ID A0A2A3EFG2_APICC Unreviewed; 270 AA.
AC A0A2A3EFG2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Post-GPI attachment to proteins factor 2 {ECO:0000256|ARBA:ARBA00016871};
GN ORFNames=APICC_06407 {ECO:0000313|EMBL:PBC29949.1};
OS Apis cerana cerana (Oriental honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC29949.1, ECO:0000313|Proteomes:UP000242457};
RN [1] {ECO:0000313|EMBL:PBC29949.1, ECO:0000313|Proteomes:UP000242457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC29949.1};
RA Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA Wu J.;
RT "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT insights into honey bee biology.";
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}.
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DR EMBL; KZ288269; PBC29949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3EFG2; -.
DR STRING; 94128.A0A2A3EFG2; -.
DR Proteomes; UP000242457; 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:UP000242457};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 270 AA; 31632 MW; ECC04A8DBA65D50D CRC64;
MVDCMLNIPI KMNKSRVGSE YIPLVGDDML QTRYVLHFAK LAWFTVSLPF FAFLFCITWS
VVYNFEHSTS THCKVYNFLP SVSAAIGHYR PQRDVWKIAI ALQAVVRILV LIMYRRYYKE
HIYKWAQNIC NVATVIYAIE NISLISLSFW TSNENYVFHK VSFITFLITS VIHMQIAYYI
MRNCRNITKE SSEAISLKWK RRSMMLNLLC ILFAAYFFYR HNKYCEPLVY SMFALSEYGV
VLSNIGFHST TAWDFANSSL MISGKGFRII
//
