POMT1_MOUSE
ID POMT1_MOUSE Reviewed; 746 AA.
AC Q8R2R1; Q3UYD8; Q64J18; Q8BPJ6; Q8BPU1; Q8R474;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Wang X., Jigami Y.;
RT "A putative mouse O-mannosyltransferase mPOMT1.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX PubMed=15383666; DOI=10.1073/pnas.0405899101;
RA Willer T., Prados B., Falcon-Perez J.M., Renner-Mueller I.,
RA Przemeck G.K.H., Lommel M., Coloma A., Valero M.C., De Angelis M.H.,
RA Tanner W., Wolf E., Strahl S., Cruces J.;
RT "Targeted disruption of the Walker-Warburg syndrome gene Pomt1 in mouse
RT results in embryonic lethality.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14126-14131(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Medulla oblongata, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- DEVELOPMENTAL STAGE: Expressed ubiquitously at low level after 7.5 dpc.
CC At 8.5 dpc high levels of expression are detected throughout the neural
CC tube, and in the dorsal aspects of the neural folds of the future
CC midbrain region and the somites. At 9.0 dpc high levels of expression
CC are detected in the ventral domain of the neural tube, developing eye,
CC floor plate, notochord, and gut endothelium. At 10.5 dpc expression
CC high levels of expression are detected in the dermomyotome of the
CC somites, limb-bud mesenchyme, mantle layer of the dorsal neural tube,
CC and developing trigeminal ganglion. {ECO:0000269|PubMed:15383666}.
CC -!- DISRUPTION PHENOTYPE: Mice suffer of developmental arrest around 7.5
CC dpc and die between 7.5 dpc and 9.5 dpc. Defects are observed in the
CC formation of Reichert's membrane that are probably due to abnormal
CC glycosylation and maturation of dystroglycan and impaired recruitment
CC of laminin. {ECO:0000269|PubMed:15383666}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35577.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY007238; AAG15588.1; -; mRNA.
DR EMBL; AY494857; AAS76201.1; -; mRNA.
DR EMBL; AK053889; BAC35577.1; ALT_FRAME; mRNA.
DR EMBL; AK134770; BAE22274.1; -; mRNA.
DR EMBL; AK153984; BAE32295.1; -; mRNA.
DR EMBL; BC027325; AAH27325.1; -; mRNA.
DR CCDS; CCDS15908.1; -.
DR RefSeq; NP_660127.1; NM_145145.1.
DR AlphaFoldDB; Q8R2R1; -.
DR SMR; Q8R2R1; -.
DR STRING; 10090.ENSMUSP00000038722; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR GlyConnect; 2639; 3 N-Linked glycans (1 site).
DR GlyGen; Q8R2R1; 3 sites, 3 N-linked glycans (1 site).
DR PhosphoSitePlus; Q8R2R1; -.
DR EPD; Q8R2R1; -.
DR MaxQB; Q8R2R1; -.
DR PaxDb; Q8R2R1; -.
DR PeptideAtlas; Q8R2R1; -.
DR PRIDE; Q8R2R1; -.
DR ProteomicsDB; 289786; -.
DR Antibodypedia; 31602; 191 antibodies from 27 providers.
DR DNASU; 99011; -.
DR Ensembl; ENSMUST00000036473; ENSMUSP00000038722; ENSMUSG00000039254.
DR GeneID; 99011; -.
DR KEGG; mmu:99011; -.
DR UCSC; uc008jeq.1; mouse.
DR CTD; 10585; -.
DR MGI; MGI:2138994; Pomt1.
DR VEuPathDB; HostDB:ENSMUSG00000039254; -.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000158049; -.
DR HOGENOM; CLU_008438_1_0_1; -.
DR InParanoid; Q8R2R1; -.
DR OMA; FWTQNDT; -.
DR OrthoDB; 203029at2759; -.
DR PhylomeDB; Q8R2R1; -.
DR TreeFam; TF300552; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 99011; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Pomt1; mouse.
DR PRO; PR:Q8R2R1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R2R1; protein.
DR Bgee; ENSMUSG00000039254; Expressed in spermatocyte and 254 other tissues.
DR ExpressionAtlas; Q8R2R1; baseline and differential.
DR Genevisible; Q8R2R1; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
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; IDA:MGI.
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; IMP:MGI.
DR GO; GO:1904100; P:positive regulation of protein O-linked glycosylation; ISO:MGI.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..746
FT /note="Protein O-mannosyl-transferase 1"
FT /id="PRO_0000121485"
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 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
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"
FT CONFLICT 2
FT /note="G -> S (in Ref. 3; BAC35577)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="R -> P (in Ref. 1; AAG15588)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="P -> H (in Ref. 3; BAE22274)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="K -> E (in Ref. 1; AAG15588)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 85234 MW; 05CB97DFC79BAE0A CRC64;
MGSHSTGLEE TLGVLPSWLF CKMLRFLKRP LVVTVDINLN LVALTGLGLL TRLWQLSYPR
AVVFDEVYYG QYISFYMKRI FFLDDSGPPF GHMLLALGGW LGGFDGNFLW NRIGAEYSSN
VPIWSLRLLP ALAGALSVPM AYQIVLELHF SHGAAIGAAL LMLIENALIT QSRLMLLESI
LIFFNLLAVL SYLKFFNSQT HSPFSVHWWL WLLLTGVSCS CAVGIKYMGI FTYLLVLGIA
AVHAWNLIGD QTLSNMRVLS HLLARIVALL VVPVFLYLLF FYVHLMLLYR SGPHDQIMSS
AFQASLEGGL ARITQGQPLE VAFGSQVTLK SVSGKPLPCW LHSHKNTYPM IYENGRGSSH
QQQVTCYPFK DINNWWIVKD PGRHQLVVNN PPRPVRHGDI VQLVHGMTTR LLNTHDVAAP
LSPHSQEVSC YIDYNISMPA QNLWKLDIVN RESNRDTWKT ILSEVRFVHV NTSAILKLSG
AHLPDWGFRQ LEVVGEKLSP GYHESMVWNV EEHRYGKSHE QKERELELHS PTQLDISRNL
SFMARFSELQ WKMLTLKNED LEHQYSSTPL EWLTLDTNIA YWLHPRTSAQ IHLLGNIVIW
TSASLATVVY TLLFFWYLLR RRRSICDLPE DAWSRWVLAG ALCTGGWALN YLPFFLMERV
LFLYHYLPAL TFQILLLPIV LQHASDHLCR SQLQRNVFSA LVVAWYSSAC HVSNMLRPLT
YGDTSLSPGE LRALRWKDSW DILIRK
