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Q9EQY6 (PIGM_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423GPI mannosyltransferase 1
PRO_0000246217

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q9EQY6 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028126 mRNA. Translation: BAB18566.1.
RefSeqNP_077058.1. NM_024144.1.
UniGeneRn.163231.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000010551.

Protein family/group databases

CAZyGT50. Glycosyltransferase Family 50.

Proteomic databases

PRIDEQ9EQY6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010551; ENSRNOP00000010551; ENSRNOG00000007735.
GeneID79112.
KEGGrno:79112.
UCSCRGD:71041. rat.

Organism-specific databases

CTD93183.
RGD71041. Pigm.

Phylogenomic databases

eggNOGNOG268708.
GeneTreeENSGT00390000017728.
HOGENOMHOG000186884.
HOVERGENHBG082137.
InParanoidQ9EQY6.
KOK05284.
OMAEFLEHTY.
OrthoDBEOG7SBNQM.
PhylomeDBQ9EQY6.
TreeFamTF314752.

Enzyme and pathway databases

UniPathwayUPA00196.

Gene expression databases

GenevestigatorQ9EQY6.

Family and domain databases

InterProIPR007704. Mannosyltransferase_DXD.
[Graphical view]
PANTHERPTHR12886. PTHR12886. 1 hit.
PfamPF05007. Mannosyl_trans. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio614510.
PROQ9EQY6.

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: May 14, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways