POMT2_DROPS
ID POMT2_DROPS Reviewed; 749 AA.
AC Q29IL2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Protein O-mannosyl-transferase 2;
DE EC=2.4.1.109;
DE AltName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 2;
DE AltName: Full=Protein twisted;
GN Name=tw {ECO:0000250|UniProtKB:Q9W5D4}; ORFNames=GA11548;
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] {ECO:0000312|EMBL:EAL32641.1}
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 Rt/POMT1. {ECO:0000250|UniProtKB:Q9W5D4}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9W5D4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9W5D4}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL32641.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH379063; EAL32641.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001355582.1; XM_001355546.3.
DR AlphaFoldDB; Q29IL2; -.
DR SMR; Q29IL2; -.
DR STRING; 7237.FBpp0273533; -.
DR EnsemblMetazoa; FBtr0275095; FBpp0273533; FBgn0071599.
DR GeneID; 4815847; -.
DR KEGG; dpo:Dpse_GA11548; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_5_0_1; -.
DR InParanoid; Q29IL2; -.
DR OMA; DANDVWR; -.
DR PhylomeDB; Q29IL2; -.
DR UniPathway; UPA00378; -.
DR ChiTaRS; tws; fly.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0071599; Expressed in adult organism.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007517; P:muscle organ development; 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..749
FT /note="Protein O-mannosyl-transferase 2"
FT /id="PRO_0000307927"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 316..372
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 382..438
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 443..499
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 749 AA; 84957 MW; 4235318C19C91334 CRC64;
MAASVVKTPK CPRRGSAKEQ QSKASPKSNN ESNNWHWWIL LASVFLITFA TRFYKVTEPD
HICWDETHFG KMGSWYINRT FFFDVHPPLG KMLIGLSGYL TGYNGTFPFE KPGDKYNETA
YQGMRYFCTT LGALIMPMGF DTVYDLTRSH EAALLSAAYL IFDVGLLTLN QYILLDPILL
FFMMGSVWGM VKISKATASG GSYSVRWWFW LFLTGTMLSC TISVKFVGLF VVLLVGLHTA
TELWLILGDL GQPIVETLKQ IACRAIALIL WPILLYTLFF YIHLSVLNRS GNGDGFYSSA
FQSRLIGNSL YNASMPRDVA YGSVVTIKNH KTGGGYLHSH FHLYPKGSGA RQQQITTYTH
KDDNNKWVIK PHNKQRLPKD KLQLLRHGDL VRLEHLVTKR NLHSHSEPAP MTKKHLQVTG
YGESGVGDAN DVWRVLIVGG KVNETVHTVT SRLMLIHYLQ NCALTSSGKQ LPKWGFEQQE
VSCNLNVRDK YAHWNVEDNE HKLLPSVSFS VYAPGFFARF LESHAVMLQG NAGLKPKEGE
VTSRPWQWPI NYRGQFFSGS SYRIYLLGNP VIWWSNLVFL ALFVAVFLGN AILEQRRAGQ
ARALVRSQAD SEDSEPSTTD VPLCTCCPEE QQLLSRPREE HRDPLGAAAW LFVGWLLHYL
PFWAMGRVLY FHHYFPALIF NSLLTGVMFH HIIQSLPRWI QHVLLGGLLS LIVYSFALFS
PLAYGMSGPL ANEPNSTMHS LKWLSTWEF
