PGAP1_RAT
ID PGAP1_RAT Reviewed; 922 AA.
AC Q765A7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
DE AltName: Full=Post-GPI attachment to proteins factor 1;
GN Name=Pgap1;
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, AND
RP MUTAGENESIS OF SER-174.
RX PubMed=14734546; DOI=10.1074/jbc.m313755200;
RA Tanaka S., Maeda Y., Tashima Y., Kinoshita T.;
RT "Inositol deacylation of glycosylphosphatidylinositol-anchored proteins is
RT mediated by mammalian PGAP1 and yeast Bst1p.";
RL J. Biol. Chem. 279:14256-14263(2004).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-558, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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.
CC {ECO:0000269|PubMed:14734546}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14734546}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14734546}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000305}.
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DR EMBL; AB116149; BAD08353.1; -; mRNA.
DR RefSeq; NP_973719.1; NM_201990.1.
DR AlphaFoldDB; Q765A7; -.
DR STRING; 10116.ENSRNOP00000017967; -.
DR ESTHER; ratno-q765a7; PGAP1.
DR GlyGen; Q765A7; 3 sites, 9 N-linked glycans (1 site).
DR iPTMnet; Q765A7; -.
DR SwissPalm; Q765A7; -.
DR PaxDb; Q765A7; -.
DR PRIDE; Q765A7; -.
DR Ensembl; ENSRNOT00000017967; ENSRNOP00000017967; ENSRNOG00000013388.
DR GeneID; 316400; -.
DR KEGG; rno:316400; -.
DR CTD; 80055; -.
DR RGD; 1303213; Pgap1.
DR eggNOG; KOG3724; Eukaryota.
DR GeneTree; ENSGT00390000016484; -.
DR HOGENOM; CLU_013735_1_0_1; -.
DR InParanoid; Q765A7; -.
DR OMA; YGLYYYY; -.
DR OrthoDB; 438490at2759; -.
DR PhylomeDB; Q765A7; -.
DR TreeFam; TF314565; -.
DR Reactome; R-RNO-162791; Attachment of GPI anchor to uPAR.
DR PRO; PR:Q765A7; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000013388; Expressed in duodenum and 19 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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; IMP:UniProtKB.
DR GO; GO:0009948; P:anterior/posterior axis specification; ISO:RGD.
DR GO; GO:0009880; P:embryonic pattern specification; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0021871; P:forebrain regionalization; ISO:RGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:RGD.
DR GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central.
DR GO; GO:0060322; P:head development; ISO:RGD.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
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 Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..922
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277625"
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..816
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 838..853
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 875..894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 916..922
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 776..801
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 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:0007744|PubMed:24090084"
FT MUTAGEN 174
FT /note="S->A: Abolishes the inositol deacylation of GPI-
FT anchor proteins."
FT /evidence="ECO:0000269|PubMed:14734546"
SQ SEQUENCE 922 AA; 104384 MW; B07E02DF99875FD3 CRC64;
MFLHSVNLWN LAFYVFMVFL ATLGLWDVFF GFEENKCSMS YMFEYPEYQK IELPKKLTKR
YPAYELYLYG EGSYAEEHKI LPLTGIPVLF LPGNAGSYKQ VRSIGSIALR KAEDIDFKYH
FDFFSVNFNE ELVALYGGSL QKQTKFVHEC IKAILKLYKG QEFPPTSVAI IGHSMGGLVA
RALLTLKNFK QDLINLLVTQ ATPHVAPVMP LDRFITEFYM TVNNYWILNA RHINLTTLSV
AGGFRDYQVR SGLTFLPTLS HHTSALSVVT SAVPKTWVST DHLSIVWCKQ LQLTTIRAFF
DLIDADTKQI TQKSKKKLSV LNHHFIRHPA KQFEENPSII SDLTGTSMWV PVKVSRWSYV
AYNESDKIYF AFPLANHRKV YTHAYCQSTM LDTNSWIFGC INSTSMCRQG VDLSWKAELL
PTIKSLTLRL QDYPSLSHIV VYVPSVHGSK FVVDCEFFKK EARSIQLPVT HLFSFGLSSR
KAIINTSGRY YNIELLNLGQ IYQAFKVNVV SKCTGGKEEI TSIYKLHIPW SYEDSLTIAQ
VPSSVDISLK LHVAQPENDS HVALLKMYTS SDCQYEVTIK TSFPQILGQV VRFHGGALPA
YVVSSILLAY GGQLYSLLST GFCLEYGTML DKEAKPYKVD PFVIMIKFLL GYKWFKELWD
AVLLPELDAI VLTSQSMCFP LVSLILFLFG TCTAYWSGLL SSASVQLLSS LWLALKRPAE
LPKDVKVMSP DLPVLTVVFL IISWTTCGAL AILLSYLYYV FKVVHLQASL TTFKNNQPVN
PKHSRRSEKK SNHHKDSAIQ NPRLSANDAE DSLRMHSTVI NLLTWVVLLS MPSLIYWSKN
LRYYFKLNPD PCKPLAFLLI PAIAVLGNTH TVSIKSSKLL KTASQFPLPL AVGVIAFGSS
HLYRVPCFVI IPLVFHSLCN FM
