POMT1_DROPS
ID POMT1_DROPS Reviewed; 908 AA.
AC Q2LZ62;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein O-mannosyltransferase 1;
DE EC=2.4.1.109;
DE AltName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 1;
DE AltName: Full=Protein rotated abdomen;
GN Name=rt {ECO:0000250|UniProtKB:Q9VTK2}; ORFNames=GA19350;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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:0000250}.
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; Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with tw/POMT2. {ECO:0000250|UniProtKB:Q9VTK2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9VTK2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9VTK2}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000255}.
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DR EMBL; CH379069; EAL29647.2; -; Genomic_DNA.
DR RefSeq; XP_001353911.2; XM_001353875.3.
DR AlphaFoldDB; Q2LZ62; -.
DR SMR; Q2LZ62; -.
DR STRING; 7237.FBpp0275409; -.
DR PRIDE; Q2LZ62; -.
DR EnsemblMetazoa; FBtr0276971; FBpp0275409; FBgn0079347.
DR GeneID; 4813592; -.
DR KEGG; dpo:Dpse_GA19350; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_1_0_1; -.
DR InParanoid; Q2LZ62; -.
DR OMA; FWTQNDT; -.
DR UniPathway; UPA00378; -.
DR ChiTaRS; rt; fly.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0079347; Expressed in female reproductive system and 1 other tissue.
DR GO; GO:0031502; C:dolichyl-phosphate-mannose-protein mannosyltransferase complex; IEA:EnsemblMetazoa.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016203; P:muscle attachment; IEA:EnsemblMetazoa.
DR GO; GO:0007517; P:muscle organ development; ISS:UniProtKB.
DR GO; GO:0060025; P:regulation of synaptic activity; IEA:EnsemblMetazoa.
DR GO; GO:0045214; P:sarcomere organization; IEA:EnsemblMetazoa.
DR GO; GO:0007525; P:somatic muscle development; IEA:EnsemblMetazoa.
DR GO; GO:0007385; P:specification of segmental identity, abdomen; ISS: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 3: Inferred from homology;
KW Developmental protein; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..908
FT /note="Protein O-mannosyltransferase 1"
FT /id="PRO_0000307926"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 788..808
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 473..534
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 545..602
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 608..664
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 908 AA; 102912 MW; 3D0182C4D63416C4 CRC64;
MYNNNNDGGG GGSANGNTMQ QRRKTTTRSR SKQQQQQQCT SENVIEKNQT NGAQNERLHF
RGSSKDSALS TPLLPRSRST TSAINSPSPL CCNGGLSILN CCRDVNCHLN APLRGSVESS
RSRRSESRQS SLTATPTTTP KQASPSPTIS ERSRSCSGSR SRSCSCDGRL VDCHKHSAAA
AAASTAAPQF TVNLSIDLFS WTLFLLAFCT RFYKLATPPH IVFDELHYGK YIAHYMRNIF
FFDQHPPLGK QLIAGLVSLA GYDGNYTFSR IGAAYAPDVP IFWFRFIPAL CGSLLAPAVY
RLLLEARLHR WAAALGGLLV VLDNSLLTQS RFVLMESMLL LASTLGIACL LRFQRCRLGS
FQWLCNGSAA GVLLACAGAV KYIGFLALAL AGYLLCRHLW QLLYDASLTN RQLWMHALSR
LLLFVGIPIA VYIGVFYVHF RTLHRAGPHD SIMTSAFQAS LEGGLASITS GQPLAVVHGS
QITLRHTHGR TCWLHSHAAV YPVRYKDKRG SSHQQQVTCY SFKDVNNWWI VKRPERDDLV
VGEQPDVIQH GDVIQLVHGI TSRALNSHDV AAPMTPQCQE VSCYIDYEIK MAGELLWRVE
ILNRNSEGDS WHAIKSEIRL VHESTGAALK FSGRQLPDWG FNQHEVVADR DQVHEDAIWN
VEEHRYTKTQ DQRERERQLL SAEMIPTKRT KLSFWAKLLE LQTKMFWHGK HLQAHMYSSL
PHEWPLMDKG IAYWLDSQSS AQIYLLGNVL IWYTASAGIL VYATLLAFYA VRRRRLCFDV
SQHEWQRFLM AGDTFFVGYM MHYLPYYFVD RTLFLHNYLP AFVFKLLLLC FVVEHLDYLL
RRHCSGRGVH LVRVYRLALL LWLLAVGSVF VKFLPLSYGA RKMTIEEVRR LRWKDTWDFI
LQKNYALN
