POMT1_DROME
ID POMT1_DROME Reviewed; 886 AA.
AC Q9VTK2; Q60GL9; Q8SYW7; Q94891;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein O-mannosyltransferase 1;
DE EC=2.4.1.109;
DE AltName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 1;
DE Short=dPOMT1;
DE AltName: Full=Protein rotated abdomen;
GN Name=rt {ECO:0000312|EMBL:AAF50046.2};
GN Synonyms=POMT1 {ECO:0000312|EMBL:BAD54754.1}; ORFNames=CG6097;
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:CAA65194.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=8650217; DOI=10.1073/pnas.93.12.6048;
RA Martin-Blanco E., Garcia-Bellido A.;
RT "Mutations in the rotated abdomen locus affect muscle development and
RT reveal an intrinsic asymmetry in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:6048-6052(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD54754.1}
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 [3] {ECO:0000312|EMBL:AAF50046.2}
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:AAF50046.2}
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:AAL48892.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48892.1};
RC TISSUE=Embryo {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).
RN [6]
RP FUNCTION, SUBCELLULAR 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).
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, ECO:0000269|PubMed:8650217}.
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 tw/POMT2. {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. After dorsal closure, expression has
CC disappeared from the mesoderm and remains in the endoderm. Some
CC expression is detected in a few cells of the head and the pharyngeal
CC muscles. {ECO:0000269|PubMed:15271988, ECO:0000269|PubMed:8650217}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression peaks at embryonic stages 8-16.
CC {ECO:0000269|PubMed:15271988, ECO:0000269|PubMed:16219785,
CC ECO:0000269|PubMed:8650217}.
CC -!- DISRUPTION PHENOTYPE: Death during development, the few adult escapers
CC exhibit clockwise rotation of the abdomen and defects in embryonic
CC muscle development. {ECO:0000269|PubMed:15271988,
CC ECO:0000269|PubMed:8650217}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48892.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=CAA65194.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X95956; CAA65194.1; ALT_FRAME; mRNA.
DR EMBL; AB176550; BAD54754.1; -; mRNA.
DR EMBL; AE014296; AAF50046.2; -; Genomic_DNA.
DR EMBL; AY071270; AAL48892.1; ALT_SEQ; mRNA.
DR RefSeq; NP_524025.2; NM_079301.4.
DR AlphaFoldDB; Q9VTK2; -.
DR SMR; Q9VTK2; -.
DR BioGRID; 64662; 2.
DR IntAct; Q9VTK2; 3.
DR STRING; 7227.FBpp0075877; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR GlyGen; Q9VTK2; 2 sites.
DR PaxDb; Q9VTK2; -.
DR PRIDE; Q9VTK2; -.
DR EnsemblMetazoa; FBtr0076146; FBpp0075877; FBgn0003292.
DR GeneID; 39297; -.
DR KEGG; dme:Dmel_CG6097; -.
DR CTD; 39297; -.
DR FlyBase; FBgn0003292; rt.
DR VEuPathDB; VectorBase:FBgn0003292; -.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000158049; -.
DR HOGENOM; CLU_008438_1_0_1; -.
DR InParanoid; Q9VTK2; -.
DR OMA; FWTQNDT; -.
DR OrthoDB; 203029at2759; -.
DR PhylomeDB; Q9VTK2; -.
DR SignaLink; Q9VTK2; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 39297; 0 hits in 1 CRISPR screen.
DR ChiTaRS; rt; fly.
DR GenomeRNAi; 39297; -.
DR PRO; PR:Q9VTK2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003292; Expressed in capitellum (Drosophila) and 20 other tissues.
DR Genevisible; Q9VTK2; 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:0060025; P:regulation of synaptic activity; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IGI:FlyBase.
DR GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR GO; GO:0007385; P:specification of segmental identity, abdomen; IMP:UniProtKB.
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..886
FT /note="Protein O-mannosyltransferase 1"
FT /id="PRO_0000121487"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 450..511
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 522..579
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 585..642
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 87..90
FT /note="LRGS -> APGR (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> T (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..229
FT /note="QL -> TV (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 233..235
FT /note="LVS -> TGH (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="S -> I (in Ref. 5; AAL48892)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="A -> T (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 458..459
FT /note="QI -> KS (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 514..518
FT /note="ENLVV -> RTWWW (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="E -> K (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="E -> K (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="T -> I (in Ref. 2; BAD54754)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="R -> P (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="K -> R (in Ref. 5; AAL48892)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="V -> E (in Ref. 1; CAA65194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 101194 MW; 5147C832EC5BC275 CRC64;
MSATYTNTIT QRRKTAKVRQ QQQHQWTGSD LSGESNERLH FRSRSTNSMQ QHTAISNSPS
PLCCNGARAL TMLNCCVDVN CHLNAPLRGS VNRHTTPTPT PTATPTPVAT PKQASPSPTS
DRSRSLSRSP SPSRSRSLSC QKQIDKNSAG AASAEERKTA NASSQPFTVN LRIDLFSWTL
FLLAFGTRFY KLATPPHIVF DELHYGKYIS MYMRNIFFFD QHPPLGKQLI AGLVSLAGYD
GNYTFTRIGE PYSPEMPIFW FRFLPAMCGS LLAPAVYNLL LEAKLSRWSS ALGGLLVVLD
NSLLTQSRFV LMESMLLLAT TVGIACLLRF QRSRLGSLEW FFTGTAAAVC LGAAGTVKYV
GFLALGLAFY LLCRHLWQLL YDAGLTDRQL WMHAISRLLI FVGIPLAVYL GVFYIHFKTL
HRAGPHDSIM TSAFQASLDG GLASITKGQP LAVVHGSQIT LRHTHGRTCW LHSHAAVYPV
RYPDKRGSSH QQQVTCYSFK DVNNWWLVKR PTKENLVVGD EPDIIRHGEI IQLVHGITSR
ALNSHDVAAA MTPQCQEVSC YIDYEIKMAG ELLWRVEILN RDSEGDIWHA IKSEVRLVHV
STEASLKFSG RQLPEWGFNQ HEVVADREKA IHEDAIWNVE EHRYTQTEDH RERERQMLTA
EMIPTKRTRI SFWAKLLELQ SKMLFQTKSV PNHMYSSMPH EWPLMDKGIA YWLDSQSSAQ
IYLLGNILLW YTATMGILVY AGLLAFYAMR RQRLCFDISE QEWQRFVLAG DTFFMGYVMH
YIPYFCVDRT LFLHNYLPAF VFKLLLLCFV VEHLDYLLRR FCTGRGVHLV RLYRLMLILW
LVGVLSIFSK FIPFSYGARK MTLNEVRSLR WKDTWDFVLH KNHHLY
