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Reviewed, UniProtKB/Swiss-Prot Q9EQY6 (PIGM_RAT)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    GPI mannosyltransferase 1
    EC=2.4.1.-
Alternative name(s):
    GPI mannosyltransferase I
      Short name=GPI-MT-I
    Phosphatidylinositol-glycan biosynthesis class M protein
      Short name=PIG-M
Gene names
Name: Pigm
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly By similarity.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the PIGM family.

Ontologies

Keywords
   Biological processGPI-anchor biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase
Gene Ontology (GO)
   Biological processGPI anchor biosynthetic process Ref.1

Inferred from direct assay. Source: RGD

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmannosyltransferase activity Ref.1

Inferred from direct assay. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423GPI mannosyltransferase 1
PRO_0000246217

Regions

Topological domain1 – 1717Cytoplasmic Potential
Transmembrane18 – 3821 Potential
Topological domain39 – 8951Lumenal Potential
Transmembrane90 – 11021 Potential
Topological domain111 – 16959Cytoplasmic Potential
Transmembrane170 – 19021 Potential
Topological domain191 – 22434Lumenal Potential
Transmembrane225 – 24521 Potential
Topological domain246 – 28742Cytoplasmic Potential
Transmembrane288 – 30821 Potential
Topological domain309 – 32921Lumenal Potential
Transmembrane330 – 35021 Potential
Topological domain351 – 3577Cytoplasmic Potential
Transmembrane358 – 37821 Potential
Topological domain379 – 3846Lumenal Potential
Transmembrane385 – 40521 Potential
Topological domain406 – 42318Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
Q9EQY6-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 7FC172B5DF98992D

FASTA42349,594
        10         20         30         40         50         60 
MSYTKHWGEW FLNLRVPPAG VFGVAFLARV ALVFYGVFQD RTLLVRYTDI DYHVFTDAAR 

        70         80         90        100        110        120 
FVTEGRSPYL RATYRYTPLL SWLLTPNVYL SELFGKFLFI SCDLLTAFLL YRLLLLKGLG 

       130        140        150        160        170        180 
RRQACGYCVF WLLNPLPMAV SSRGNADSIV ASLVLTTLYL IEKRLIACAA VFYGFAVHMK 

       190        200        210        220        230        240 
MYPVTYILPI ALHLRPERDS DEGLRLARYS FQARLYDFLK RLCSWAVLLF VAIAGLTFLA 

       250        260        270        280        290        300 
LSFGFYYKYG WEFLEHTYLY HLTRRDIRHN FSPYFYMLYL TAESKWSFTL GIAAFLPQFI 

       310        320        330        340        350        360 
LLSAASFAYY RDLVFCCFLH TSIFVTFNKV CTSQYFLWYL CLLPLVMPLV RMPWKRAVVL 

       370        380        390        400        410        420 
LMLWFIGQAL WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN CSILIQIISH YKEDRLTERI 


KYD 

« Hide

References

[1]"PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER."
Maeda Y., Watanabe R., Harris C.L., Hong Y., Ohishi K., Kinoshita K., Kinoshita T.
EMBO J. 20:250-261(2001) [PubMed: 11226175] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

AB028126 mRNA. Translation: BAB18566.1.
IPIIPI00190580.
RefSeqNP_077058.1.
UniGeneRn.163231

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT50. Glycosyltransferase Family 50.

Genome annotation databases

EnsemblENSRNOG00000007735. Rattus norvegicus. [Contig view]
GeneID79112.
KEGGrno:79112.

Organism-specific databases

RGD71041. Pigm.

Phylogenomic databases

HOVERGENQ9EQY6.
OMAQ9EQY6. NFSPYFY.

Gene expression databases

ArrayExpressQ9EQY6.
GermOnlineENSRNOG00000007735. Rattus norvegicus.

Family and domain databases

InterProIPR007704. Mannosyltransferase_DXD.
[Graphical view]
PANTHERPTHR12886. Mannos_trans_DXD. 1 hit.
PfamPF05007. Mannosyl_trans. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio614510.

Entry information

Entry namePIGM_RAT
AccessionPrimary (citable) accession number: Q9EQY6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents