GPAA1

Last updated
GPAA1
Identifiers
Aliases GPAA1 , GAA1, hGAA1, glycosylphosphatidylinositol anchor attachment 1, GPIBD15
External IDs OMIM: 603048 MGI: 1202392 HomoloGene: 37852 GeneCards: GPAA1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003801

NM_010331

RefSeq (protein)

NP_003792

NP_034461

Location (UCSC) Chr 8: 144.08 – 144.09 Mb Chr 15: 76.22 – 76.22 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Glycosylphosphatidylinositol anchor attachment 1 protein is a protein that in humans is encoded by the GPAA1 gene. [5] [6]

Contents

Posttranslational glycosylphosphatidylinositol (GPI) anchor attachment serves as a general mechanism for linking proteins to the cell surface membrane. The protein encoded by this gene presumably functions in GPI anchoring at the GPI transfer step. The mRNA transcript is ubiquitously expressed in both fetal and adult tissues. The anchor attachment protein 1 contains an N-terminal signal sequence, 1 cAMP- and cGMP-dependent protein kinase phosphorylation site, 1 leucine zipper pattern, 2 potential N-glycosylation sites, and 8 putative transmembrane domains. [6]

Interactions

GPAA1 has been shown to interact with PIGT [7] [8] and PIGK. [8] [9]

Related Research Articles

Lipid-anchored protein

Lipid-anchored proteins are proteins located on the surface of the cell membrane that are covalently attached to lipids embedded within the cell membrane. These proteins insert and assume a place in the bilayer structure of the membrane alongside the similar fatty acid tails. The lipid-anchored protein can be located on either side of the cell membrane. Thus, the lipid serves to anchor the protein to the cell membrane. They are a type of proteolipids.

In enzymology, a N-acetylglucosaminylphosphatidylinositol deacetylase (EC 3.5.1.89) is an enzyme that catalyzes the chemical reaction

In enzymology, a phosphatidylinositol N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction

PIGA Protein-coding gene in the species Homo sapiens

Phosphatidylinositol N-acetylglucosaminyltransferase subunit A is the catalytic subunit of the phosphatidylinositol N-acetylglucosaminyltransferase enzyme, which in humans is encoded by the PIGA gene.

PIGT

GPI transamidase component PIG-T is an enzyme that in humans is encoded by the PIGT gene.

PIGK Protein-coding gene in the species Homo sapiens

GPI-anchor transamidase is an enzyme that in humans is encoded by the PIGK gene.

PIGQ

Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q is an enzyme that in humans is encoded by the PIGQ gene.

DPM1

Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1 gene.

PIGC Enzyme

Phosphatidylinositol N-acetylglucosaminyltransferase subunit C is an enzyme that in humans is encoded by the PIGC gene.

PIGF

Phosphatidylinositol-glycan biosynthesis class F protein is a protein that in humans is encoded by the PIGF gene.

PIGS (gene)

GPI transamidase component PIG-S is an enzyme that in humans is encoded by the PIGS gene. This gene encodes a protein that is involved in GPI-anchor biosynthesis.

PIGU

Phosphatidylinositol glycan anchor biosynthesis class U protein is a protein that in humans is encoded by the PIGU gene.

PIGB

GPI mannosyltransferase 3 is an enzyme that in humans is encoded by the PIGB gene.

PIGH

Phosphatidylinositol N-acetylglucosaminyltransferase subunit H is an enzyme that in humans is encoded by the PIGH gene. The PIGH gene is located on the reverse strand of chromosome 14 in humans, and is neighbored by TMEM229B.

PIGV Protein-coding gene in the species Homo sapiens

GPI mannosyltransferase 2 is an enzyme that in humans is encoded by the PIGV gene.

DPM3 Protein-coding gene in the species Homo sapiens

dolichyl-phosphate mannosyltransferase polypeptide 3, also known as DPM3, is a human gene.

DPM2 Protein-coding gene in the species Homo sapiens

Dolichol phosphate-mannose biosynthesis regulatory protein is a protein that in humans is encoded by the DPM2 gene.

Glypiation is the addition by covalent bonding of a glycosylphosphatidylinositol (GPI) anchor and is a common post-translational modification that localizes proteins to cell membranes. This special kind of glycosylation is widely detected on surface glycoproteins in eukaryotes and some Archaea.

PIGN (gene)

Phosphatidylinositol glycan anchor biosynthesis, class N is a protein that in humans is encoded by the PIGN gene.

PGAP1

Post-GPI attachment to proteins 1 is a protein that in humans is encoded by the PGAP1 gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000197858 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022561 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Hiroi Y, Komuro I, Matsushita I, Aburatani H, Hosoda T, Nakahori Y, et al. (December 1998). "Assignment of the human GPAA1 gene, which encodes a product required for the attachment of glycosylphosphatidylinositols to proteins, at 8q24". Genomics. 54 (2): 354–5. doi:10.1006/geno.1998.5490. PMID   9828142.
  6. 1 2 "Entrez Gene: GPAA1 glycosylphosphatidylinositol anchor attachment protein 1 homolog (yeast)".
  7. Ohishi K, Inoue N, Kinoshita T (August 2001). "PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8". The EMBO Journal. 20 (15): 4088–98. doi:10.1093/emboj/20.15.4088. PMC   149153 . PMID   11483512.
  8. 1 2 Vainauskas S, Maeda Y, Kurniawan H, Kinoshita T, Menon AK (August 2002). "Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex". The Journal of Biological Chemistry. 277 (34): 30535–42. doi: 10.1074/jbc.M205402200 . PMID   12052837.
  9. Ohishi K, Inoue N, Maeda Y, Takeda J, Riezman H, Kinoshita T (May 2000). "Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins". Molecular Biology of the Cell. 11 (5): 1523–33. doi:10.1091/mbc.11.5.1523. PMC   14864 . PMID   10793132.

Further reading