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Protein

Protein O-mannosyl-transferase 1

Gene

Pomt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

Dolichyl D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein.By similarity

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. extracellular matrix organization Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

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 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2138994. Pomt1.

Subcellular locationi

Topology

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

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
Complete GO annotation...

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

MaxQBiQ8R2R1.
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

BgeeiQ8R2R1.
CleanExiMM_POMT1.
ExpressionAtlasiQ8R2R1. baseline and differential.
GenevestigatoriQ8R2R1.

Structurei

3D structure databases

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

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.
OMAiLTYPRAV.
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

« Hide

        10         20         30         40         50
MGSHSTGLEE TLGVLPSWLF CKMLRFLKRP LVVTVDINLN LVALTGLGLL
60 70 80 90 100
TRLWQLSYPR AVVFDEVYYG QYISFYMKRI FFLDDSGPPF GHMLLALGGW
110 120 130 140 150
LGGFDGNFLW NRIGAEYSSN VPIWSLRLLP ALAGALSVPM AYQIVLELHF
160 170 180 190 200
SHGAAIGAAL LMLIENALIT QSRLMLLESI LIFFNLLAVL SYLKFFNSQT
210 220 230 240 250
HSPFSVHWWL WLLLTGVSCS CAVGIKYMGI FTYLLVLGIA AVHAWNLIGD
260 270 280 290 300
QTLSNMRVLS HLLARIVALL VVPVFLYLLF FYVHLMLLYR SGPHDQIMSS
310 320 330 340 350
AFQASLEGGL ARITQGQPLE VAFGSQVTLK SVSGKPLPCW LHSHKNTYPM
360 370 380 390 400
IYENGRGSSH QQQVTCYPFK DINNWWIVKD PGRHQLVVNN PPRPVRHGDI
410 420 430 440 450
VQLVHGMTTR LLNTHDVAAP LSPHSQEVSC YIDYNISMPA QNLWKLDIVN
460 470 480 490 500
RESNRDTWKT ILSEVRFVHV NTSAILKLSG AHLPDWGFRQ LEVVGEKLSP
510 520 530 540 550
GYHESMVWNV EEHRYGKSHE QKERELELHS PTQLDISRNL SFMARFSELQ
560 570 580 590 600
WKMLTLKNED LEHQYSSTPL EWLTLDTNIA YWLHPRTSAQ IHLLGNIVIW
610 620 630 640 650
TSASLATVVY TLLFFWYLLR RRRSICDLPE DAWSRWVLAG ALCTGGWALN
660 670 680 690 700
YLPFFLMERV LFLYHYLPAL TFQILLLPIV LQHASDHLCR SQLQRNVFSA
710 720 730 740
LVVAWYSSAC HVSNMLRPLT YGDTSLSPGE LRALRWKDSW DILIRK
Length:746
Mass (Da):85,234
Last modified:May 31, 2002 - v1
Checksum:i05CB97DFC79BAE0A
GO

Sequence cautioni

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

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

PTM databases

PhosphoSiteiQ8R2R1.

Proteomic databases

MaxQBiQ8R2R1.
PaxDbiQ8R2R1.
PRIDEiQ8R2R1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10585.
MGIiMGI:2138994. Pomt1.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi353755.
PROiQ8R2R1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R2R1.
CleanExiMM_POMT1.
ExpressionAtlasiQ8R2R1. baseline and differential.
GenevestigatoriQ8R2R1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A putative mouse O-mannosyltransferase mPOMT1."
    Wang X., Jigami Y.
    Submitted (JUL-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(2004) [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(2003) [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 19, 2003
Last sequence update: May 31, 2002
Last modified: March 3, 2015
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.