PIGW_RAT
ID PIGW_RAT Reviewed; 502 AA.
AC Q7TSN4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Phosphatidylinositol-glycan biosynthesis class W protein {ECO:0000305};
DE Short=PIG-W {ECO:0000303|PubMed:14517336};
DE EC=2.3.-.- {ECO:0000269|PubMed:14517336};
GN Name=Pigw {ECO:0000305};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=14517336; DOI=10.1091/mbc.e03-03-0193;
RA Murakami Y., Siripanyapinyo U., Hong Y., Kang J.Y., Ishihara S.,
RA Nakakuma H., Maeda Y., Kinoshita T.;
RT "PIG-W is critical for inositol acylation but not for flipping of
RT glycosylphosphatidylinositol-anchor.";
RL Mol. Biol. Cell 14:4285-4295(2003).
CC -!- FUNCTION: Required for the transport of GPI-anchored proteins to the
CC plasma membrane (By similarity). Probable acetyltransferase, which
CC acetylates the inositol ring of phosphatidylinositol during
CC biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis
CC is not essential for the subsequent mannosylation and is usually
CC removed soon after the attachment of GPIs to proteins
CC (PubMed:14517336). {ECO:0000250|UniProtKB:Q7Z7B1,
CC ECO:0000269|PubMed:14517336}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000269|PubMed:14517336}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14517336}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14517336}.
CC -!- SIMILARITY: Belongs to the PIGW family. {ECO:0000305}.
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DR EMBL; AB097817; BAC77020.1; -; Genomic_DNA.
DR RefSeq; NP_919443.1; NM_194461.1.
DR AlphaFoldDB; Q7TSN4; -.
DR STRING; 10116.ENSRNOP00000060195; -.
DR GlyGen; Q7TSN4; 1 site.
DR PaxDb; Q7TSN4; -.
DR GeneID; 378774; -.
DR KEGG; rno:378774; -.
DR CTD; 284098; -.
DR RGD; 727962; Pigw.
DR eggNOG; KOG0411; Eukaryota.
DR InParanoid; Q7TSN4; -.
DR OrthoDB; 1202772at2759; -.
DR PhylomeDB; Q7TSN4; -.
DR Reactome; R-RNO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q7TSN4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032216; F:glucosaminyl-phosphatidylinositol O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR InterPro; IPR009447; PIGW/GWT1.
DR PANTHER; PTHR20661; PTHR20661; 1.
DR Pfam; PF06423; GWT1; 1.
DR PIRSF; PIRSF017321; GWT1; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..502
FT /note="Phosphatidylinositol-glycan biosynthesis class W
FT protein"
FT /id="PRO_0000246284"
FT TOPO_DOM 1..21
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7B1"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 502 AA; 56443 MW; 0CAC8FB68B33714E CRC64;
MSQKQLKEAF VSNLSGTSVL EVTQGLCFPA FCILCRGLLI IFSQHLCSFL HTWTTQFFMD
FVVLIVPLVI TLTVLSSFIL LENLTVILCG AWLLYQIYHR RTCYAKVPVQ KVFASFLKIS
LESEYNPAIT CYRVINSVFT AIAILAVDFP LFPRRFAKTE LYGTGAMDFG VGGFIFGAAM
VCPEVRRKYT EGSRFNHLRK SLYSVWPLVF LGMGRLVIIK SIGYQEHSTE YGVHWNFFFT
IIVVKLITSL LLIIFPLNKS WIVAISITVL YQLALDFTPL KGIILYGTDG RGTRVGLLNA
NREGIISTLG YVAIYMAGVQ TGFYVFKRRA QVRDWIKATC WVFSVAVGFF ISLNIVQVNV
EAVSRRMANL AFCLWVVASS LMLLSCLLLS GIVLSFAKFL IKGALVPCSW KLIQSATTNR
QSESLIVEAE KNKPSFCLIT ALNRNQLFFF LLSNVATGLI NLTVDTLHTG AFWTLAVLSI
YMFANCLVIY VLDLQGKTIK FW
