PGAP1_XENLA
ID PGAP1_XENLA Reviewed; 927 AA.
AC Q66J01;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=GPI inositol-deacylase;
DE EC=3.1.-.-;
DE AltName: Full=Post-GPI attachment to proteins factor 1;
GN Name=pgap1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the GPI inositol-deacylase family.
CC {ECO:0000305}.
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DR EMBL; BC081123; AAH81123.1; -; mRNA.
DR RefSeq; NP_001087710.1; NM_001094241.1.
DR AlphaFoldDB; Q66J01; -.
DR ESTHER; xenla-q66j01; PGAP1.
DR MaxQB; Q66J01; -.
DR PRIDE; Q66J01; -.
DR DNASU; 447534; -.
DR GeneID; 447534; -.
DR KEGG; xla:447534; -.
DR CTD; 447534; -.
DR Xenbase; XB-GENE-5818693; pgap1.L.
DR OrthoDB; 438490at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 447534; Expressed in egg cell and 18 other tissues.
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: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..927
FT /note="GPI inositol-deacylase"
FT /id="PRO_0000277626"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..595
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..672
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..733
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 755..821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 843..858
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 888..908
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 909..927
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 169
FT /evidence="ECO:0000250"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 927 AA; 105636 MW; 281849F45530F44E CRC64;
MNPLSAVFNS VVLVLLALGV TDVFFSYESS RCSMTYMFEY PQYLQIKLSK KVSRLYPLYE
LYLYGEGSYA EENKNLTLTG VPVLFLPGNA GSYKQARSFA SVALRKAENI GNRYHFNIFT
VNFNEELVAL YGGSLRRQTR FVHECIKTIL SLYKNQTFPP ESVAIIGHSM GGLVARALFT
LKHFKPDLIN VIITQATPHI LPVLSTDIYL TDFYTMVNNY WIYNSLKLRN ITMLSVAGGY
SDYQVRSGLT FLPTSSFHTS ALSVVSSAVP ITWASTDHLS IVWCRELVLV TARALFDLID
EHTKQINIDP QSRMSVIKHH FVRHPAKHLE SRHQITASFT ETPKFTLVED SKWTYTVNKE
SNESFFLFPL LDKRIAYSHF HCQNTFLYTH SWIFGCNKTV SPKCLQINDL SWETELLPSA
KVVNLKLDVY SNLSHFILYI PATNGSKFSV ECEFLSEEAR TVHVPVTHVL SFGFSSSHAP
LNSSGLLYVI QFEDFSKIYQ AFNVFIVRNC GQNKESKSSI YKFHVPWSHE DLIGVLSDEL
PVRISAKLHA EQPQNDNRLV KLFLYASPEC LHEVTISTSF SQILGQIVRF HGIYLPVYIV
ANLLLAYGAQ LHSILIQGSC MDLDLSFDVA AKPYKVDPVL IICKYLLNYK WFKNYWDGLM
LPQLDAVQLH AYGFWFPLAS LFFFIFGTSI AYWSSIGLQA AVRILSSLWI YLKRPSMFPK
ESKCITYRVY AETLFFAFIS WRSCGTFSLL LVFLRYLSKV LILYSSMKNY VSLNAHIVKD
TSSKQDSVKT DSDTNINSNQ LTHHQPSSLE IKALDDCLKM HFTILHLNLW IVLLGLPSFI
YWLKTLRYTI QLDPDPNRVS ALVLIFILEI LMNSTTSAIK SSVCLKTAAV LQLPLSIIVV
AFGTLHLYRI SNLIAFSLFL HVVCCFV
