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Protein

Phosphatidylinositol-glycan biosynthesis class W protein

Gene

Pigw

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Required for the transport of GPI-anchored proteins to the plasma membrane. 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.By similarity

Pathwayi: glycosylphosphatidylinositol-anchor biosynthesis

This protein is involved in the pathway glycosylphosphatidylinositol-anchor biosynthesis, which is part of Glycolipid biosynthesis.By similarity
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

ReactomeiR-MMU-162710. Synthesis of glycosylphosphatidylinositol (GPI).
UniPathwayiUPA00196.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol-glycan biosynthesis class W proteinCurated (EC:2.3.-.-By similarity)
Short name:
PIG-WCurated
Gene namesi
Name:PigwImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1917575. Pigw.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121LumenalSequence analysisAdd
BLAST
Transmembranei22 – 4221HelicalSequence analysisAdd
BLAST
Transmembranei61 – 8121HelicalSequence 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
Transmembranei340 – 36021HelicalSequence analysisAdd
BLAST
Transmembranei381 – 40121HelicalSequence analysisAdd
BLAST
Transmembranei448 – 46821HelicalSequence analysisAdd
BLAST
Transmembranei473 – 49321HelicalSequence 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 – 503503Phosphatidylinositol-glycan biosynthesis class W proteinPRO_0000246283Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi13 – 131N-linked (GlcNAc...)Sequence analysis
Modified residuei415 – 4151PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8C398.
PaxDbiQ8C398.
PRIDEiQ8C398.

PTM databases

PhosphoSiteiQ8C398.

Expressioni

Gene expression databases

BgeeiQ8C398.
ExpressionAtlasiQ8C398. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064547.

Structurei

3D structure databases

ProteinModelPortaliQ8C398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PIGW family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0411. Eukaryota.
COG5062. LUCA.
GeneTreeiENSGT00390000013520.
HOGENOMiHOG000204712.
HOVERGENiHBG079452.
InParanoidiQ8C398.
KOiK05283.
OMAiHEDPLGI.
OrthoDBiEOG71K646.
PhylomeDBiQ8C398.
TreeFamiTF314687.

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.

Q8C398-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKQLKEAF VRNLSGTSVL EVTQGLCFPA FCILCRGLWI IFSQHVCSFS
60 70 80 90 100
NTWSTRFLMD FVVLIVPLVI TLTVLSSFIL LENLTVIVWG AWLLYQIYHR
110 120 130 140 150
RTCYAKVPVQ KVFANFLKIS LESEYNPAIT CYRVINSVFT AIAILAVDFP
160 170 180 190 200
LFPRRFAKTE LYGTGAMDFG VGGFIFGAAM VCPEVRRKSI EESRFNYLRK
210 220 230 240 250
SLYSVWPLVF LGMGRLVIIK SIGYQEHSTE YGIHWNFFFT IIVVRLVTSL
260 270 280 290 300
LLIIFPLNKS WIVAVSITVV YQLALDYTPL KRILLYGTDG SGTRVGFLNA
310 320 330 340 350
NREGIISTLG YVTIHMAGVQ TGLYVLKGRA QVRDWIKATC WVFSVAVGFF
360 370 380 390 400
ISLHIVQVNI EAVSRRMANL AFCLWVVASS LMLLSCLLLS GIILSFAQFL
410 420 430 440 450
IKGSLVPCSW KLIQSPTTHK NHSESLILEA EKNQPSLCLI TALNRNQLFF
460 470 480 490 500
FLLSNITTGL INLTMDTLHT GALWTLVVLS IYMFTNCLVI YVLDLQGKTI

KFW
Length:503
Mass (Da):56,841
Last modified:March 1, 2003 - v1
Checksum:i3814E3D18680BACF
GO

Sequence cautioni

The sequence BAC38199.1 differs from that shown. Reason: Frameshift at position 453. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011762 mRNA. Translation: BAB27826.3.
AK081337 mRNA. Translation: BAC38199.1. Frameshift.
AK086537 mRNA. Translation: BAC39687.1.
AL645623 Genomic DNA. Translation: CAI25488.1.
CCDSiCCDS36263.1.
RefSeqiNP_001071104.1. NM_001077636.1.
NP_081664.2. NM_027388.2.
XP_006534222.1. XM_006534159.1.
UniGeneiMm.390414.

Genome annotation databases

EnsembliENSMUST00000067058; ENSMUSP00000064547; ENSMUSG00000045140.
ENSMUST00000108080; ENSMUSP00000103715; ENSMUSG00000045140.
GeneIDi70325.
KEGGimmu:70325.
UCSCiuc007kqy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011762 mRNA. Translation: BAB27826.3.
AK081337 mRNA. Translation: BAC38199.1. Frameshift.
AK086537 mRNA. Translation: BAC39687.1.
AL645623 Genomic DNA. Translation: CAI25488.1.
CCDSiCCDS36263.1.
RefSeqiNP_001071104.1. NM_001077636.1.
NP_081664.2. NM_027388.2.
XP_006534222.1. XM_006534159.1.
UniGeneiMm.390414.

3D structure databases

ProteinModelPortaliQ8C398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064547.

PTM databases

PhosphoSiteiQ8C398.

Proteomic databases

MaxQBiQ8C398.
PaxDbiQ8C398.
PRIDEiQ8C398.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067058; ENSMUSP00000064547; ENSMUSG00000045140.
ENSMUST00000108080; ENSMUSP00000103715; ENSMUSG00000045140.
GeneIDi70325.
KEGGimmu:70325.
UCSCiuc007kqy.1. mouse.

Organism-specific databases

CTDi284098.
MGIiMGI:1917575. Pigw.

Phylogenomic databases

eggNOGiKOG0411. Eukaryota.
COG5062. LUCA.
GeneTreeiENSGT00390000013520.
HOGENOMiHOG000204712.
HOVERGENiHBG079452.
InParanoidiQ8C398.
KOiK05283.
OMAiHEDPLGI.
OrthoDBiEOG71K646.
PhylomeDBiQ8C398.
TreeFamiTF314687.

Enzyme and pathway databases

UniPathwayiUPA00196.
ReactomeiR-MMU-162710. Synthesis of glycosylphosphatidylinositol (GPI).

Miscellaneous databases

PROiQ8C398.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C398.
ExpressionAtlasiQ8C398. baseline and differential.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiPIGW_MOUSE
AccessioniPrimary (citable) accession number: Q8C398
Secondary accession number(s): Q8C4S0, Q9CSX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 94 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.