POMT2_DROME
ID POMT2_DROME Reviewed; 765 AA.
AC Q9W5D4; O77437;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein O-mannosyl-transferase 2;
DE EC=2.4.1.109;
DE AltName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 2;
DE Short=DmPOMT2;
DE Short=dPOMT2;
DE AltName: Full=Protein twisted;
GN Name=tw; Synonyms=Pomt2; ORFNames=CG12311;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD54755.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15271988; DOI=10.1074/jbc.m404900200;
RA Ichimiya T., Manya H., Ohmae Y., Yoshida H., Takahashi K., Ueda R.,
RA Endo T., Nishihara S.;
RT "The twisted abdomen phenotype of Drosophila POMT1 and POMT2 mutants
RT coincides with their heterophilic protein O-mannosyltransferase activity.";
RL J. Biol. Chem. 279:42638-42647(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE TW[1]), FUNCTION, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16219785; DOI=10.1534/genetics.105.049650;
RA Lyalin D., Koles K., Roosendaal S.D., Repnikova E., Van Wechel L.,
RA Panin V.M.;
RT "The twisted gene encodes Drosophila protein O-mannosyltransferase 2 and
RT genetically interacts with the rotated abdomen gene encoding Drosophila
RT protein O-mannosyltransferase 1.";
RL Genetics 172:343-353(2006).
RN [3] {ECO:0000312|EMBL:AAF45548.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF45548.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000312|EMBL:CAA20897.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6] {ECO:0000312|EMBL:AAM12256.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM12256.1};
RC TISSUE=Larva {ECO:0000269|PubMed:12537569}, and
RC Pupae {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Rt/POMT1 and tw/POMT2 function as a protein O-
CC mannosyltransferase in association with each other to generate and
CC maintain normal muscle development. {ECO:0000269|PubMed:15271988,
CC ECO:0000269|PubMed:16219785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with Rt/POMT1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16219785}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16219785}.
CC -!- TISSUE SPECIFICITY: At the cellular blastoderm stage, expression
CC accumulates in the ventrally located mesoderm primordium. At germ band
CC extension, mesoderm expression is seen as stripes of strong expression.
CC A very strong signal is also detected in the invaginating gut. As the
CC germ band retracts, mesodermal expression decays and becomes restricted
CC to somatic muscle precursors. {ECO:0000269|PubMed:15271988}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development; expression peaks
CC at embryonic stages 8-16. {ECO:0000269|PubMed:15271988,
CC ECO:0000269|PubMed:16219785}.
CC -!- DISRUPTION PHENOTYPE: Death during development, the few adult escapers
CC exhibit clockwise rotation of the abdomen.
CC {ECO:0000269|PubMed:15271988}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20897.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB176551; BAD54755.1; -; mRNA.
DR EMBL; AE014298; AAF45548.1; -; Genomic_DNA.
DR EMBL; AL031583; CAA20897.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY095525; AAM12256.1; -; mRNA.
DR PIR; T13483; T13483.
DR RefSeq; NP_001259102.1; NM_001272173.1.
DR RefSeq; NP_569858.1; NM_130502.3.
DR AlphaFoldDB; Q9W5D4; -.
DR SMR; Q9W5D4; -.
DR BioGRID; 57592; 2.
DR STRING; 7227.FBpp0070134; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR GlyGen; Q9W5D4; 7 sites.
DR PaxDb; Q9W5D4; -.
DR EnsemblMetazoa; FBtr0070139; FBpp0070134; FBgn0086368.
DR EnsemblMetazoa; FBtr0335403; FBpp0307386; FBgn0086368.
DR GeneID; 31024; -.
DR KEGG; dme:Dmel_CG12311; -.
DR CTD; 8168; -.
DR FlyBase; FBgn0086368; tw.
DR VEuPathDB; VectorBase:FBgn0086368; -.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000156829; -.
DR HOGENOM; CLU_008438_5_0_1; -.
DR InParanoid; Q9W5D4; -.
DR OMA; DANDVWR; -.
DR OrthoDB; 203029at2759; -.
DR PhylomeDB; Q9W5D4; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 31024; 0 hits in 1 CRISPR screen.
DR ChiTaRS; tws; fly.
DR GenomeRNAi; 31024; -.
DR PRO; PR:Q9W5D4; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0086368; Expressed in eye disc (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9W5D4; baseline and differential.
DR Genevisible; Q9W5D4; DM.
DR GO; GO:0031502; C:dolichyl-phosphate-mannose-protein mannosyltransferase complex; IDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016203; P:muscle attachment; IGI:FlyBase.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; IDA:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IGI:FlyBase.
DR GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; SSF82109; 1.
DR PROSITE; PS50919; MIR; 3.
PE 2: Evidence at transcript level;
KW Developmental protein; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..765
FT /note="Protein O-mannosyl-transferase 2"
FT /id="PRO_0000121490"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 318..374
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 384..440
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 445..501
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 59
FT /note="T -> GS (in allele tw[1])"
SQ SEQUENCE 765 AA; 86250 MW; 250CC8486330CB94 CRC64;
MAASVVKTPK CPRRGSVKDV AQNAPRTAPT SSKEANWNWW LLLATVFLVT FATRFYKVTE
PDHICWDETH FGKMGSWYIN RTFFFDVHPP LGKMLIGLSG YLTGYNGTFP FEKPGDKYNE
TRYQGMRYFC TTLGALIMPM GFDTVYDLTR SHEAALLAAA YLIFDVGLLT LNQYILLDPI
LLFFMMASVW GMVKVSKSTA SGGSYGLRWW LWLFLTGTML SCTISVKFVG LFVVLLVGLH
TATELWLILG DLGQPILETV KQLACRAITL IVWPVLLYIL FFYIHLSVLN RSGNGDGFYS
SAFQSRLIGN SLYNASMPRD VAYGSLVTIK NHKTGGGYLH SHHHLYPKGS GARQQQVTTY
THKDENNKWL IRPHNKPGPP KGKVQILRHG DLVRLTHMAT RRNLHSHNEP APMTKKHLQV
TGYGELGLGD ANDVWRVLIV GGKVNETVHT VTSRLKFIHL LQNCALTSSG KQLPKWGFEQ
QEVSCNPNVR DKNSQWNVED NEHKLMPSVS FSVYAPGFFA RFLESHAVML QGNAGLKPKE
GEVTSRPWQW PINYRGQFFS GSSYRIYLLG NPLIWWSNLV FLALFVTVFL CNAVVQQRRA
GFARSAAQNQ AQVPDSETVA QDEESEHSTT DICSCCTPAK EIVPKAVPSG SPEAPNPAQS
LRAAAWLFLG WMLHYLPFWA MGRVLYFHHY FPALIFNSLL TGVMYNYILR VLPKWIHHVI
LGLVLSILVY SFAAFSPLAY GMSGPLANEP NSTMYNLKWL STWEF
