PIGN_MOUSE
ID PIGN_MOUSE Reviewed; 931 AA.
AC Q9R1S3; Q3V0S6; Q8VCC3; Q9R1S1; Q9R1S2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class N protein;
DE Short=PIG-N;
GN Name=Pign;
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 [MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 1-391, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=10574991; DOI=10.1074/jbc.274.49.35099;
RA Hong Y., Maeda Y., Watanabe R., Ohishi K., Mishkind M., Riezman H.,
RA Kinoshita T.;
RT "Pig-n, a mammalian homologue of yeast Mcd4p, is involved in transferring
RT phosphoethanolamine to the first mannose of the
RT glycosylphosphatidylinositol.";
RL J. Biol. Chem. 274:35099-35106(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; 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).
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the first alpha-1,4-linked mannose of the
CC glycosylphosphatidylinositol precursor of GPI-anchor. May act as
CC suppressor of replication stress and chromosome missegregation.
CC {ECO:0000269|PubMed:10574991}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10574991}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10574991}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9R1S3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R1S3-2; Sequence=VSP_019837, VSP_019838;
CC Name=3;
CC IsoId=Q9R1S3-3; Sequence=VSP_019836, VSP_019839;
CC Name=4;
CC IsoId=Q9R1S3-4; Sequence=VSP_019834, VSP_019835;
CC -!- MISCELLANEOUS: Target of the inhibitor of GPI biosynthesis
CC YW3548/BE49385A.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
CC {ECO:0000305}.
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DR EMBL; AB030279; BAA82619.1; -; mRNA.
DR EMBL; AB030280; BAA82620.1; -; mRNA.
DR EMBL; AB030316; BAA82663.1; -; Genomic_DNA.
DR EMBL; AK132928; BAE21427.1; -; mRNA.
DR EMBL; BC021148; AAH21148.1; -; mRNA.
DR CCDS; CCDS15205.1; -. [Q9R1S3-1]
DR AlphaFoldDB; Q9R1S3; -.
DR SMR; Q9R1S3; -.
DR STRING; 10090.ENSMUSP00000139638; -.
DR GlyGen; Q9R1S3; 5 sites.
DR iPTMnet; Q9R1S3; -.
DR PhosphoSitePlus; Q9R1S3; -.
DR SwissPalm; Q9R1S3; -.
DR EPD; Q9R1S3; -.
DR MaxQB; Q9R1S3; -.
DR PaxDb; Q9R1S3; -.
DR PRIDE; Q9R1S3; -.
DR ProteomicsDB; 287719; -. [Q9R1S3-1]
DR ProteomicsDB; 287720; -. [Q9R1S3-2]
DR ProteomicsDB; 287721; -. [Q9R1S3-3]
DR ProteomicsDB; 287722; -. [Q9R1S3-4]
DR UCSC; uc011wqa.2; mouse. [Q9R1S3-4]
DR MGI; MGI:1351629; Pign.
DR eggNOG; KOG2124; Eukaryota.
DR InParanoid; Q9R1S3; -.
DR PhylomeDB; Q9R1S3; -.
DR BRENDA; 2.7.7.B25; 3474.
DR Reactome; R-MMU-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR ChiTaRS; Pign; mouse.
DR PRO; PR:Q9R1S3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R1S3; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; TAS:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR CDD; cd16020; GPI_EPT_1; 1.
DR Gene3D; 3.40.720.10; -; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007070; GPI_EtnP_transferase_1.
DR InterPro; IPR017852; GPI_EtnP_transferase_1_C.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037671; PIGN_N.
DR PANTHER; PTHR12250; PTHR12250; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF04987; PigN; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..931
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246199"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..442
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..618
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..685
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..786
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..824
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 825..845
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 846..858
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 916..931
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..602
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019834"
FT VAR_SEQ 603..692
FT /note="AVFPLMPVVGRKPNLSLVMGAGFLVLLLSLAVVTTLGKRNIKLVKGELLVLL
FT LQMLSTVLSMYVVYSTHHSLLKKEGLPLMNQIVSWATL -> MVLFISITCLYVFSSFS
FT VRTSTCLIVFSCFSLRTCNSLAVFSCISLSDLLKSFLMSSIIIMRYAFKSRSRFSGVLG
FT CPGLGEVGVLGSDD (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019835"
FT VAR_SEQ 791..826
FT /note="VFFLLTAFFGTGNIASINSFDLASVYCFLTVFSPFM -> ILLIFPVFLRLF
FT DYKRIRILLAQENYHRSLKAAWEL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019836"
FT VAR_SEQ 791..798
FT /note="VFFLLTAF -> FFCPRRNY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574991"
FT /id="VSP_019837"
FT VAR_SEQ 799..931
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574991"
FT /id="VSP_019838"
FT VAR_SEQ 827..931
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019839"
FT CONFLICT 17
FT /note="A -> V (in Ref. 1; BAA82619/BAA82620)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="I -> M (in Ref. 1; BAA82619/BAA82620/BAA82663)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="I -> V (in Ref. 1; BAA82619/BAA82620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 931 AA; 105045 MW; 75637C514E8D3AF4 CRC64;
MLLFFALGLL IHFVFFASIF DIYFTSPLVH GMTPQFTPLP PPAKRLVLFV ADGLRADTLY
ELDEDGNSRA PFIRNVIIHE GSWGVSHTRV PTESRPGHVA LIAGFYEDVS AVAKGWKENP
VEFDSLFNES KYTWSWGSPD ILPMFAKGAS GDHVYTYSYD AQREDFGAHD ATKLDTWVFD
KVKDFFDAAR NNQSLFTKVN EEKVVFFLHL LGIDTNGHAH RPSSREYKDN IKKVDDGVKE
IVSIFKHFYG DDGKTAFIFT SDHGMTDWGS HGAGHPSETL TPFVTWGAGI KFPQNVSAQQ
YDDEFLKEWR LENWKRRDVN QADIAPLMAS LIGVPFPLNS VGILPVGYLN NTGLFKAESM
FTNAVQILEQ FKVKMTQKKE ATLPFLFTPF KLLSDSQQLD ILRKARSYIK QEKFDEVVSL
CEELIDLALR GLSYYHTYDR LFLGINVAVG FVGWMSYTSL LIIKSHSNIP KGTRKEGKKP
HCLLLYSFIA TGVLVACFLM IQACPWTYYV YCLLPVPIWY AVLREHEVIQ DLVESLLTFP
RSHFVAYLLV FTLGIEVLVL SFFYRYMLTA GLIVFAGWPF LTQLWTRAKI TFLSWAFFSL
LLAVFPLMPV VGRKPNLSLV MGAGFLVLLL SLAVVTTLGK RNIKLVKGEL LVLLLQMLST
VLSMYVVYST HHSLLKKEGL PLMNQIVSWA TLASSLVAPL LSSTALSQRL ASILLSLMST
YLLLSTGYEA LFPLVLSCLM FVWIQVEQET LQQPGVSCKQ KLTSIQFTCD TDIAQFRQLC
PDDIRRAFFL VFFLLTAFFG TGNIASINSF DLASVYCFLT VFSPFMMGAL MMWKILIPFV
LVMCAFEAVQ ITTQLSSKGL FLVVLIISDI MALHFFFLVK DSGSWLDIGT SISHYVIVMS
MTIFLVFLNG LAQLLTTKKL QLCGKPKSHL M
