PGAP2_MOUSE
ID PGAP2_MOUSE Reviewed; 254 AA.
AC Q3TQR0; Q3TVW2; Q3U814; Q3UJI0; Q99KA1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Post-GPI attachment to proteins factor 2;
DE AltName: Full=FGF receptor-activating protein 1;
GN Name=Pgap2; Synonyms=Frag1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Bone marrow, and Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH PGAP2IP.
RX PubMed=17761529; DOI=10.1091/mbc.e07-05-0482;
RA Umemura M., Fujita M., Yoko-O T., Fukamizu A., Jigami Y.;
RT "Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid
RT moiety of GPI anchors to ceramides.";
RL Mol. Biol. Cell 18:4304-4316(2007).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PGAP2IP. {ECO:0000269|PubMed:17761529}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TQR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TQR0-2; Sequence=VSP_032553;
CC Name=3;
CC IsoId=Q3TQR0-3; Sequence=VSP_032552;
CC -!- SIMILARITY: Belongs to the PGAP2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE37322.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK134287; BAE22083.1; -; mRNA.
DR EMBL; AK146442; BAE27175.1; -; mRNA.
DR EMBL; AK152420; BAE31205.1; -; mRNA.
DR EMBL; AK159933; BAE35494.1; -; mRNA.
DR EMBL; AK159950; BAE35506.1; -; mRNA.
DR EMBL; AK163373; BAE37322.1; ALT_INIT; mRNA.
DR EMBL; BC004794; AAH04794.1; -; mRNA.
DR CCDS; CCDS40048.1; -. [Q3TQR0-2]
DR CCDS; CCDS90290.1; -. [Q3TQR0-1]
DR RefSeq; NP_001278287.1; NM_001291358.1. [Q3TQR0-2]
DR RefSeq; NP_663558.1; NM_145583.3. [Q3TQR0-2]
DR RefSeq; XP_006507706.1; XM_006507643.3.
DR RefSeq; XP_006507707.1; XM_006507644.3. [Q3TQR0-1]
DR RefSeq; XP_006507708.1; XM_006507645.2.
DR RefSeq; XP_006507709.1; XM_006507646.2.
DR RefSeq; XP_006507713.1; XM_006507650.3.
DR RefSeq; XP_006507714.1; XM_006507651.3.
DR AlphaFoldDB; Q3TQR0; -.
DR BioGRID; 231428; 1.
DR STRING; 10090.ENSMUSP00000033292; -.
DR PhosphoSitePlus; Q3TQR0; -.
DR MaxQB; Q3TQR0; -.
DR PaxDb; Q3TQR0; -.
DR PRIDE; Q3TQR0; -.
DR ProteomicsDB; 288048; -. [Q3TQR0-1]
DR ProteomicsDB; 288049; -. [Q3TQR0-2]
DR ProteomicsDB; 288050; -. [Q3TQR0-3]
DR Antibodypedia; 42139; 87 antibodies from 16 providers.
DR Ensembl; ENSMUST00000033292; ENSMUSP00000033292; ENSMUSG00000030990. [Q3TQR0-1]
DR Ensembl; ENSMUST00000120879; ENSMUSP00000114016; ENSMUSG00000030990. [Q3TQR0-2]
DR Ensembl; ENSMUST00000156529; ENSMUSP00000121521; ENSMUSG00000030990. [Q3TQR0-2]
DR GeneID; 233575; -.
DR KEGG; mmu:233575; -.
DR UCSC; uc009ird.2; mouse. [Q3TQR0-2]
DR UCSC; uc009ire.1; mouse. [Q3TQR0-1]
DR CTD; 27315; -.
DR MGI; MGI:2385286; Pgap2.
DR VEuPathDB; HostDB:ENSMUSG00000030990; -.
DR eggNOG; KOG3979; Eukaryota.
DR GeneTree; ENSGT00510000047299; -.
DR InParanoid; Q3TQR0; -.
DR OMA; HYREHIR; -.
DR OrthoDB; 1166083at2759; -.
DR PhylomeDB; Q3TQR0; -.
DR TreeFam; TF314112; -.
DR BioGRID-ORCS; 233575; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Pgap2; mouse.
DR PRO; PR:Q3TQR0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3TQR0; protein.
DR Bgee; ENSMUSG00000030990; Expressed in lens of camera-type eye and 74 other tissues.
DR ExpressionAtlas; Q3TQR0; baseline and differential.
DR Genevisible; Q3TQR0; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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 GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR039545; PGAP2.
DR PANTHER; PTHR12892; PTHR12892; 1.
DR Pfam; PF10277; Frag1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Golgi apparatus;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..254
FT /note="Post-GPI attachment to proteins factor 2"
FT /id="PRO_0000326095"
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 1..33
FT /note="MYQVPLTLDRDGTLVRLRFTMVALITVCCPLVA -> MFSAALDPDGTVFRL
FT RFTAFVWWVITFPLFG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032552"
FT VAR_SEQ 172..175
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032553"
FT CONFLICT 39
FT /note="L -> I (in Ref. 1; BAE31205)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="L -> V (in Ref. 1; BAE31205)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..53
FT /note="KETTSTH -> EYTVATD (in Ref. 1; BAE31205)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="S -> A (in Ref. 1; BAE27175)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="H -> R (in Ref. 1; BAE35506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 29446 MW; 9509552B88374A55 CRC64;
MYQVPLTLDR DGTLVRLRFT MVALITVCCP LVAFFFCILW SLLFHFKETT STHCGVPNYL
PSVSSAIGGE VPQRYVWRFC IGLHSAPRFL TAFAYWNHYL SCASPCPGYR LLCRINFSLN
VVENLALLVL TYVSSSEDFT IHENAFIVFI AASLGYMLLT CILWRLTKKH TVSQEDRKSY
SWKQRLFVIN FISFFSALAV YFRHNMYCEA GVYTIFAILE YTVVLTNMAF HMTAWWDFGN
KELLITSQPE EKRF
