ID A0A1I7T2H1_9PELO Unreviewed; 215 AA.
AC A0A1I7T2H1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Post-GPI attachment to proteins factor 2 {ECO:0000256|ARBA:ARBA00016871};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold478.g1786.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold478.g1786.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00024944}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004653}.
CC -!- SIMILARITY: Belongs to the PGAP2 family.
CC {ECO:0000256|ARBA:ARBA00007414}.
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DR AlphaFoldDB; A0A1I7T2H1; -.
DR STRING; 1561998.A0A1I7T2H1; -.
DR WBParaSite; Csp11.Scaffold478.g1786.t1; Csp11.Scaffold478.g1786.t1; Csp11.Scaffold478.g1786.
DR eggNOG; KOG3979; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR039545; PGAP2.
DR PANTHER; PTHR12892; FGF RECEPTOR ACTIVATING PROTEIN 1; 1.
DR PANTHER; PTHR12892:SF11; POST-GPI ATTACHMENT TO PROTEINS FACTOR 2; 1.
DR Pfam; PF10277; Frag1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 215 AA; 23913 MW; 488FC7F3ADD21E1A CRC64;
MALGDDDILP IPFKYFVYCI GGLPASALLI CVLLSLLLHF DQATSTHCEV PNWLPSISAA
VATYTPEKYI WRILIALHIS PRLYVAGAFR HFLISSPLRP YTGSKRFKFL CDIACGLNIL
EIFFLLALTC ISSTEDHSLH AKCFGGFAIS SIIYMLMSTW LFSESGRRRA THLGEKSYEY
KILGASAFVV FSSWVLMSIG GTILTVKREL TLSSL
//