PGAP3_MOUSE
ID PGAP3_MOUSE Reviewed; 320 AA.
AC A2A559; A2A558; Q3TCA8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Post-GPI attachment to proteins factor 3;
DE AltName: Full=PER1-like domain-containing protein 1;
DE Flags: Precursor;
GN Name=Pgap3; Synonyms=Perld1;
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] (ISOFORM 1).
RC STRAIN=NOD;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Involved in the lipid remodeling steps of GPI-anchor
CC maturation. Lipid remodeling steps consist in the generation of 2
CC saturated fatty chains at the sn-2 position of GPI-anchors proteins.
CC Required for phospholipase A2 activity that removes an acyl-chain at
CC the sn-2 position of GPI-anchors during the remodeling of GPI (By
CC similarity). {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}. Note=Mainly
CC localizes to Golgi apparatus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2A559-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A559-2; Sequence=VSP_034159;
CC -!- SIMILARITY: Belongs to the PGAP3 family. {ECO:0000305}.
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DR EMBL; AK170817; BAE42049.1; -; mRNA.
DR EMBL; AL591390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25348.1; -. [A2A559-1]
DR RefSeq; NP_001028709.2; NM_001033537.2. [A2A559-1]
DR RefSeq; XP_006533612.1; XM_006533549.3. [A2A559-2]
DR AlphaFoldDB; A2A559; -.
DR BioGRID; 236192; 3.
DR STRING; 10090.ENSMUSP00000088337; -.
DR GlyGen; A2A559; 1 site.
DR MaxQB; A2A559; -.
DR PaxDb; A2A559; -.
DR PRIDE; A2A559; -.
DR ProteomicsDB; 301798; -. [A2A559-1]
DR ProteomicsDB; 301799; -. [A2A559-2]
DR Antibodypedia; 16261; 160 antibodies from 22 providers.
DR DNASU; 320655; -.
DR Ensembl; ENSMUST00000090827; ENSMUSP00000088337; ENSMUSG00000038208. [A2A559-1]
DR Ensembl; ENSMUST00000128897; ENSMUSP00000119668; ENSMUSG00000038208. [A2A559-2]
DR GeneID; 320655; -.
DR KEGG; mmu:320655; -.
DR UCSC; uc007lgh.1; mouse. [A2A559-1]
DR CTD; 93210; -.
DR MGI; MGI:2444461; Pgap3.
DR VEuPathDB; HostDB:ENSMUSG00000038208; -.
DR eggNOG; KOG2970; Eukaryota.
DR GeneTree; ENSGT00390000001304; -.
DR HOGENOM; CLU_032917_1_0_1; -.
DR InParanoid; A2A559; -.
DR OMA; FMIEDCR; -.
DR OrthoDB; 828384at2759; -.
DR PhylomeDB; A2A559; -.
DR TreeFam; TF300031; -.
DR BioGRID-ORCS; 320655; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Pgap3; mouse.
DR PRO; PR:A2A559; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2A559; protein.
DR Bgee; ENSMUSG00000038208; Expressed in retinal neural layer and 97 other tissues.
DR Genevisible; A2A559; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; ISS:UniProtKB.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:MGI.
DR GO; GO:0006505; P:GPI anchor metabolic process; ISS:UniProtKB.
DR InterPro; IPR007217; Per1-like.
DR PANTHER; PTHR13148; PTHR13148; 1.
DR Pfam; PF04080; Per1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..320
FT /note="Post-GPI attachment to proteins factor 3"
FT /id="PRO_0000339357"
FT TOPO_DOM 24..98
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..169
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..223
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 94..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034159"
FT CONFLICT 277
FT /note="L -> P (in Ref. 1; BAE42049)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="L -> P (in Ref. 1; BAE42049)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 36528 MW; 151EA9AB17E95BDC CRC64;
MAKRTAPLLL LTLAVGLAGG SQGDREPVYR DCVLRCEERN CSGDALKHFR SRQPIYMSLA
GWTCRDDCKY ECMWFTVGLY LQEGHRVPQF HGKWPFSRFL FIQEPASAVA SLLNGLASLV
MLCRYRASVP ASSPMYHTCM AFAWVSLNAW FWSTVFHTRD TDLTEKMDYF CASAVILHSV
YLCCVRTVGL QHPSVASAFG ALLLLLLTGH ISYLSLVHFD YGYNMMANVA IGLVNLAWWL
VWCLRNRQRL PHTRRCMVVV VLLQGLSLLE LLDFPPLFWV LDAHAIWHIS TIPVHTLFFR
FLEDDSLYLL KESGAMFKLD
