ID A0A093X737_9PEZI Unreviewed; 309 AA.
AC A0A093X737;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Post-GPI attachment to proteins factor 2 {ECO:0000256|ARBA:ARBA00016871};
DE Flags: Fragment;
GN ORFNames=O988_09018 {ECO:0000313|EMBL:KFX88443.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX88443.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFX88443.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX88443.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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. {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX88443.1}.
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DR EMBL; JPJR01002447; KFX88443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093X737; -.
DR STRING; 1391699.A0A093X737; -.
DR HOGENOM; CLU_901831_0_0_1; -.
DR Proteomes; UP000029329; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 309
FT /evidence="ECO:0000313|EMBL:KFX88443.1"
SQ SEQUENCE 309 AA; 35026 MW; 60AE4966BE2C3ED6 CRC64;
MAPKTKDGDV VLAFSGKWVT WAHTFTAYAA FISALIVGVS LHYHKIVKNE HYGYPQEWFP
SVSATIGDRY PERSFFMFFI AITSGPRFAL VGLWYLLTKR PGQQLSKYVA IVGIFRTITC
GGWTYVTSTD DHDWHDIFMI SYLVATLPWT LGCLALSPPN PTTIKYRKIF GGAFFGTIVP
LVYFFIQHKV HKIAGAYTTY AFFEWTLVLL DVAFDAVTML DFDSFEVVIK DVTGASKGQP
KRDSGIEMHK DKPVVQVLNQ SFLWTDAIDA VAEVYHGFVF WSMLTSLGLC VWYFPLWNMG
ISGYEILVM
//
