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Protein

Phosphatidylinositol-glycan biosynthesis class W protein

Gene

Pigw

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Required for the transport of GPI-anchored proteins to the plasma membrane (By similarity). Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins (PubMed:14517336).By similarity1 Publication

Pathwayi: glycosylphosphatidylinositol-anchor biosynthesis

This protein is involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis, which is part of Glycolipid biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis and in Glycolipid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

GPI-anchor biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00196.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol-glycan biosynthesis class W proteinCurated (EC:2.3.-.-1 Publication)
Short name:
PIG-W1 Publication
Gene namesi
Name:PigwCurated
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi727962. Pigw.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121LumenalSequence analysisAdd
BLAST
Transmembranei22 – 4221HelicalSequence analysisAdd
BLAST
Transmembranei61 – 7414HelicalSequence analysisAdd
BLAST
Transmembranei75 – 9723HelicalSequence analysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence analysisAdd
BLAST
Transmembranei161 – 18121HelicalSequence analysisAdd
BLAST
Transmembranei202 – 22221HelicalSequence analysisAdd
BLAST
Transmembranei237 – 25721HelicalSequence analysisAdd
BLAST
Transmembranei260 – 28021HelicalSequence analysisAdd
BLAST
Transmembranei305 – 32521HelicalSequence analysisAdd
BLAST
Transmembranei338 – 35821HelicalSequence analysisAdd
BLAST
Transmembranei374 – 39421HelicalSequence analysisAdd
BLAST
Transmembranei447 – 46721HelicalSequence analysisAdd
BLAST
Transmembranei472 – 49221HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 502502Phosphatidylinositol-glycan biosynthesis class W proteinPRO_0000246284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi13 – 131N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ7TSN4.
PRIDEiQ7TSN4.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060195.

Family & Domainsi

Sequence similaritiesi

Belongs to the PIGW family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0411. Eukaryota.
COG5062. LUCA.
HOGENOMiHOG000204712.
HOVERGENiHBG079452.
InParanoidiQ7TSN4.
KOiK05283.
PhylomeDBiQ7TSN4.

Family and domain databases

InterProiIPR009447. GWT1.
[Graphical view]
PANTHERiPTHR20661. PTHR20661. 1 hit.
PfamiPF06423. GWT1. 1 hit.
[Graphical view]
PIRSFiPIRSF017321. GWT1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7TSN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKQLKEAF VSNLSGTSVL EVTQGLCFPA FCILCRGLLI IFSQHLCSFL
60 70 80 90 100
HTWTTQFFMD FVVLIVPLVI TLTVLSSFIL LENLTVILCG AWLLYQIYHR
110 120 130 140 150
RTCYAKVPVQ KVFASFLKIS LESEYNPAIT CYRVINSVFT AIAILAVDFP
160 170 180 190 200
LFPRRFAKTE LYGTGAMDFG VGGFIFGAAM VCPEVRRKYT EGSRFNHLRK
210 220 230 240 250
SLYSVWPLVF LGMGRLVIIK SIGYQEHSTE YGVHWNFFFT IIVVKLITSL
260 270 280 290 300
LLIIFPLNKS WIVAISITVL YQLALDFTPL KGIILYGTDG RGTRVGLLNA
310 320 330 340 350
NREGIISTLG YVAIYMAGVQ TGFYVFKRRA QVRDWIKATC WVFSVAVGFF
360 370 380 390 400
ISLNIVQVNV EAVSRRMANL AFCLWVVASS LMLLSCLLLS GIVLSFAKFL
410 420 430 440 450
IKGALVPCSW KLIQSATTNR QSESLIVEAE KNKPSFCLIT ALNRNQLFFF
460 470 480 490 500
LLSNVATGLI NLTVDTLHTG AFWTLAVLSI YMFANCLVIY VLDLQGKTIK

FW
Length:502
Mass (Da):56,443
Last modified:October 1, 2003 - v1
Checksum:i0CAC8FB68B33714E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB097817 Genomic DNA. Translation: BAC77020.1.
RefSeqiNP_919443.1. NM_194461.1.
UniGeneiRn.59828.

Genome annotation databases

GeneIDi378774.
KEGGirno:378774.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB097817 Genomic DNA. Translation: BAC77020.1.
RefSeqiNP_919443.1. NM_194461.1.
UniGeneiRn.59828.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060195.

Proteomic databases

PaxDbiQ7TSN4.
PRIDEiQ7TSN4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi378774.
KEGGirno:378774.

Organism-specific databases

CTDi284098.
RGDi727962. Pigw.

Phylogenomic databases

eggNOGiKOG0411. Eukaryota.
COG5062. LUCA.
HOGENOMiHOG000204712.
HOVERGENiHBG079452.
InParanoidiQ7TSN4.
KOiK05283.
PhylomeDBiQ7TSN4.

Enzyme and pathway databases

UniPathwayiUPA00196.

Miscellaneous databases

PROiQ7TSN4.

Family and domain databases

InterProiIPR009447. GWT1.
[Graphical view]
PANTHERiPTHR20661. PTHR20661. 1 hit.
PfamiPF06423. GWT1. 1 hit.
[Graphical view]
PIRSFiPIRSF017321. GWT1. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "PIG-W is critical for inositol acylation but not for flipping of glycosylphosphatidylinositol-anchor."
    Murakami Y., Siripanyapinyo U., Hong Y., Kang J.Y., Ishihara S., Nakakuma H., Maeda Y., Kinoshita T.
    Mol. Biol. Cell 14:4285-4295(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, CATALYTIC ACTIVITY, PATHWAY.

Entry informationi

Entry nameiPIGW_RAT
AccessioniPrimary (citable) accession number: Q7TSN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 1, 2003
Last modified: June 8, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.