Q29IL2 (POMT2_DROPS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein O-mannosyl-transferase 2
EC=2.4.1.109

Alternative name(s):
Dolichyl-phosphate-mannose--protein mannosyltransferase 2
Protein twisted

Gene names

Name:	tw
ORF Names:	GA11548

Organism

Drosophila pseudoobscura pseudoobscura (Fruit fly) [Reference proteome]

Taxonomic identifier

46245 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › obscura group › pseudoobscura subgroup › Drosophila pseudoobscura

Protein attributes

Sequence length	749 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 Rt/POMT1 By similarity. UniProtKB Q9W5D4
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity UniProtKB Q9W5D4.
Sequence similarities	Belongs to the glycosyltransferase 39 family. Contains 3 MIR domains.
Sequence caution	The sequence EAL32641.1 differs from that shown. Reason: Erroneous gene model prediction.

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
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 electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 749	749	Protein O-mannosyl-transferase 2		PRO_0000307927
Regions
	Transmembrane	34 – 54	21	Helical; Potential
	Transmembrane	126 – 146	21	Helical; Potential
	Transmembrane	173 – 193	21	Helical; Potential
	Transmembrane	204 – 224	21	Helical; Potential
	Transmembrane	226 – 246	21	Helical; Potential
	Transmembrane	266 – 286	21	Helical; Potential
	Transmembrane	572 – 592	21	Helical; Potential
	Transmembrane	645 – 665	21	Helical; Potential
	Transmembrane	669 – 689	21	Helical; Potential
	Transmembrane	703 – 723	21	Helical; Potential
	Domain	316 – 372	57	MIR 1
	Domain	382 – 438	57	MIR 2
	Domain	443 – 499	57	MIR 3
Amino acid modifications
	Glycosylation	78	1	N-linked (GlcNAc...) Potential
	Glycosylation	104	1	N-linked (GlcNAc...) Potential
	Glycosylation	117	1	N-linked (GlcNAc...) Potential
	Glycosylation	288	1	N-linked (GlcNAc...) Potential
	Glycosylation	312	1	N-linked (GlcNAc...) Potential
	Glycosylation	443	1	N-linked (GlcNAc...) Potential
	Glycosylation	735	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q29IL2 [UniParc]. Last modified April 4, 2006. Version 1. Checksum: 4235318C19C91334	FASTA	749	84,957
	10 20 30 40 50 60 MAASVVKTPK CPRRGSAKEQ QSKASPKSNN ESNNWHWWIL LASVFLITFA TRFYKVTEPD 70 80 90 100 110 120 HICWDETHFG KMGSWYINRT FFFDVHPPLG KMLIGLSGYL TGYNGTFPFE KPGDKYNETA 130 140 150 160 170 180 YQGMRYFCTT LGALIMPMGF DTVYDLTRSH EAALLSAAYL IFDVGLLTLN QYILLDPILL 190 200 210 220 230 240 FFMMGSVWGM VKISKATASG GSYSVRWWFW LFLTGTMLSC TISVKFVGLF VVLLVGLHTA 250 260 270 280 290 300 TELWLILGDL GQPIVETLKQ IACRAIALIL WPILLYTLFF YIHLSVLNRS GNGDGFYSSA 310 320 330 340 350 360 FQSRLIGNSL YNASMPRDVA YGSVVTIKNH KTGGGYLHSH FHLYPKGSGA RQQQITTYTH 370 380 390 400 410 420 KDDNNKWVIK PHNKQRLPKD KLQLLRHGDL VRLEHLVTKR NLHSHSEPAP MTKKHLQVTG 430 440 450 460 470 480 YGESGVGDAN DVWRVLIVGG KVNETVHTVT SRLMLIHYLQ NCALTSSGKQ LPKWGFEQQE 490 500 510 520 530 540 VSCNLNVRDK YAHWNVEDNE HKLLPSVSFS VYAPGFFARF LESHAVMLQG NAGLKPKEGE 550 560 570 580 590 600 VTSRPWQWPI NYRGQFFSGS SYRIYLLGNP VIWWSNLVFL ALFVAVFLGN AILEQRRAGQ 610 620 630 640 650 660 ARALVRSQAD SEDSEPSTTD VPLCTCCPEE QQLLSRPREE HRDPLGAAAW LFVGWLLHYL 670 680 690 700 710 720 PFWAMGRVLY FHHYFPALIF NSLLTGVMFH HIIQSLPRWI QHVLLGGLLS LIVYSFALFS 730 740 PLAYGMSGPL ANEPNSTMHS LKWLSTWEF

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. , Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., Weinstock G.M., 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	CH379063 Genomic DNA. Translation: EAL32641.1. Sequence problems.
RefSeq	XP_001355582.1. XM_001355546.2.
3D structure databases
ProteinModelPortal	Q29IL2.
ModBase	Search...
Protein-protein interaction databases
STRING	7237.FBpp0273533.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0275095; FBpp0273533; FBgn0071599.
GeneID	4815847.
KEGG	dpo:Dpse_GA11548.
Organism-specific databases
FlyBase	FBgn0071599. Dpse\GA11548.
Phylogenomic databases
eggNOG	COG1928.
InParanoid	Q29IL2.
KO	K00728.
OMA	WPINYRG.
OrthoDB	EOG44B8H7.
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

POMT2_DROPS

Accession

Primary (citable) accession number: Q29IL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	April 4, 2006
Last modified:	April 3, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project