PIGO_MOUSE
ID PIGO_MOUSE Reviewed; 1093 AA.
AC Q9JJI6; Q9CRY2;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=GPI ethanolamine phosphate transferase 3;
DE EC=2.-.-.-;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class O protein;
DE Short=PIG-O;
GN Name=Pigo;
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], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=10781593; DOI=10.1074/jbc.m001913200;
RA Hong Y., Maeda Y., Watanabe R., Inoue N., Ohishi K., Kinoshita T.;
RT "Requirement of PIG-F and PIG-O for transferring phosphoethanolamine to the
RT third mannose in glycosylphosphatidylinositol.";
RL J. Biol. Chem. 275:20911-20919(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 923-1093.
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
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).
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the GPI third mannose which links the GPI-
CC anchor to the C-terminus of the proteins by an amide bond.
CC {ECO:0000269|PubMed:10781593}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with PIGF. PIGF is required to stabilize PIGO.
CC {ECO:0000269|PubMed:10781593}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10781593}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10781593}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96254.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB038560; BAA96254.1; ALT_INIT; mRNA.
DR EMBL; AK013913; BAB29052.1; -; mRNA.
DR AlphaFoldDB; Q9JJI6; -.
DR SMR; Q9JJI6; -.
DR STRING; 10090.ENSMUSP00000095713; -.
DR GlyGen; Q9JJI6; 1 site.
DR PhosphoSitePlus; Q9JJI6; -.
DR EPD; Q9JJI6; -.
DR MaxQB; Q9JJI6; -.
DR PaxDb; Q9JJI6; -.
DR PRIDE; Q9JJI6; -.
DR ProteomicsDB; 287723; -.
DR MGI; MGI:1861452; Pigo.
DR eggNOG; KOG2126; Eukaryota.
DR InParanoid; Q9JJI6; -.
DR UniPathway; UPA00196; -.
DR ChiTaRS; Pigo; mouse.
DR PRO; PR:Q9JJI6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JJI6; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; ISO:MGI.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; TAS:MGI.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:UniProtKB.
DR CDD; cd16023; GPI_EPT_3; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037675; PIG-O_N.
DR InterPro; IPR039524; PIGO/GPI13.
DR PANTHER; PTHR23071; PTHR23071; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1093
FT /note="GPI ethanolamine phosphate transferase 3"
FT /id="PRO_0000058439"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 945..965
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1018..1038
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1052..1072
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 971..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1000
FT /note="V -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1093 AA; 119156 MW; AB641F9F3527296C CRC64;
MRKVSVLLFL AWVCFLFYAG IALFTSGFLL TRLELTNQSS CQELPGPGPL PWGSHGKPGA
CWMPSRFSRV VLVLIDALRF DFAQPQRSHV PGEPPVSVPF LGKLGSLQRI LESQPHHGRL
YRSQVDPPTT TMQRLKALTT GSLPTFIDAG SNFASHAIVE DNVIQQLNSA GRRVVFMGDD
TWRDLFPGAF SQAFFFSSFN VRDLHTVDNG ILEHLYPTLD GGSWDVLIAH FLGVDHCGHK
HGPHHPEMAK KLSQMDQVIQ GLIERLENDT LLVVAGDHGM TMNGDHGGDS ELEVSAALFL
YSPTALFPSV PPEEPEVIPQ VSLVPTLALL LGLPIPFGNT GEVMAELFSG GSDSSHPHSS
ALAQVSALHI NAQQVSRFLH TYSAATQDLQ VKELHRLQTL FSKASARYQH FLRDPQEAEA
ALSTLTAEFQ QFLRGARALC IESWARFSLV RMAGGAALLA AACLLCLLAS QLAVAPGFLF
RPLLLIPVAW GLTWTILYAG VSVTTGSKID LVVLGAVAAA GSLLPFLWKA WVSRGSKRPL
APLLPVPRPV LILLLIRLAT FFSDSFFVVE ARATPFLLGS LVFFLVAQLH WEGQLLPPKP
LTMSRLGSSA PTAPPRHSGA HALWLGIGLL LFTRLAGLFH RCPEETPACR SSPWLSPLAS
MVGGRAKNLW YGACVGALVA LLVVVRLWLR RYGNLKSPEP PVLFVRWGMP LMVLGTAAYW
ALASGAEEAP PRLRALVAGA SAVLPRAVMG LAALGLVLLL WRPVTVLVKA GAATSRTRTI
LTPFSGPPTS QADLDYVVPQ IYRHMQEEFQ GRLERTKAQG PITVAAYQLG SVYSAAMVTA
LLLLAFPLML LHVERVSLVF LLLFLQSFLL LHLLAAGTPV ATPGPFTVLW QAVSAWVLLA
TQTFYSTGHQ PVFSAIHWHA AFVGFPDGHG SSTWLPALLV GANTFASHLL FAVGCPLLLL
WPFLCERQGP KRRQPLPGSE SEARVRPEEE EELQEPLMEV RLRDAPNHFN AALLQLGLKY
LFILGAQILA CALAASILRR HLMVWKVFAP KFIFEAVGFI VSSVGLLLGI ALVMRVDVAV
SSWFKKLVLA QQR
