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Q9W5D4

- POMT2_DROME

UniProt

Q9W5D4 - POMT2_DROME

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Protein
Protein O-mannosyl-transferase 2
Gene
tw, Pomt2, CG12311
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.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. 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; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei35 – 5521Helical; Reviewed prediction
Add
BLAST
Transmembranei128 – 14821Helical; Reviewed prediction
Add
BLAST
Transmembranei175 – 19521Helical; Reviewed prediction
Add
BLAST
Transmembranei206 – 22621Helical; Reviewed prediction
Add
BLAST
Transmembranei228 – 24821Helical; Reviewed prediction
Add
BLAST
Transmembranei268 – 28821Helical; Reviewed prediction
Add
BLAST
Transmembranei566 – 58621Helical; Reviewed prediction
Add
BLAST
Transmembranei667 – 68721Helical; Reviewed prediction
Add
BLAST
Transmembranei689 – 70921Helical; Reviewed prediction
Add
BLAST
Transmembranei719 – 73921Helical; Reviewed prediction
Add
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.1 Publication

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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 Inferred.

Structurei

3D structure databases

ProteinModelPortaliQ9W5D4.
SMRiQ9W5D4. Positions 320-496.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini318 – 37457MIR 1
Add
BLAST
Domaini384 – 44057MIR 2
Add
BLAST
Domaini445 – 50157MIR 3
Add
BLAST

Sequence similaritiesi

Contains 3 MIR domains.

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

MAASVVKTPK CPRRGSVKDV AQNAPRTAPT SSKEANWNWW LLLATVFLVT    50
FATRFYKVTE PDHICWDETH FGKMGSWYIN RTFFFDVHPP LGKMLIGLSG 100
YLTGYNGTFP FEKPGDKYNE TRYQGMRYFC TTLGALIMPM GFDTVYDLTR 150
SHEAALLAAA YLIFDVGLLT LNQYILLDPI LLFFMMASVW GMVKVSKSTA 200
SGGSYGLRWW LWLFLTGTML SCTISVKFVG LFVVLLVGLH TATELWLILG 250
DLGQPILETV KQLACRAITL IVWPVLLYIL FFYIHLSVLN RSGNGDGFYS 300
SAFQSRLIGN SLYNASMPRD VAYGSLVTIK NHKTGGGYLH SHHHLYPKGS 350
GARQQQVTTY THKDENNKWL IRPHNKPGPP KGKVQILRHG DLVRLTHMAT 400
RRNLHSHNEP APMTKKHLQV TGYGELGLGD ANDVWRVLIV GGKVNETVHT 450
VTSRLKFIHL LQNCALTSSG KQLPKWGFEQ QEVSCNPNVR DKNSQWNVED 500
NEHKLMPSVS FSVYAPGFFA RFLESHAVML QGNAGLKPKE GEVTSRPWQW 550
PINYRGQFFS GSSYRIYLLG NPLIWWSNLV FLALFVTVFL CNAVVQQRRA 600
GFARSAAQNQ AQVPDSETVA QDEESEHSTT DICSCCTPAK EIVPKAVPSG 650
SPEAPNPAQS LRAAAWLFLG WMLHYLPFWA MGRVLYFHHY FPALIFNSLL 700
TGVMYNYILR VLPKWIHHVI LGLVLSILVY SFAAFSPLAY GMSGPLANEP 750
NSTMYNLKWL STWEF 765
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: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Larva and Pupae.

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: July 9, 2014
This is version 93 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

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