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Database: UniProt
Entry: A0A1J1IJK0_9DIPT
LinkDB: A0A1J1IJK0_9DIPT
Original site: A0A1J1IJK0_9DIPT 
ID   A0A1J1IJK0_9DIPT        Unreviewed;       266 AA.
AC   A0A1J1IJK0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-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=CLUMA_CG013678 {ECO:0000313|EMBL:CRL00411.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRL00411.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRL00411.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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; CVRI01000054; CRL00411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1IJK0; -.
DR   STRING; 568069.A0A1J1IJK0; -.
DR   OrthoDB; 3668913at2759; -.
DR   Proteomes; UP000183832; 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:UP000183832};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        222..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   266 AA;  31364 MW;  BA7A3B220FA1408D CRC64;
     MKRRKMLPEY QKLKDENGLI DKGPVFTISF SRFSLITVSL PLFSFIFCVS YSLLFFFEQS
     TSTHCHVWNY LPSISAAIGS FQPQAFVWQI SIIVHFIPRL IITWMYKSYY DRVIRRNRQN
     VAKFALLLNV VENFSLLGLS IYTSNDNYEI HKNCFCTFIV VSETYMMLSY YLNKNAKRDP
     KSSHSENKSI NLKRNLFIIN ITSIVLAAYF FVRHNDRCEG GIYTFFALFE YIVVLTNMGY
     HMTAAIDFHN QHLVFDWHHG LQIHFQ
//
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