Q9W5D4 (POMT2_DROME) 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
Short name=DmPOMT2
Short name=dPOMT2
Protein twisted

Gene names

Name:	tw
Synonyms:	Pomt2
ORF Names:	CG12311

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [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 › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	765 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

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. Ref.1 Ref.2
Catalytic activity	Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein. Ref.1
Pathway	Protein modification; protein glycosylation.
Subunit structure	Interacts with Rt/POMT1 Probable.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.2.
Tissue specificity	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. Ref.1
Developmental stage	Expressed throughout development; expression peaks at embryonic stages 8-16. Ref.1 Ref.2
Disruption phenotype	Death during development, the few adult escapers exhibit clockwise rotation of the abdomen. Ref.1
Sequence similarities	Belongs to the glycosyltransferase 39 family. Contains 3 MIR domains.
Sequence caution	The sequence CAA20897.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
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 mutant phenotype Ref.1. Source: UniProtKB muscle attachment Inferred from genetic interaction PubMed 17881734. Source: FlyBase protein O-linked mannosylation Inferred from direct assay Ref.1. Source: FlyBase sarcomere organization Inferred from genetic interaction PubMed 17881734. Source: FlyBase somatic muscle development Inferred from mutant phenotype PubMed 20644630. Source: FlyBase
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.2. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from sequence or structural similarity Ref.1. Source: FlyBase
Molecular_function	dolichyl-phosphate-mannose-protein mannosyltransferase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 765	765	Protein O-mannosyl-transferase 2		PRO_0000121490
Regions
	Transmembrane	35 – 55	21	Helical; Potential
	Transmembrane	128 – 148	21	Helical; Potential
	Transmembrane	175 – 195	21	Helical; Potential
	Transmembrane	206 – 226	21	Helical; Potential
	Transmembrane	228 – 248	21	Helical; Potential
	Transmembrane	268 – 288	21	Helical; Potential
	Transmembrane	566 – 586	21	Helical; Potential
	Transmembrane	667 – 687	21	Helical; Potential
	Transmembrane	689 – 709	21	Helical; Potential
	Transmembrane	719 – 739	21	Helical; Potential
	Domain	318 – 374	57	MIR 1
	Domain	384 – 440	57	MIR 2
	Domain	445 – 501	57	MIR 3
Amino acid modifications
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Glycosylation	106	1	N-linked (GlcNAc...) Potential
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	290	1	N-linked (GlcNAc...) Potential
	Glycosylation	314	1	N-linked (GlcNAc...) Potential
	Glycosylation	445	1	N-linked (GlcNAc...) Potential
	Glycosylation	751	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	59	1	T → GS in allele tw[1].

Sequences

	Sequence		Length	Mass (Da)
	Q9W5D4 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 250CC8486330CB94	FASTA	765	86,250
	10 20 30 40 50 60 MAASVVKTPK CPRRGSVKDV AQNAPRTAPT SSKEANWNWW LLLATVFLVT FATRFYKVTE 70 80 90 100 110 120 PDHICWDETH FGKMGSWYIN RTFFFDVHPP LGKMLIGLSG YLTGYNGTFP FEKPGDKYNE 130 140 150 160 170 180 TRYQGMRYFC TTLGALIMPM GFDTVYDLTR SHEAALLAAA YLIFDVGLLT LNQYILLDPI 190 200 210 220 230 240 LLFFMMASVW GMVKVSKSTA SGGSYGLRWW LWLFLTGTML SCTISVKFVG LFVVLLVGLH 250 260 270 280 290 300 TATELWLILG DLGQPILETV KQLACRAITL IVWPVLLYIL FFYIHLSVLN RSGNGDGFYS 310 320 330 340 350 360 SAFQSRLIGN SLYNASMPRD VAYGSLVTIK NHKTGGGYLH SHHHLYPKGS GARQQQVTTY 370 380 390 400 410 420 THKDENNKWL IRPHNKPGPP KGKVQILRHG DLVRLTHMAT RRNLHSHNEP APMTKKHLQV 430 440 450 460 470 480 TGYGELGLGD ANDVWRVLIV GGKVNETVHT VTSRLKFIHL LQNCALTSSG KQLPKWGFEQ 490 500 510 520 530 540 QEVSCNPNVR DKNSQWNVED NEHKLMPSVS FSVYAPGFFA RFLESHAVML QGNAGLKPKE 550 560 570 580 590 600 GEVTSRPWQW PINYRGQFFS GSSYRIYLLG NPLIWWSNLV FLALFVTVFL CNAVVQQRRA 610 620 630 640 650 660 GFARSAAQNQ AQVPDSETVA QDEESEHSTT DICSCCTPAK EIVPKAVPSG SPEAPNPAQS 670 680 690 700 710 720 LRAAAWLFLG WMLHYLPFWA MGRVLYFHHY FPALIFNSLL TGVMYNYILR VLPKWIHHVI 730 740 750 760 LGLVLSILVY SFAAFSPLAY GMSGPLANEP NSTMYNLKWL STWEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"From sequence to chromosome: the tip of the X chromosome of D. melanogaster." Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M. Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Oregon-R.
[6]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Larva and Pupae.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB176551 mRNA. Translation: BAD54755.1. AE014298 Genomic DNA. Translation: AAF45548.1. AL031583 Genomic DNA. Translation: CAA20897.1. Sequence problems. AY095525 mRNA. Translation: AAM12256.1.
PIR	T13483.
RefSeq	NP_001259102.1. NM_001272173.1. NP_569858.1. NM_130502.3.
UniGene	Dm.12266.
3D structure databases
ProteinModelPortal	Q9W5D4.
SMR	Q9W5D4. Positions 320-496.
ModBase	Search...
Protein family/group databases
CAZy	GT39. Glycosyltransferase Family 39.
Proteomic databases
PaxDb	Q9W5D4.
PRIDE	Q9W5D4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0070139; FBpp0070134; FBgn0086368.
GeneID	31024.
KEGG	dme:Dmel_CG12311.
Organism-specific databases
CTD	8168.
FlyBase	FBgn0086368. tw.
Phylogenomic databases
eggNOG	COG1928.
GeneTree	ENSGT00700000104570.
InParanoid	Q9W5D4.
KO	K00728.
OMA	WPINYRG.
OrthoDB	EOG44B8H7.
PhylomeDB	Q9W5D4.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	Q9W5D4.
GermOnline	CG12311. Drosophila melanogaster.
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...
Other
GenomeRNAi	31024.
NextBio	771564.

Entry information

Entry name

POMT2_DROME

Accession

Primary (citable) accession number: Q9W5D4
Secondary accession number(s): O77437

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project