Q9Y2B2 (PIGL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
EC=3.5.1.89

Alternative name(s):
Phosphatidylinositol-glycan biosynthesis class L protein
Short name=PIG-L

Gene names

Name:

PIGL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Catalytic activity	6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate.
Pathway	Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity.
Involvement in disease	Coloboma, congenital heart disease, ichthyosiform dermatosis, mental retardation and ear anomalies syndrome (CHIME) [MIM:280000]: An extremely rare autosomal recessive multisystem disorder clinically characterized by colobomas, congenital heart defects, migratory ichthyosiform dermatosis, mental retardation, and ear anomalies including conductive hearing loss. Other clinical features include distinctive facial features, abnormal growth, genitourinary abnormalities, seizures, and feeding difficulties. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5
Sequence similarities	Belongs to the PIGL family.

Ontologies

Keywords
Biological process	GPI-anchor biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Disease	Deafness Disease mutation Ichthyosis Mental retardation
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase
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	N-acetylglucosaminylphosphatidylinositol deacetylase activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 252	252	N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase		PRO_0000207167
Regions
	Transmembrane	2 – 22	21	Helical; Potential
	Topological domain	23 – 252	230	Cytoplasmic Potential
Natural variations
	Natural variant	167	1	L → P in CHIME. Ref.5 Corresponds to variant rs145303331 [ dbSNP | Ensembl ].		VAR_068221

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2B2 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 420454DCA51704FB	FASTA	252	28,531
	10 20 30 40 50 60 MEAMWLLCVA LAVLAWGFLW VWDSSERMKS REQGGRLGAE SRTLLVIAHP DDEAMFFAPT 70 80 90 100 110 120 VLGLARLRHW VYLLCFSAGN YYNQGETRKK ELLQSCDVLG IPLSSVMIID NRDFPDDPGM 130 140 150 160 170 180 QWDTEHVARV LLQHIEVNGI NLVVTFDAGG VSGHSNHIAL YAAVRALHSE GKLPKGCSVL 190 200 210 220 230 240 TLQSVNVLRK YISLLDLPLS LLHTQDVLFV LNSKEVAQAK KAMSCHRSQL LWFRRLYIIF 250 SRYMRINSLS FL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis." Watanabe R., Ohishi K., Maeda Y., Nakamura N., Kinoshita T. Biochem. J. 339:185-192(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Mutations in the glycosylphosphatidylinositol gene PIGL cause CHIME syndrome." Ng B.G., Hackmann K., Jones M.A., Eroshkin A.M., He P., Wiliams R., Bhide S., Cantagrel V., Gleeson J.G., Paller A.S., Schnur R.E., Tinschert S., Zunich J., Hegde M.R., Freeze H.H. Am. J. Hum. Genet. 90:685-688(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CHIME PRO-167.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB017165 mRNA. Translation: BAA74775.1. AK292932 mRNA. Translation: BAF85621.1. CH471222 Genomic DNA. Translation: EAX04498.1. BC068197 mRNA. Translation: AAH68197.1.
IPI	IPI00032002.
RefSeq	NP_004269.1. NM_004278.3.
UniGene	Hs.499793. Hs.625050.
3D structure databases
ProteinModelPortal	Q9Y2B2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000225609.
Polymorphism databases
DMDM	14916637.
Proteomic databases
PaxDb	Q9Y2B2.
PRIDE	Q9Y2B2.
Protocols and materials databases
DNASU	9487.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000225609; ENSP00000225609; ENSG00000108474.
GeneID	9487.
KEGG	hsa:9487.
UCSC	uc002gpv.3. human.
Organism-specific databases
CTD	9487.
GeneCards	GC17P016120.
HGNC	HGNC:8966. PIGL.
HPA	HPA012739.
MIM	280000. phenotype. 605947. gene.
neXtProt	NX_Q9Y2B2.
Orphanet	3474. Zunich-Kaye syndrome.
PharmGKB	PA33297.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2120.
HOGENOM	HOG000176611.
HOVERGEN	HBG019149.
InParanoid	Q9Y2B2.
KO	K03434.
OMA	WFRRLYI.
OrthoDB	EOG45490F.
PhylomeDB	Q9Y2B2.
Enzyme and pathway databases
BRENDA	3.5.1.89. 2681.
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00196.
Gene expression databases
ArrayExpress	Q9Y2B2.
Bgee	Q9Y2B2.
CleanEx	HS_PIGL.
Genevestigator	Q9Y2B2.
GermOnline	ENSG00000108474. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.10320. 1 hit.
InterPro	IPR003737. GlcNAc_PIno_de-acetylase. IPR024078. LmbE-like_dom. [Graphical view]
PANTHER	PTHR12993. PTHR12993. 1 hit.
Pfam	PF02585. PIG-L. 1 hit. [Graphical view]
SUPFAM	SSF102588. SSF102588. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PIGL. human.
GenomeRNAi	9487.
NextBio	35548.
SOURCE	Search...

Entry information

Entry name

PIGL_HUMAN

Accession

Primary (citable) accession number: Q9Y2B2
Secondary accession number(s): A8KA67

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 100 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.