PIGL_MOUSE
ID PIGL_MOUSE Reviewed; 252 AA.
AC Q5SX19;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase;
DE EC=3.5.1.89;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class L protein;
DE Short=PIG-L;
GN Name=Pigl; Synonyms=Gm737;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Involved in the second step of GPI biosynthesis. De-N-
CC acetylation of N-acetylglucosaminyl-phosphatidylinositol (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-
CC inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-
CC glycero-3-phospho)-1D-myo-inositol; Xref=Rhea:RHEA:11660,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:57265,
CC ChEBI:CHEBI:57997; EC=3.5.1.89;
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
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DR EMBL; AK158149; BAE34385.1; -; mRNA.
DR EMBL; AL596181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX470084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24824.1; -.
DR RefSeq; NP_001034625.1; NM_001039536.2.
DR AlphaFoldDB; Q5SX19; -.
DR SMR; Q5SX19; -.
DR STRING; 10090.ENSMUSP00000014389; -.
DR PhosphoSitePlus; Q5SX19; -.
DR EPD; Q5SX19; -.
DR MaxQB; Q5SX19; -.
DR PaxDb; Q5SX19; -.
DR PRIDE; Q5SX19; -.
DR ProteomicsDB; 288208; -.
DR Antibodypedia; 2335; 120 antibodies from 19 providers.
DR DNASU; 327942; -.
DR Ensembl; ENSMUST00000014389; ENSMUSP00000014389; ENSMUSG00000014245.
DR GeneID; 327942; -.
DR KEGG; mmu:327942; -.
DR UCSC; uc007jje.1; mouse.
DR CTD; 9487; -.
DR MGI; MGI:2681271; Pigl.
DR VEuPathDB; HostDB:ENSMUSG00000014245; -.
DR eggNOG; KOG3332; Eukaryota.
DR GeneTree; ENSGT00390000018434; -.
DR HOGENOM; CLU_034979_1_0_1; -.
DR InParanoid; Q5SX19; -.
DR OMA; RWGWITI; -.
DR OrthoDB; 1454301at2759; -.
DR PhylomeDB; Q5SX19; -.
DR TreeFam; TF315150; -.
DR Reactome; R-MMU-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 327942; 13 hits in 76 CRISPR screens.
DR ChiTaRS; Pigl; mouse.
DR PRO; PR:Q5SX19; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SX19; protein.
DR Bgee; ENSMUSG00000014245; Expressed in otolith organ and 217 other tissues.
DR Genevisible; Q5SX19; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
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:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0000225; F:N-acetylglucosaminylphosphatidylinositol deacetylase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:MGI.
DR Gene3D; 3.40.50.10320; -; 1.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR039516; GPI12.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR PANTHER; PTHR12993; PTHR12993; 1.
DR PANTHER; PTHR12993:SF11; PTHR12993:SF11; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; SSF102588; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; GPI-anchor biosynthesis; Hydrolase;
KW Lipid metabolism; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..252
FT /note="N-acetylglucosaminyl-phosphatidylinositol de-N-
FT acetylase"
FT /id="PRO_0000307824"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 252 AA; 28183 MW; 5C243350751F3A6F CRC64;
MELVGFLCVA VAVLTWGFLR VWNSAERMRS PEQAGLPGAG SRALVVIAHP DDEAMFFAPT
MLGLARLEQQ VSLLCFSSGN YYNQGEIRKK ELLQSCAVLG IPPSRVMIID KRDFPDDPEV
QWDTELVAST LLQHIHANGT DLVVTFDAEG VSGHSNHIAL YKAVRALHSG GKLPKGCSVL
TLQSVNALRK YAFLLDLPWT LLSPQDVLFV LTSKEVAQAK KAMSCHRSQL LWFRYLYVLF
SRYMRINSLR FL
