PGAP1_DROME
ID PGAP1_DROME Reviewed; 980 AA.
AC Q9W495; Q8T8Q8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
DE AltName: Full=Post-GPI attachment to proteins factor 1;
GN Name=PGAP1 {ECO:0000312|FlyBase:FBgn0029789};
GN ORFNames=CG3160 {ECO:0000312|FlyBase:FBgn0029789};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Involved in inositol deacylation of GPI-anchored proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000305}.
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DR EMBL; AE014298; AAF46062.3; -; Genomic_DNA.
DR EMBL; AY075574; AAL68379.1; -; mRNA.
DR RefSeq; NP_572245.1; NM_132017.2.
DR AlphaFoldDB; Q9W495; -.
DR BioGRID; 57990; 3.
DR IntAct; Q9W495; 5.
DR STRING; 7227.FBpp0070812; -.
DR ESTHER; drome-CG3160; PGAP1.
DR GlyGen; Q9W495; 3 sites.
DR PaxDb; Q9W495; -.
DR PRIDE; Q9W495; -.
DR EnsemblMetazoa; FBtr0070847; FBpp0070812; FBgn0029789.
DR GeneID; 31487; -.
DR KEGG; dme:Dmel_CG3160; -.
DR UCSC; CG3160-RA; d. melanogaster.
DR CTD; 80055; -.
DR FlyBase; FBgn0029789; PGAP1.
DR VEuPathDB; VectorBase:FBgn0029789; -.
DR eggNOG; KOG3724; Eukaryota.
DR GeneTree; ENSGT00940000167854; -.
DR HOGENOM; CLU_013735_1_0_1; -.
DR InParanoid; Q9W495; -.
DR OMA; YGLYYYY; -.
DR OrthoDB; 438490at2759; -.
DR PhylomeDB; Q9W495; -.
DR BioGRID-ORCS; 31487; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31487; -.
DR PRO; PR:Q9W495; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029789; Expressed in mouthpart and 22 other tissues.
DR Genevisible; Q9W495; DM.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006505; P:GPI anchor metabolic process; IBA:GO_Central.
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 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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..980
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277627"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..628
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 629..649
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 650..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..774
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 775..795
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 796..867
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 889..895
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 896..916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 917..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 951..954
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 955..975
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 976..980
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 821..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /evidence="ECO:0000250"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 459
FT /note="L -> V (in Ref. 3; AAL68379)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="E -> D (in Ref. 3; AAL68379)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 111625 MW; 72EA24B3B68E18EF CRC64;
MFMFRNCAVL LVIGSICCFI YGLFRLHVEV EPNACRMTYM FGEPMFAKVG VRDGDQYPNY
ALYYYYEGLR QPLDPLKRRM TGAPVIFVPG NAGSYKQVRS LASVALRKAM SNDAGIHLDY
YTIDYDEELS ALYGGYLHRQ QSYLKLCIRT ILSIYEGRTE QPSIVLIGHS MGGKLAQSVL
VDPAIGQHIN TIISISTPLD QPVLNLDTQL EEFYDQTDAV LSKLRTATVP TMTTNVCDSL
HQRPPSVQRM ASQDSSARLD NVLLISTGGG NRDLLVRPGL TSSRFNDLHA MTSAIPKVSL
SCDHLSAVWC LQFMQAINRF LFSVAYVRED RSSIAFGTNK QRNLQTALST FVKPRRRQQN
TVRFGAAGNW HEERRLVINK YFTNGLKGTF FDLIGLQRQE RYRKAAIEAL NVDDEDWLFG
CSAEDNNKTG QLYCEKATSL MHLVQWLPNE DREPRSIALL DLHNLRKTYV HWTHLLVRLP
PSAKRIGYNL DIYDPKERVT DIKMPRWYTM AKLPLINETL QGTLHHRVRI SEMVDPYQSI
RVIVEPLQCI NPEYRVTARI CVPWAAGFER FQTLKSFDQK PQLYVNVPTL VPRHYNTTLN
PVTLELYLDP TCRYRISYEY SYSSALSRLV LEFYGWLPAH LVCVLLIVLR KQVETFYDVG
TFRSLRPYVG YLQYTSLYIV TACRLLKKLI ISSRVFPEPE PLDYSINVSI VIHCAAIALS
LLATLGTWLA LTLYGNAFYR LALRITRLSQ ATSNVMISIM THLPITYGIL TIATAMGTCS
GVGLLLAFVF YFLMLSNAYK DYLEDFLWQK AANLVRGKPS AVTEQEDATE EQNEEQNALK
QNDEQKQQQQ EEEEPEACVG LQNFSFHVTL LLMLFVQLLL NAPSSLAWLR SRRHGINLPD
PSLYPSIVVL ASLSLLLQLR APQKCQGYWM LSIAFYILAG VVLLYCQAAI YRLTYVIAGA
FALLSAHQSL WILWGRVSRV
