GPI ethanolamine phosphate transferase 1

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O95427 (PIGN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
GPI ethanolamine phosphate transferase 1
EC=2.-.-.-

Alternative name(s):
MCD4 homolog
Phosphatidylinositol-glycan biosynthesis class N protein
Short name=PIG-N

Gene names

Name:	PIGN
Synonyms:	MCD4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	931 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor By similarity. May act as suppressor of replication stress and chromosome missegregation. Ref.4
Pathway	Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Involvement in disease	Multiple congenital anomalies-hypotonia-seizures syndrome 1 (MCAHS1) [MIM:614080]: An autosomal recessive disorder characterized by neonatal hypotonia, lack of psychomotor development, seizures, dysmorphic features, and variable congenital anomalies involving the cardiac, urinary, and gastrointestinal systems. Most affected individuals die before 3 years of age. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5
Sequence similarities	Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Epilepsy
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	C-terminal protein lipidation Traceable author statement. Source: Reactome preassembly of GPI anchor in ER membrane Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 931

931

GPI ethanolamine phosphate transferase 1

PRO_0000246198

Regions

Topological domain

Cytoplasmic Potential

Transmembrane

2 – 24

Helical; Potential

Topological domain

25 – 442

418

Lumenal Potential

Transmembrane

443 – 463

Helical; Potential

Topological domain

464 – 482

Cytoplasmic Potential

Transmembrane

483 – 503

Helical; Potential

Topological domain

504 – 508

Lumenal Potential

Transmembrane

509 – 529

Helical; Potential

Topological domain

530 – 543

Cytoplasmic Potential

Transmembrane

544 – 564

Helical; Potential

Topological domain

565

Lumenal Potential

Transmembrane

566 – 586

Helical; Potential

Topological domain

587 – 591

Cytoplasmic Potential

Transmembrane

592 – 612

Helical; Potential

Topological domain

613 – 618

Lumenal Potential

Transmembrane

619 – 639

Helical; Potential

Topological domain

640 – 649

Cytoplasmic Potential

Transmembrane

650 – 670

Helical; Potential

Topological domain

671 – 685

Lumenal Potential

Transmembrane

686 – 706

Helical; Potential

Topological domain

707 – 723

Cytoplasmic Potential

Transmembrane

724 – 744

Helical; Potential

Topological domain

745 – 786

Lumenal Potential

Transmembrane

787 – 807

Helical; Potential

Topological domain

808 – 824

Cytoplasmic Potential

Transmembrane

825 – 845

Helical; Potential

Topological domain

846 – 858

Lumenal Potential

Transmembrane

859 – 879

Helical; Potential

Topological domain

880 – 894

Cytoplasmic Potential

Transmembrane

895 – 915

Helical; Potential

Topological domain

916 – 931

Lumenal Potential

Amino acid modifications

Glycosylation

128

N-linked (GlcNAc...) Potential

Glycosylation

192

N-linked (GlcNAc...) Potential

Glycosylation

350

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

162

K → E.
Corresponds to variant rs17069506 [ dbSNP | Ensembl ].

VAR_053573

Natural variant

229

H → D. Ref.2
Corresponds to variant rs9320001 [ dbSNP | Ensembl ].

VAR_053574

Natural variant

469

L → F.
Corresponds to variant rs3862712 [ dbSNP | Ensembl ].

VAR_053575

Natural variant

470

I → L.
Corresponds to variant rs3862712 [ dbSNP | Ensembl ].

VAR_053576

Natural variant

709

R → Q in MCAHS1. Ref.5

VAR_066402

Natural variant

904

F → C.
Corresponds to variant rs34231046 [ dbSNP | Ensembl ].

VAR_053577

Natural variant

904

F → L.
Corresponds to variant rs34231046 [ dbSNP | Ensembl ].

VAR_053578

Sequences

Sequence

Length

Mass (Da)

Tools

O95427 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: D67B376EF7864C55
Show »

FASTA

931

105,810

        10         20         30         40         50         60 
MLLFFTLGLL IHFVFFASIF DIYFTSPLVH GMTPQFTPLP PPARRLVLFV ADGLRADALY 

        70         80         90        100        110        120 
ELDENGNSRA PFIRNIIMHE GSWGISHTRV PTESRPGHVA LIAGFYEDVS AVAKGWKENP 

       130        140        150        160        170        180 
VEFDSLFNES KYTWSWGSPD ILPMFAKGAS GDHVYTYSYD AKREDFGAQD ATKLDTWVFD 

       190        200        210        220        230        240 
NVKDFFHHAR NNQSLFSKIN EEKIVFFLHL LGIDTNGHAH RPSSRDYKHN IKKVDDGVKE 

       250        260        270        280        290        300 
IVSMFNHFYG NDGKTTFIFT SDHGMTDWGS HGAGHPSETL TPLVTWGAGI KYPQRVSAQQ 

       310        320        330        340        350        360 
FDDAFLKEWR LENWKRLDVN QADIAPLMTS LIGVPFPLNS VGILPVDYLN NTDLFKAESM 

       370        380        390        400        410        420 
FTNAVQILEQ FKVKMTQKKE VTLPFLFTPF KLLSDSKQFN ILRKARSYIK HRKFDEVVSL 

       430        440        450        460        470        480 
CKELIHLALK GLSYYHTYDR FFLGVNVVIG FVGWISYASL LIIKSHSNLI KGVSKEVKKP 

       490        500        510        520        530        540 
SHLLPCSFVA IGILVAFFLL IQACPWTYYV YGLLPLPIWY AVLREFQVIQ DLVVSVLTYP 

       550        560        570        580        590        600 
LSHFVGYLLA FTLGIEVLVL SFFYRYMLTA GLTAFAAWPF LTRLWTRAKM TSLSWTFFSL 

       610        620        630        640        650        660 
LLAVFPLMPV VGRKPDISLV MGAGLLVLLL SLCVVTSLMK RKDSFIKEEL LVHLLQVLST 

       670        680        690        700        710        720 
VLSMYVVYST QSSLLRKQGL PLMNQIISWA TLASSLVVPL LSSPVLFQRL FSILLSLMST 

       730        740        750        760        770        780 
YLLLSTGYEA LFPLVLSCLM FVWINIEQET LQQSGVCCKQ KLTSIQFSYN TDITQFRQLY 

       790        800        810        820        830        840 
LDDIRRAFFL VFFLVTAFFG TGNIASINSF DLASVYCFLT VFSPFMMGAL MMWKILIPFV 

       850        860        870        880        890        900 
LVMCAFEAVQ LTTQLSSKSL FLIVLVISDI MALHFFFLVK DYGSWLDIGT SISHYVIVMS 

       910        920        930 
MTIFLVFLNG LAQLLTTKKL RLCGKPKSHF M

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast." Gaynor E.C., Mondesert G., Grimme S.J., Reed S.I., Orlean P., Emr S.D. Mol. Biol. Cell 10:627-648(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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], VARIANT ASP-229. Tissue: Testis.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-931. Tissue: Testis.
[4]	"Replication stress links structural and numerical cancer chromosomal instability." Burrell R.A., McClelland S.E., Endesfelder D., Groth P., Weller M.C., Shaikh N., Domingo E., Kanu N., Dewhurst S.M., Gronroos E., Chew S.K., Rowan A.J., Schenk A., Sheffer M., Howell M., Kschischo M., Behrens A., Helleday T. , Bartek J., Tomlinson I.P., Swanton C. Nature 494:492-496(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Multiple congenital anomalies-hypotonia-seizures syndrome is caused by a mutation in PIGN." Maydan G., Noyman I., Har-Zahav A., Neriah Z.B., Pasmanik-Chor M., Yeheskel A., Albin-Kaplanski A., Maya I., Magal N., Birk E., Simon A.J., Halevy A., Rechavi G., Shohat M., Straussberg R., Basel-Vanagaite L. J. Med. Genet. 48:383-389(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MCAHS1 GLN-709.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF109219 mRNA. Translation: AAD11432.1. BC028363 mRNA. Translation: AAH28363.1. AL137607 mRNA. Translation: CAB70839.1.
IPI	IPI00017598.
PIR	T46311.
RefSeq	NP_036459.1. NM_012327.5. NP_789744.1. NM_176787.4. XP_005266732.1. XM_005266675.1.
UniGene	Hs.157031.
3D structure databases
ProteinModelPortal	O95427.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95427. 2 interactions.
STRING	9606.ENSP00000350263.
PTM databases
PhosphoSite	O95427.
Proteomic databases
PaxDb	O95427.
PRIDE	O95427.
Protocols and materials databases
DNASU	23556.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000357637; ENSP00000350263; ENSG00000197563. ENST00000400334; ENSP00000383188; ENSG00000197563.
GeneID	23556.
KEGG	hsa:23556.
UCSC	uc021ulb.1. human.
Organism-specific databases
CTD	23556.
GeneCards	GC18M059684.
HGNC	HGNC:8967. PIGN.
HPA	HPA039922. HPA040374.
MIM	606097. gene. 614080. phenotype.
neXtProt	NX_O95427.
Orphanet	280633. Multiple congenital anomalies - hypotonia - seizures syndrome.
PharmGKB	PA33298.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1524.
HOGENOM	HOG000170818.
HOVERGEN	HBG082138.
InParanoid	O95427.
KO	K05285.
OMA	VLVMCAF.
OrthoDB	EOG7F7W83.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00196.
Gene expression databases
ArrayExpress	O95427.
Bgee	O95427.
CleanEx	HS_PIGN.
Genevestigator	O95427.
Family and domain databases
Gene3D	3.40.720.10. 1 hit.
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR007070. GPI_EtnP_transferase_1. IPR017852. GPI_EtnP_transferase_1_C. IPR002591. Phosphodiest/P_Trfase. [Graphical view]
PANTHER	PTHR12250. PTHR12250. 1 hit.
Pfam	PF01663. Phosphodiest. 1 hit. PF04987. PigN. 1 hit. [Graphical view]
SUPFAM	SSF53649. SSF53649. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PIGN. human.
GenomeRNAi	23556.
NextBio	46124.
PRO	O95427.
SOURCE	Search...

Entry information

Entry name

PIGN_HUMAN

Accession

Primary (citable) accession number: O95427
Secondary accession number(s): Q7L8F8, Q8TC01, Q9NT05

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	May 1, 1999
Last modified:	November 13, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 18

Human chromosome 18: 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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents