PGAP2_RAT
ID PGAP2_RAT Reviewed; 254 AA.
AC Q2ABP3; P70561;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Post-GPI attachment to proteins factor 2;
DE AltName: Full=FGF receptor-activating protein 1;
GN Name=Pgap2; Synonyms=Frag1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND CHROMOSOMAL TRANSLOCATION WITH FGFR2.
RC TISSUE=Brain;
RX PubMed=8799135; DOI=10.1073/pnas.93.17.8956;
RA Lorenzi M.V., Horii Y., Yamanaka R., Sakaguchi K., Miki T.;
RT "FRAG1, a gene that potently activates fibroblast growth factor receptor by
RT C-terminal fusion through chromosomal rearrangement.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8956-8961(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
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; Multi-pass membrane
CC protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2ABP3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2ABP3-2; Sequence=VSP_032554;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver,
CC skeletal muscle, kidney and testis. {ECO:0000269|PubMed:8799135}.
CC -!- MISCELLANEOUS: In osteosarcoma cells, a chromosomal translocation with
CC FGFR2 results in an in-frame fusion of the two genes. This generates
CC FGFR2-ROS, a chimeric protein with transforming activity.
CC -!- SIMILARITY: Belongs to the PGAP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB07050.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U57715; AAB07050.1; ALT_FRAME; mRNA.
DR EMBL; AB236144; BAE80228.1; -; mRNA.
DR PIR; JC6168; JC6168.
DR RefSeq; NP_446347.2; NM_053895.2. [Q2ABP3-2]
DR RefSeq; XP_006229899.1; XM_006229837.3. [Q2ABP3-1]
DR AlphaFoldDB; Q2ABP3; -.
DR STRING; 10116.ENSRNOP00000027628; -.
DR PaxDb; Q2ABP3; -.
DR GeneID; 116675; -.
DR KEGG; rno:116675; -.
DR UCSC; RGD:619744; rat. [Q2ABP3-1]
DR CTD; 27315; -.
DR RGD; 619744; Pgap2.
DR VEuPathDB; HostDB:ENSRNOG00000020371; -.
DR eggNOG; KOG3979; Eukaryota.
DR HOGENOM; CLU_061191_1_0_1; -.
DR InParanoid; Q2ABP3; -.
DR OrthoDB; 1166083at2759; -.
DR PhylomeDB; Q2ABP3; -.
DR TreeFam; TF314112; -.
DR PRO; PR:Q2ABP3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020371; Expressed in lung and 19 other tissues.
DR ExpressionAtlas; Q2ABP3; baseline and differential.
DR Genevisible; Q2ABP3; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IGI:RGD.
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 Alternative splicing; Chromosomal rearrangement; Endoplasmic reticulum;
KW Golgi apparatus; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Post-GPI attachment to proteins factor 2"
FT /id="PRO_0000326096"
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"
FT VAR_SEQ 172..175
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8799135"
FT /id="VSP_032554"
SQ SEQUENCE 254 AA; 29491 MW; 314EF507FE4D8404 CRC64;
MYQVPLTLDR DGTLVRLRFT MVALITVCCP LVAFFFCILW SLLFHFKETT STHCGVPNYL
PSVSSAIGGE VPQRYVWRFC IGLHSAPRFL TAFAYWNHYL SCASPCPGYR LLCRLNFSLN
VVENLALLVL TYVSSSEDFT IHENAFIVFI AASLSYMLLT CILWRLTKKH TVSQEDRKSY
SWKQRLFIIN FISFFSALAV YFRHNMYCEA GVYTIFAILE YTVVLTNMAF HMTAWWDFGN
KELLITSQPE EKRF
