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Reviewed, UniProtKB/Swiss-Prot Q9H3S5 (PIGM_HUMAN)

Last modified November 25, 2008. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

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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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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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.

Pathway

Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Involvement in disease

Defects in PIGM are the cause of glycosylphosphatidylinositol deficiency (GPID) [MIM:610293]. GPID is an autosomal recessive trait that results in a propensity to venous thrombosis and seizures. Deficiency is due to a point mutation in the regulatory sequences of PIGM that disrupts binding of the transcription factor SP1 to its cognate promoter motif, leading to a strong reduction of expression.

Sequence similarities

Belongs to the PIGM family.

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Ontologies

Keywords

   Biological processGPI-anchor biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
   Molecular functionGlycosyltransferase
Transferase

Gene Ontology (GO)

   Biological processpreassembly of GPI anchor in ER membrane

Inferred from Experiment. Source: Reactome

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: InterPro

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmannosyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423GPI mannosyltransferase 1
PRO_0000246213

Regions

Topological domain1 – 1717Cytoplasmic Potential
Transmembrane18 – 3821 Potential
Topological domain39 – 7941Lumenal Potential
Transmembrane80 – 10021 Potential
Topological domain101 – 13838Cytoplasmic Potential
Transmembrane139 – 16123 Potential
Topological domain162 – 1698Lumenal Potential
Transmembrane170 – 19021 Potential
Topological domain191 – 22535Cytoplasmic Potential
Transmembrane226 – 24621 Potential
Topological domain247 – 28741Lumenal Potential
Transmembrane288 – 30821 Potential
Topological domain309 – 3146Cytoplasmic Potential
Transmembrane315 – 33723 Potential
Topological domain3381Lumenal Potential
Transmembrane339 – 35012 Potential
Topological domain351 – 3577Cytoplasmic Potential
Transmembrane358 – 37821 Potential
Topological domain379 – 3846Lumenal Potential
Transmembrane385 – 40521 Potential
Topological domain406 – 42318Cytoplasmic Potential

Natural variations

Natural variant3651F → L: dbSNP rs12409352.
VAR_027026

Experimental info

Mutagenesis491D → A: Almost abolishes enzyme activity
Mutagenesis511D → A: Abolishes enzyme activity

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Sequences

Sequence LengthMass (Da)Tools
Q9H3S5-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: E17DCD8252E28EF0

FASTA42349,460
        10         20         30         40         50         60 
MGSTKHWGEW LLNLKVAPAG VFGVAFLARV ALVFYGVFQD RTLHVRYTDI DYQVFTDAAR 

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

       130        140        150        160        170        180 
RRQACGYCVF WLLNPLPMAV SSRGNADSIV ASLVLMVLYL IKKRLVACAA VFYGFAVHMK 

       190        200        210        220        230        240 
IYPVTYILPI TLHLLPDRDN DKSLRQFRYT FQACLYELLK RLCNRAVLLF VAVAGLTFFA 

       250        260        270        280        290        300 
LSFGFYYEYG WEFLEHTYFY HLTRRDIRHN FSPYFYMLYL TAESKWSFSL GIAAFLPQLI 

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

       370        380        390        400        410        420 
LMLWFIGQAM WLAPAYVLEF QGKNTFLFIW LAGLFFLLIN CSILIQIISH YKEEPLTERI 


KYD

« Hide

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References

« Hide 'large scale' 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], FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ASP-49 AND ASP-51.
[2]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Eye.
[5]"Hypomorphic promoter mutation in PIGM causes inherited glycosylphosphatidylinositol deficiency."
Almeida A.M., Murakami Y., Layton D.M., Hillmen P., Sellick G.S., Maeda Y., Richards S., Patterson S., Kotsianidis I., Mollica L., Crawford D.H., Baker A., Ferguson M., Roberts I., Houlston R., Kinoshita T., Karadimitris A.
Nat. Med. 12:846-851(2006) [PubMed: 16767100] [Abstract]
Cited for: INVOLVEMENT IN GLYCOSYLPHOSPHATIDYLINOSITOL DEFICIENCY.

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Cross-references

Sequence databases

AB028127 mRNA. Translation: BAB18567.1.
AK074655 mRNA. Translation: BAC11116.1.
AL513302 Genomic DNA. Translation: CAH71492.1.
BC001803 mRNA. Translation: AAH01803.1.
BC019865 mRNA. Translation: AAH19865.1.
RefSeqNP_660150.1.
UniGeneHs.552810

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSG00000143315. Homo sapiens. [Contig view]
GeneID93183.
KEGGhsa:93183.

Organism-specific databases

HGNCHGNC:18858. PIGM.
MIM610273. gene.
610293. phenotype.
Orphanet83639. Hypercoagulability syndrome, due to glycosylphosphatidylinositol deficiency.
PharmGKBPA38718.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ9H3S5.
HOVERGENQ9H3S5.

Enzyme and pathway databases

ReactomeREACT_1069. Post-translational protein modification.

Gene expression databases

ArrayExpressQ9H3S5.
CleanExHS_PIGM.
GermOnlineENSG00000143315. Homo sapiens.

Family and domain databases

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

Other Resources

NextBio78019.
SOURCESearch...

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Entry information

Entry namePIGM_HUMAN
AccessionPrimary (citable) accession number: Q9H3S5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2001
Last modified: November 25, 2008
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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