ID   PGAP2_XENLA             Reviewed;         254 AA.
AC   Q5M9A7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Post-GPI attachment to proteins factor 2;
GN   Name=pgap2;
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=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the lipid remodeling steps of GPI-anchor
CC       maturation. Required for stable expression of GPI-anchored proteins at
CC       the cell surface (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PGAP2 family. {ECO:0000305}.
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DR   EMBL; BC087380; AAH87380.1; -; mRNA.
DR   RefSeq; NP_001088840.1; NM_001095371.1.
DR   AlphaFoldDB; Q5M9A7; -.
DR   DNASU; 496149; -.
DR   GeneID; 496149; -.
DR   KEGG; xla:496149; -.
DR   CTD; 496149; -.
DR   Xenbase; XB-GENE-6252506; pgap2.L.
DR   OrthoDB; 1166083at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 496149; Expressed in testis and 19 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR   InterPro; IPR039545; PGAP2.
DR   PANTHER; PTHR12892; PTHR12892; 1.
DR   Pfam; PF10277; Frag1; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Golgi apparatus; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..254
FT                   /note="Post-GPI attachment to proteins factor 2"
FT                   /id="PRO_0000326098"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..113
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..186
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..254
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   254 AA;  29553 MW;  DB5EEE07D51BD13D CRC64;
     MVPISMAPDR GANSLVSLRF TTFAVSTVCL PLFAFLFCIV WSLLFNFSET TETHCHVPNY
     LPSVSAAIGG ETPQRYLWRL CIGLHSAPRF LVAMAYLKYY QGTPCSNPYY PRLCHINFLL
     NSCEIFFLML LTYVSSSENH EVHKLGFMSF MFFSLGYMFV TCTLWRMTRK WSGSPEERTS
     YAWKKRLFGF YLLMFLASIV VYIWHNMYCE PGVYTLFAFL EYLVVLSNMA FHMTAWWDFG
     NKELMICSPG DKRI