Protein O-mannosyltransferase 1 - Drosophila pseudoobscura pseudoobscura (Fruit fly)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Protein O-mannosyltransferase 1
EC=2.4.1.109

Alternative name(s):
Dolichyl-phosphate-mannose--protein mannosyltransferase 1
Protein rotated abdomen

Gene names

Name:	rt
ORF Names:	GA19350

Organism

Drosophila pseudoobscura pseudoobscura (Fruit fly) [Reference proteome]

Taxonomic identifier

46245 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length	908 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Rt/POMT1 and tw/POMT2 function as a protein O-mannosyltransferase in association with each other to generate and maintain normal muscle development By similarity.
Catalytic activity	Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Interacts with tw/POMT2 By similarity. UniProtKB Q9VTK2
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity UniProtKB Q9VTK2.
Sequence similarities	Belongs to the glycosyltransferase 39 family. Contains 3 MIR domains.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Repeat Transmembrane Transmembrane helix
Molecular function	Developmental protein Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid glycosylation Inferred from sequence or structural similarity. Source: UniProtKB muscle organ development Inferred from sequence or structural similarity. Source: UniProtKB protein O-linked glycosylation Inferred from electronic annotation. Source: InterPro specification of segmental identity, abdomen Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	dolichyl-phosphate-mannose-protein mannosyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 908

908

Protein O-mannosyltransferase 1

PRO_0000307926

Regions

Transmembrane

190 – 210

21

Helical; Potential

Transmembrane

279 – 299

21

Helical; Potential

Transmembrane

311 – 328

18

Helical; Potential

Transmembrane

331 – 351

21

Helical; Potential

Transmembrane

370 – 390

21

Helical; Potential

Transmembrane

418 – 438

21

Helical; Potential

Transmembrane

749 – 769

21

Helical; Potential

Transmembrane

788 – 808

21

Helical; Potential

Transmembrane

813 – 833

21

Helical; Potential

Transmembrane

857 – 877

21

Helical; Potential

Domain

473 – 534

62

MIR 1

Domain

545 – 602

58

MIR 2

Domain

608 – 664

57

MIR 3

Compositional bias

290 – 423

134

Leu-rich

Amino acid modifications

Glycosylation

265

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q2LZ62 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: 3D0182C4D63416C4
Show »

FASTA

908

102,912

        10         20         30         40         50         60 
MYNNNNDGGG GGSANGNTMQ QRRKTTTRSR SKQQQQQQCT SENVIEKNQT NGAQNERLHF 

        70         80         90        100        110        120 
RGSSKDSALS TPLLPRSRST TSAINSPSPL CCNGGLSILN CCRDVNCHLN APLRGSVESS 

       130        140        150        160        170        180 
RSRRSESRQS SLTATPTTTP KQASPSPTIS ERSRSCSGSR SRSCSCDGRL VDCHKHSAAA 

       190        200        210        220        230        240 
AAASTAAPQF TVNLSIDLFS WTLFLLAFCT RFYKLATPPH IVFDELHYGK YIAHYMRNIF 

       250        260        270        280        290        300 
FFDQHPPLGK QLIAGLVSLA GYDGNYTFSR IGAAYAPDVP IFWFRFIPAL CGSLLAPAVY 

       310        320        330        340        350        360 
RLLLEARLHR WAAALGGLLV VLDNSLLTQS RFVLMESMLL LASTLGIACL LRFQRCRLGS 

       370        380        390        400        410        420 
FQWLCNGSAA GVLLACAGAV KYIGFLALAL AGYLLCRHLW QLLYDASLTN RQLWMHALSR 

       430        440        450        460        470        480 
LLLFVGIPIA VYIGVFYVHF RTLHRAGPHD SIMTSAFQAS LEGGLASITS GQPLAVVHGS 

       490        500        510        520        530        540 
QITLRHTHGR TCWLHSHAAV YPVRYKDKRG SSHQQQVTCY SFKDVNNWWI VKRPERDDLV 

       550        560        570        580        590        600 
VGEQPDVIQH GDVIQLVHGI TSRALNSHDV AAPMTPQCQE VSCYIDYEIK MAGELLWRVE 

       610        620        630        640        650        660 
ILNRNSEGDS WHAIKSEIRL VHESTGAALK FSGRQLPDWG FNQHEVVADR DQVHEDAIWN 

       670        680        690        700        710        720 
VEEHRYTKTQ DQRERERQLL SAEMIPTKRT KLSFWAKLLE LQTKMFWHGK HLQAHMYSSL 

       730        740        750        760        770        780 
PHEWPLMDKG IAYWLDSQSS AQIYLLGNVL IWYTASAGIL VYATLLAFYA VRRRRLCFDV 

       790        800        810        820        830        840 
SQHEWQRFLM AGDTFFVGYM MHYLPYYFVD RTLFLHNYLP AFVFKLLLLC FVVEHLDYLL 

       850        860        870        880        890        900 
RRHCSGRGVH LVRVYRLALL LWLLAVGSVF VKFLPLSYGA RKMTIEEVRR LRWKDTWDFI 


LQKNYALN

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References

[1]

"Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution."
Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L.

Gibbs R.A.
Genome Res. 15:1-18(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MV2-25 / Tucson 14011-0121.94.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH379069 Genomic DNA. Translation: EAL29647.2.
RefSeq	XP_001353911.2. XM_001353875.2.
3D structure databases
ProteinModelPortal	Q2LZ62.
ModBase	Search...
Protein-protein interaction databases
STRING	7237.FBpp0275409.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0276971; FBpp0275409; FBgn0079347.
GeneID	4813592.
KEGG	dpo:Dpse_GA19350.
Organism-specific databases
FlyBase	FBgn0079347. Dpse\GA19350.
Phylogenomic databases
eggNOG	COG1928.
InParanoid	Q2LZ62.
KO	K00728.
OrthoDB	EOG42JM6H.
Enzyme and pathway databases
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR027005. GlyclTrfase_39_like. IPR003342. Glyco_trans_39. IPR016093. MIR_motif. [Graphical view]
PANTHER	PTHR10050. PTHR10050. 1 hit.
Pfam	PF02815. MIR. 1 hit. PF02366. PMT. 1 hit. [Graphical view]
SMART	SM00472. MIR. 3 hits. [Graphical view]
SUPFAM	SSF82109. MIR. 1 hit.
PROSITE	PS50919. MIR. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POMT1_DROPS

Accession

Primary (citable) accession number: Q2LZ62

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	October 23, 2007
Last modified:	April 3, 2013
This is version 42 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents