PGAP2_CRIGR
ID PGAP2_CRIGR Reviewed; 254 AA.
AC Q2ABP2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Post-GPI attachment to proteins factor 2;
DE AltName: Full=FGF receptor-activating protein 1;
GN Name=Pgap2; Synonyms=Frag1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=16407401; DOI=10.1091/mbc.e05-11-1005;
RA Tashima Y., Taguchi R., Murata C., Ashida H., Kinoshita T., Maeda Y.;
RT "PGAP2 is essential for correct processing and stable expression of GPI-
RT anchored proteins.";
RL Mol. Biol. Cell 17:1410-1420(2006).
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:0000269|PubMed:16407401}.
CC -!- SUBUNIT: Interacts with PGAP2IP. {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; AB236145; BAE80229.1; -; mRNA.
DR RefSeq; NP_001233740.1; NM_001246811.1.
DR AlphaFoldDB; Q2ABP2; -.
DR STRING; 10029.NP_001233740.1; -.
DR Ensembl; ENSCGRT00001027357; ENSCGRP00001023112; ENSCGRG00001021425.
DR GeneID; 100689385; -.
DR KEGG; cge:100689385; -.
DR CTD; 27315; -.
DR eggNOG; KOG3979; Eukaryota.
DR GeneTree; ENSGT00510000047299; -.
DR OrthoDB; 1166083at2759; -.
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 Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Post-GPI attachment to proteins factor 2"
FT /id="PRO_0000326093"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..114
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..185
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..254
FT /note="Lumenal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 254 AA; 29426 MW; 989179E11D85B99F CRC64;
MYQVPLTLDR DGTLVRLRFT MVALITVCCP LVAFLFCILW SLLFHFKETT STHCGVPNYL
PSVSSAIGGE VPQRYVWRFC IGLHSAPRFL AAFAYWNHYL SCASPCPGYR LLCRLNFSLN
VVENLALLVL TYVSSSEDFT IHENAFIVFI AASLSYMLLT CILWRLTKKH TVSQEDRKSY
SWKQRLFIIN FISFFSALAV YFRHNMYCEA GVYTIFAILE YTVVLTNMAF HMTAWWDFGN
KELLITSQPE EKRF