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   24-JAN-2024, entry version 145.
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   GlyCosmos; Q99PR0; 3 sites, 2 glycans.
DR   GlyGen; Q99PR0; 3 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; Q99PR0; -.
DR   PhosphoSitePlus; Q99PR0; -.
DR   PaxDb; 10116-ENSRNOP00000015214; -.
DR   Ensembl; ENSRNOT00000015214.5; ENSRNOP00000015214.3; ENSRNOG00000010477.7.
DR   Ensembl; ENSRNOT00065045653; ENSRNOP00065037435; ENSRNOG00065026419.
DR   GeneID; 84430; -.
DR   KEGG; rno:84430; -.
DR   UCSC; RGD:620078; rat.
DR   AGR; RGD:620078; -.
DR   CTD; 10585; -.
DR   RGD; 620078; Pomt1.
DR   eggNOG; KOG3359; Eukaryota.
DR   GeneTree; ENSGT00940000158049; -.
DR   InParanoid; Q99PR0; -.
DR   OMA; NCHLNAP; -.
DR   OrthoDB; 5489060at2759; -.
DR   PhylomeDB; Q99PR0; -.
DR   TreeFam; TF300552; -.
DR   BRENDA; 2.4.1.109; 5301.
DR   Reactome; R-RNO-5173105; O-linked glycosylation.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q99PR0; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000010477; Expressed in testis and 19 other cell types or tissues.
DR   ExpressionAtlas; Q99PR0; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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   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:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 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; MIR domain; 1.
DR   PROSITE; PS50919; MIR; 3.
DR   Genevisible; Q99PR0; RN.
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
//