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Q8R2R1

- POMT1_MOUSE

UniProt

Q8R2R1 - POMT1_MOUSE

Protein

Protein O-mannosyl-transferase 1

Gene

Pomt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Transfers mannosyl residues to the hydroxyl group of serine or threonine residues.By similarity

    Catalytic activityi

    Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.

    Cofactori

    Magnesium.By similarity

    Pathwayi

    GO - Molecular functioni

    1. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. extracellular matrix organization Source: MGI

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT39. Glycosyltransferase Family 39.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein O-mannosyl-transferase 1 (EC:2.4.1.109)
    Alternative name(s):
    Dolichyl-phosphate-mannose--protein mannosyltransferase 1
    Gene namesi
    Name:Pomt1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2138994. Pomt1.

    Subcellular locationi

    GO - Cellular componenti

    1. acrosomal vesicle Source: MGI
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. sarcoplasmic reticulum Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice suffer of developmental arrest around E7.5 and die between E7.5 and E9.5. Defects are observed in the formation of Reichert's membrane that are probably due to abnormal glycosylation and maturation of dystroglycan and impaired recruitment of laminin.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 746746Protein O-mannosyl-transferase 1PRO_0000121485Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi435 – 4351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ8R2R1.
    PRIDEiQ8R2R1.

    PTM databases

    PhosphoSiteiQ8R2R1.

    Expressioni

    Developmental stagei

    Expressed ubiquitously at low level after E7.5. At E8.5 high levels of expression are detected throughout the neural tube, and in the dorsal aspects of the neural folds of the future midbrain region and the somites. At E9.0 high levels of expression are detected in the ventral domain of the neural tube, developing eye, floor plate, notochord, and gut endothelium. At E10.5 expression high levels of expression are detected in the dermomyotome of the somites, limb-bud mesenchyme, mantle layer of the dorsal neural tube, and developing trigeminal ganglion.1 Publication

    Gene expression databases

    ArrayExpressiQ8R2R1.
    BgeeiQ8R2R1.
    CleanExiMM_POMT1.
    GenevestigatoriQ8R2R1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8R2R1.
    SMRiQ8R2R1. Positions 319-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei30 – 5021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei90 – 11021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei121 – 14121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei144 – 16421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei176 – 19621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei228 – 24821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei266 – 28621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei597 – 61721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei636 – 65621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei660 – 68021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini318 – 38164MIR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini392 – 44958MIR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini453 – 51361MIR 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyltransferase 39 family.Curated
    Contains 3 MIR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1928.
    GeneTreeiENSGT00740000115531.
    HOGENOMiHOG000157526.
    HOVERGENiHBG053637.
    InParanoidiQ8R2R1.
    KOiK00728.
    OMAiLLFFYVH.
    OrthoDBiEOG79KPDP.
    PhylomeDBiQ8R2R1.
    TreeFamiTF300552.

    Family and domain databases

    InterProiIPR027005. GlyclTrfase_39_like.
    IPR003342. Glyco_trans_39.
    IPR016093. MIR_motif.
    [Graphical view]
    PANTHERiPTHR10050. PTHR10050. 1 hit.
    PfamiPF02815. MIR. 1 hit.
    PF02366. PMT. 1 hit.
    [Graphical view]
    SMARTiSM00472. MIR. 3 hits.
    [Graphical view]
    SUPFAMiSSF82109. SSF82109. 1 hit.
    PROSITEiPS50919. MIR. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8R2R1-1 [UniParc]FASTAAdd to Basket

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    MGSHSTGLEE TLGVLPSWLF CKMLRFLKRP LVVTVDINLN LVALTGLGLL    50
    TRLWQLSYPR AVVFDEVYYG QYISFYMKRI FFLDDSGPPF GHMLLALGGW 100
    LGGFDGNFLW NRIGAEYSSN VPIWSLRLLP ALAGALSVPM AYQIVLELHF 150
    SHGAAIGAAL LMLIENALIT QSRLMLLESI LIFFNLLAVL SYLKFFNSQT 200
    HSPFSVHWWL WLLLTGVSCS CAVGIKYMGI FTYLLVLGIA AVHAWNLIGD 250
    QTLSNMRVLS HLLARIVALL VVPVFLYLLF FYVHLMLLYR SGPHDQIMSS 300
    AFQASLEGGL ARITQGQPLE VAFGSQVTLK SVSGKPLPCW LHSHKNTYPM 350
    IYENGRGSSH QQQVTCYPFK DINNWWIVKD PGRHQLVVNN PPRPVRHGDI 400
    VQLVHGMTTR LLNTHDVAAP LSPHSQEVSC YIDYNISMPA QNLWKLDIVN 450
    RESNRDTWKT ILSEVRFVHV NTSAILKLSG AHLPDWGFRQ LEVVGEKLSP 500
    GYHESMVWNV EEHRYGKSHE QKERELELHS PTQLDISRNL SFMARFSELQ 550
    WKMLTLKNED LEHQYSSTPL EWLTLDTNIA YWLHPRTSAQ IHLLGNIVIW 600
    TSASLATVVY TLLFFWYLLR RRRSICDLPE DAWSRWVLAG ALCTGGWALN 650
    YLPFFLMERV LFLYHYLPAL TFQILLLPIV LQHASDHLCR SQLQRNVFSA 700
    LVVAWYSSAC HVSNMLRPLT YGDTSLSPGE LRALRWKDSW DILIRK 746
    Length:746
    Mass (Da):85,234
    Last modified:June 1, 2002 - v1
    Checksum:i05CB97DFC79BAE0A
    GO

    Sequence cautioni

    The sequence BAC35577.1 differs from that shown. Reason: Frameshift at position 255.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21G → S in BAC35577. (PubMed:16141072)Curated
    Sequence conflicti257 – 2571R → P in AAG15588. 1 PublicationCurated
    Sequence conflicti318 – 3181P → H in BAE22274. (PubMed:16141072)Curated
    Sequence conflicti330 – 3301K → E in AAG15588. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007238 mRNA. Translation: AAG15588.1.
    AY494857 mRNA. Translation: AAS76201.1.
    AK053889 mRNA. Translation: BAC35577.1. Frameshift.
    AK134770 mRNA. Translation: BAE22274.1.
    AK153984 mRNA. Translation: BAE32295.1.
    BC027325 mRNA. Translation: AAH27325.1.
    CCDSiCCDS15908.1.
    RefSeqiNP_660127.1. NM_145145.1.
    UniGeneiMm.31192.

    Genome annotation databases

    EnsembliENSMUST00000036473; ENSMUSP00000038722; ENSMUSG00000039254.
    GeneIDi99011.
    KEGGimmu:99011.
    UCSCiuc008jeq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY007238 mRNA. Translation: AAG15588.1 .
    AY494857 mRNA. Translation: AAS76201.1 .
    AK053889 mRNA. Translation: BAC35577.1 . Frameshift.
    AK134770 mRNA. Translation: BAE22274.1 .
    AK153984 mRNA. Translation: BAE32295.1 .
    BC027325 mRNA. Translation: AAH27325.1 .
    CCDSi CCDS15908.1.
    RefSeqi NP_660127.1. NM_145145.1.
    UniGenei Mm.31192.

    3D structure databases

    ProteinModelPortali Q8R2R1.
    SMRi Q8R2R1. Positions 319-476.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT39. Glycosyltransferase Family 39.

    PTM databases

    PhosphoSitei Q8R2R1.

    Proteomic databases

    PaxDbi Q8R2R1.
    PRIDEi Q8R2R1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000036473 ; ENSMUSP00000038722 ; ENSMUSG00000039254 .
    GeneIDi 99011.
    KEGGi mmu:99011.
    UCSCi uc008jeq.1. mouse.

    Organism-specific databases

    CTDi 10585.
    MGIi MGI:2138994. Pomt1.

    Phylogenomic databases

    eggNOGi COG1928.
    GeneTreei ENSGT00740000115531.
    HOGENOMi HOG000157526.
    HOVERGENi HBG053637.
    InParanoidi Q8R2R1.
    KOi K00728.
    OMAi LLFFYVH.
    OrthoDBi EOG79KPDP.
    PhylomeDBi Q8R2R1.
    TreeFami TF300552.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    NextBioi 353755.
    PROi Q8R2R1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8R2R1.
    Bgeei Q8R2R1.
    CleanExi MM_POMT1.
    Genevestigatori Q8R2R1.

    Family and domain databases

    InterProi IPR027005. GlyclTrfase_39_like.
    IPR003342. Glyco_trans_39.
    IPR016093. MIR_motif.
    [Graphical view ]
    PANTHERi PTHR10050. PTHR10050. 1 hit.
    Pfami PF02815. MIR. 1 hit.
    PF02366. PMT. 1 hit.
    [Graphical view ]
    SMARTi SM00472. MIR. 3 hits.
    [Graphical view ]
    SUPFAMi SSF82109. SSF82109. 1 hit.
    PROSITEi PS50919. MIR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A putative mouse O-mannosyltransferase mPOMT1."
      Wang X., Jigami Y.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
      Strain: Swiss Webster / NIH.
      Tissue: Embryo.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Eye, Medulla oblongata and Thymus.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiPOMT1_MOUSE
    AccessioniPrimary (citable) accession number: Q8R2R1
    Secondary accession number(s): Q3UYD8
    , Q64J18, Q8BPJ6, Q8BPU1, Q8R474
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3