PIGP_MOUSE
ID PIGP_MOUSE Reviewed; 132 AA.
AC Q9JHG1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit P {ECO:0000305};
DE AltName: Full=Down syndrome critical region protein 5 homolog;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class P protein;
DE Short=PIG-P;
GN Name=Pigp {ECO:0000312|MGI:MGI:1860433}; Synonyms=Dcrc, Dscr5;
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], AND TISSUE SPECIFICITY.
RX PubMed=11331941; DOI=10.1007/s003350010283;
RA Choi D.K., Suzuki Y., Yoshimura S., Togashi T., Hida M., Taylor T.D.,
RA Wang Y., Sugano S., Hattori M., Sakaki Y.;
RT "Molecular cloning and characterization of a gene expressed in mouse
RT developing tongue, mDscr5 gene, a homolog of human DSCR5 (Down syndrome
RT critical region gene 5).";
RL Mamm. Genome 12:347-351(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Salivary gland, and Thymus;
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: Part of the glycosylphosphatidylinositol-N-
CC acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the
CC transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to
CC phosphatidylinositol and participates in the first step of GPI
CC biosynthesis. {ECO:0000250|UniProtKB:P57054}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000250|UniProtKB:P57054}.
CC -!- SUBUNIT: Component of the glycosylphosphatidylinositol-N-
CC acetylglucosaminyltransferase (GPI-GnT) complex composed at least by
CC PIGA, PIGC, PIGH, PIGP, PIGQ, PIGY and DPM2. Interacts directly with
CC PIGA and PIGQ. {ECO:0000250|UniProtKB:P57054}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in tongue. {ECO:0000269|PubMed:11331941}.
CC -!- SIMILARITY: Belongs to the PIGP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=PIG-
CC P_DCRC-1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_593";
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DR EMBL; AF216306; AAF32294.1; -; mRNA.
DR EMBL; AF216307; AAF32295.1; -; mRNA.
DR EMBL; AF216308; AAF32296.1; -; mRNA.
DR EMBL; AF216309; AAF32297.1; -; mRNA.
DR EMBL; AK004169; BAB23204.1; -; mRNA.
DR EMBL; BC038252; AAH38252.1; -; mRNA.
DR EMBL; BC061116; AAH61116.1; -; mRNA.
DR EMBL; BC096569; AAH96569.1; -; mRNA.
DR CCDS; CCDS28348.1; -.
DR RefSeq; NP_001153088.1; NM_001159616.1.
DR RefSeq; NP_001153089.1; NM_001159617.1.
DR RefSeq; NP_001153090.1; NM_001159618.1.
DR RefSeq; NP_001153091.1; NM_001159619.1.
DR RefSeq; NP_062416.1; NM_019543.3.
DR AlphaFoldDB; Q9JHG1; -.
DR STRING; 10090.ENSMUSP00000109547; -.
DR iPTMnet; Q9JHG1; -.
DR PhosphoSitePlus; Q9JHG1; -.
DR PaxDb; Q9JHG1; -.
DR PRIDE; Q9JHG1; -.
DR ProteomicsDB; 287724; -.
DR Antibodypedia; 8411; 129 antibodies from 23 providers.
DR DNASU; 56176; -.
DR Ensembl; ENSMUST00000113905; ENSMUSP00000109538; ENSMUSG00000022940.
DR Ensembl; ENSMUST00000113906; ENSMUSP00000109539; ENSMUSG00000022940.
DR Ensembl; ENSMUST00000232294; ENSMUSP00000155972; ENSMUSG00000022940.
DR GeneID; 56176; -.
DR KEGG; mmu:56176; -.
DR UCSC; uc008aan.2; mouse.
DR CTD; 51227; -.
DR MGI; MGI:1860433; Pigp.
DR VEuPathDB; HostDB:ENSMUSG00000022940; -.
DR eggNOG; KOG2257; Eukaryota.
DR GeneTree; ENSGT00390000013771; -.
DR InParanoid; Q9JHG1; -.
DR OMA; AIPIWAL; -.
DR OrthoDB; 1225622at2759; -.
DR PhylomeDB; Q9JHG1; -.
DR BRENDA; 2.4.1.198; 3474.
DR Reactome; R-MMU-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 56176; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Pigp; mouse.
DR PRO; PR:Q9JHG1; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9JHG1; protein.
DR Bgee; ENSMUSG00000022940; Expressed in quadriceps femoris and 79 other tissues.
DR ExpressionAtlas; Q9JHG1; baseline and differential.
DR Genevisible; Q9JHG1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; ISO:MGI.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:MGI.
DR InterPro; IPR013717; PIG-P.
DR InterPro; IPR016542; PIG-P_GPI19.
DR Pfam; PF08510; PIG-P; 1.
DR PIRSF; PIRSF008765; PIG-P_GPI19; 1.
PE 2: Evidence at transcript level;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..132
FT /note="Phosphatidylinositol N-acetylglucosaminyltransferase
FT subunit P"
FT /id="PRO_0000191784"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 132 AA; 15101 MW; D21472651F850F9D CRC64;
MVENSPSPLP ERAIYGFVLF LSSQFGFILY LVWAFVPESW LNSLGLTYWP QKYWAVALPV
YLLITVVIGY VLLFGINMMS TSPLDSIHTI TDNYAKNQQR KNYQEDAIPA LRDVPISEVN
KMFFLGAKEL NT
