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   27-MAR-2024, entry version 153.
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 Pupae
RC   {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   ComplexPortal; CPX-2372; POMT1-POMT2 O-mannosyltransferase complex.
DR   STRING; 7227.FBpp0307386; -.
DR   CAZy; GT39; Glycosyltransferase Family 39.
DR   GlyCosmos; Q9W5D4; 7 sites, No reported glycans.
DR   GlyGen; Q9W5D4; 7 sites.
DR   PaxDb; 7227-FBpp0070134; -.
DR   EnsemblMetazoa; FBtr0070139; FBpp0070134; FBgn0086368.
DR   EnsemblMetazoa; FBtr0335403; FBpp0307386; FBgn0086368.
DR   GeneID; 31024; -.
DR   KEGG; dme:Dmel_CG12311; -.
DR   AGR; FB:FBgn0086368; -.
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; MCGWDDN; -.
DR   OrthoDB; 5489060at2759; -.
DR   PhylomeDB; Q9W5D4; -.
DR   Reactome; R-DME-5173105; O-linked glycosylation.
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 cell types or tissues.
DR   ExpressionAtlas; Q9W5D4; baseline and differential.
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: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   Gene3D; 2.80.10.50; -; 1.
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; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10050:SF46; PROTEIN O-MANNOSYL-TRANSFERASE 2; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF02366; PMT; 1.
DR   Pfam; PF16192; PMT_4TMC; 2.
DR   SMART; SM00472; MIR; 3.
DR   SUPFAM; SSF82109; MIR domain; 1.
DR   PROSITE; PS50919; MIR; 3.
DR   Genevisible; Q9W5D4; DM.
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
//