genomic DNA. Translation: AAF45548.1 .
AL031583 Genomic DNA. Translation: CAA20897.1 . Sequence problems.
AY095525 mRNA. Translation: AAM12256.1 .
PIRi T13483.
RefSeqi NP_001259102.1. NM_001272173.1.
NP_569858.1. NM_130502.3.
UniGenei Dm.12266.

3D structure databases

ProteinModelPortali Q9W5D4.
SMRi Q9W5D4. Positions 320-496.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Proteomic databases

PaxDbi Q9W5D4.
PRIDEi Q9W5D4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0070139 ; FBpp0070134 ; FBgn0086368 .
GeneIDi 31024.
KEGGi dme:Dmel_CG12311.

Organism-specific databases

CTDi 8168.
FlyBasei FBgn0086368. tw.

Phylogenomic databases

eggNOGi COG1928.
GeneTreei ENSGT00740000115531.
InParanoidi Q9W5D4.
KOi K00728.
OMAi WLCISRF.
OrthoDBi EOG79KPDP.
PhylomeDBi Q9W5D4.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

GenomeRNAii 31024.
NextBioi 771564.
PROi Q9W5D4.

Gene expression databases

Bgeei Q9W5D4.

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. "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.
  2. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE TW[1]), FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  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 GENOMIC DNA].
    Strain: Oregon-R1 Publication.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BerkeleyImported.
    Tissue: Larva1 Publication and Pupae1 Publication.

Entry informationi

Entry nameiPOMT2_DROME
AccessioniPrimary (citable) accession number: Q9W5D4
Secondary accession number(s): O77437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 95 of the entry and version 1 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