POMT1_RAT
ID POMT1_RAT Reviewed; 747 AA.
AC Q99PR0; Q6IRI2;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein O-mannosyl-transferase 1;
DE EC=2.4.1.109;
DE AltName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 1;
GN Name=Pomt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Chiba A., Ronca F., Popp S., Margolis R.U.;
RT "Molecular cloning of a rat homologue of the Saccharomyces protein O-
RT mannosyltransferase gene.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. Coexpression of both POMT1 and POMT2 is
CC necessary for enzyme activity, expression of either POMT1 or POMT2
CC alone is insufficient. Essentially dedicated to O-mannosylation of
CC alpha-DAG1 and few other proteins but not of cadherins and
CC protocaherins. {ECO:0000250|UniProtKB:Q9Y6A1}.
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 Evidence={ECO:0000250|UniProtKB:Q9Y6A1};
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 Evidence={ECO:0000250|UniProtKB:Q9Y6A1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH70912.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF192388; AAG53461.1; -; mRNA.
DR EMBL; BC070912; AAH70912.1; ALT_SEQ; mRNA.
DR RefSeq; NP_445858.1; NM_053406.2.
DR AlphaFoldDB; Q99PR0; -.
DR SMR; Q99PR0; -.
DR STRING; 10116.ENSRNOP00000015214; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR GlyGen; Q99PR0; 3 sites, 2 N-linked glycans (1 site).
DR PaxDb; Q99PR0; -.
DR Ensembl; ENSRNOT00000015214; ENSRNOP00000015214; ENSRNOG00000010477.
DR GeneID; 84430; -.
DR KEGG; rno:84430; -.
DR UCSC; RGD:620078; rat.
DR CTD; 10585; -.
DR RGD; 620078; Pomt1.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000158049; -.
DR InParanoid; Q99PR0; -.
DR OMA; FWTQNDT; -.
DR OrthoDB; 203029at2759; -.
DR PhylomeDB; Q99PR0; -.
DR TreeFam; TF300552; -.
DR BRENDA; 2.4.1.109; 5301.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q99PR0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000010477; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q99PR0; baseline and differential.
DR Genevisible; Q99PR0; RN.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:1904100; P:positive regulation of protein O-linked glycosylation; IDA:RGD.
DR GO; GO:0035269; P:protein O-linked mannosylation; 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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..747
FT /note="Protein O-mannosyl-transferase 1"
FT /id="PRO_0000121486"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 318..381
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 392..449
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 453..513
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 747 AA; 85496 MW; 7ECE8F752E7FFA89 CRC64;
MGNRSMGRED TLGVLPSLLF CKMLRFLKRP LVVTIDINLN LVALTVLGLL TRLWQLSYPR
AVVFDEVYYG QYISFYMKRV FFLDDSGPPF GHMLLALGGW LGGFDGNFLW NRIGAEYSSN
VPVWSLRLLP ALAGALSVPM AYQIVLELHF SHCTAMGAAL LMLIENALIT QSRLMLLESI
LIFFNLLAVL SYLKFFNSQT HSPFSVHWWL WLMLTGVSCS CAVGIKYMGI FTYLLVLSIA
AVHAWHLIGD QTLSNICVLS HLLARAVALL VVPVFLYLLF FYVHLMLLYR SGPHDQIMSS
AFQASLEGGL ARITQGQPLE VAFGSQVTLK SVSGKPLPCW LHSHKNTYPM IYENGRGSSH
QQQVTCYPFK DINNWWIVKD PGRHQLVVNN PPRPVRHGDI VQLVHGMTTR LLNTHDVAAP
LSPHSQEVSC YIDYNISMPA QNLWKLDIVN RESNQDTWKT ILSEVRFVHV NTSAILKLSG
AHLPDWGFRQ LEVVGEKLSL GPHESMVWNV EEHRYGRGHE QKERELELHS PTQHDISRNL
SFMARFSELQ WKMLTLKNED LEHQYSSTPL EWLTLDTNIA YWLHPRTSAQ IHLLGNIVIW
TSASLATVAY TLLFFWYLLR RRRNICDLPE DAWSHWVLAG ALCIGGWALN YLPFFLMERM
LFLYHYLPAL TFQILLLPIV MQHASDHLCR SQLQRNVFSA LVVAWYSSAC HVSNMLRPLT
YGDTSLSPGE LRALRWKDSW DILIRKY
