PGAP1_MOUSE
ID PGAP1_MOUSE Reviewed; 922 AA.
AC Q3UUQ7; E9QKG7; Q8BQ77;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
DE AltName: Full=Post-GPI attachment to proteins factor 1;
GN Name=Pgap1;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-784 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Spinal ganglion;
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).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-558.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins.
CC GPI inositol deacylation may important for efficient transport of GPI-
CC anchored proteins from the endoplasmic reticulum to the Golgi (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UUQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UUQ7-2; Sequence=VSP_023045, VSP_023046;
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000305}.
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DR EMBL; AK051360; BAC34614.1; -; mRNA.
DR EMBL; AK138171; BAE23568.1; -; mRNA.
DR EMBL; AC121980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48260.1; -. [Q3UUQ7-1]
DR RefSeq; NP_001156786.1; NM_001163314.2. [Q3UUQ7-1]
DR AlphaFoldDB; Q3UUQ7; -.
DR STRING; 10090.ENSMUSP00000095346; -.
DR ChEMBL; CHEMBL3259507; -.
DR ESTHER; mouse-q3uuq7; PGAP1.
DR GlyConnect; 2359; 5 N-Linked glycans (2 sites).
DR GlyGen; Q3UUQ7; 4 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; Q3UUQ7; -.
DR PhosphoSitePlus; Q3UUQ7; -.
DR EPD; Q3UUQ7; -.
DR MaxQB; Q3UUQ7; -.
DR PaxDb; Q3UUQ7; -.
DR PeptideAtlas; Q3UUQ7; -.
DR PRIDE; Q3UUQ7; -.
DR ProteomicsDB; 301796; -. [Q3UUQ7-1]
DR Antibodypedia; 34062; 36 antibodies from 15 providers.
DR Ensembl; ENSMUST00000097739; ENSMUSP00000095346; ENSMUSG00000073678. [Q3UUQ7-1]
DR GeneID; 241062; -.
DR KEGG; mmu:241062; -.
DR UCSC; uc011wky.2; mouse. [Q3UUQ7-1]
DR CTD; 80055; -.
DR MGI; MGI:2443342; Pgap1.
DR VEuPathDB; HostDB:ENSMUSG00000073678; -.
DR eggNOG; KOG3724; Eukaryota.
DR GeneTree; ENSGT00390000016484; -.
DR HOGENOM; CLU_013735_1_0_1; -.
DR InParanoid; Q3UUQ7; -.
DR OMA; YGLYYYY; -.
DR PhylomeDB; Q3UUQ7; -.
DR TreeFam; TF314565; -.
DR Reactome; R-MMU-162791; Attachment of GPI anchor to uPAR.
DR BioGRID-ORCS; 241062; 7 hits in 75 CRISPR screens.
DR PRO; PR:Q3UUQ7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3UUQ7; protein.
DR Bgee; ENSMUSG00000073678; Expressed in epithelium of small intestine and 215 other tissues.
DR Genevisible; Q3UUQ7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0050185; F:phosphatidylinositol deacylase activity; ISS:UniProtKB.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0021871; P:forebrain regionalization; IMP:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:MGI.
DR GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central.
DR GO; GO:0060322; P:head development; IMP:MGI.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012908; PGAP1-like.
DR InterPro; IPR039529; PGAP1/BST1.
DR PANTHER; PTHR15495; PTHR15495; 1.
DR Pfam; PF07819; PGAP1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Membrane; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..922
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277624"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..597
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 619..641
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..668
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..694
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..715
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..733
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 755..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 839..894
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 916..922
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 776..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /evidence="ECO:0000250"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT VAR_SEQ 50..166
FT /note="KIELPKKLTKRYPAYELYLYGEGSYAEEHKILPLTGIPVLFLPGNAGSYKQV
FT RSIGSIALRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKAILKLYKG
FT QEFAPT -> VRPSLTCAPTPPGLLSGSDGTLRLGALLALEVSCFVLGRASSPPRPLVP
FT HPDSGPRLLTAREPALVPLPNPYTSRTLLCLQGDDFSSRPVMGVRQISLFWKEAASCRV
FT AKADLKKRL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023045"
FT VAR_SEQ 167..922
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023046"
FT CONFLICT 223
FT /note="N -> D (in Ref. 1; BAE23568)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="E -> V (in Ref. 1; BAE23568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 922 AA; 104578 MW; E503CA512882F943 CRC64;
MFLHSVNLWN LAFYVFMVFL ATLGLWDVFF GFEENKCSMS YMFEYPEYQK IELPKKLTKR
YPAYELYLYG EGSYAEEHKI LPLTGIPVLF LPGNAGSYKQ VRSIGSIALR KAEDIDFKYH
FDFFSVNFNE ELVALYGGSL QKQTKFVHEC IKAILKLYKG QEFAPTSVAI IGHSMGGLVA
RALLTLKNFK QDLINLLVTQ ATPHVAPVMP LDRFITEFYM NVNNYWILNA RHINLTTLSV
AGGFRDYQVR SGLTFLPKLS HYTSALSVVS SAVPKTWVST DHLSIVWCKQ LQLTTIRAFF
DLIDADTKQI TQKPKKKLSV LNHHFIRHPA KQFEENPSII SDLTGTSMWV PVKVSRWSYV
AYNESDKIYF AFPLANHRKI YTHAYCQSTM LDTNSWIFGC INSTSMCRQG VDLSWKAELL
PTIKSLTLRL QDYPSLSHIV VYVPSVHGSK FVVDCEFFKK EARSMQLPVT HLFSFGLSSR
KVTLNTNGLY YNIELLNFGQ IYQAFKVNVV SKCTGSKEEI TSIYKLHIPW SYEDSLTIAQ
VPSSTDISLK LHVAQPENDS HVALLKMYTS SDCQYEVTIK TSFPQILGQV VRFHGGALPA
YVVSSILLAY GGQLYSLLST GYCLEYSTIL DKEAKPYKVD PFVIMIKFLL GYKWFKELWD
AVLLPELDAI VLTSQSMCFP LVSLILFLFG TCTAYWSGLL SSTSVQLLSS LWLALKRPAE
LPKDIKVMSP DLPVLTVVFL IVSWTTCGAL AILLSYLYYV FKVVHLQASL TTFKNNQPVN
PKHSRRSEKK SNHHKDSAVQ SLRLCANDAE DSLRMHSTVI NLLTWVVLLS MPSLIYWLKN
LRYYFKLSPD PCKPLAFLLI PAIAILGNTH TVSVKSSKLL KTVSQFPLPL AVGVIAFGSS
HLYRVPCFVI IPLVFHALCN FM
