PIGT_MOUSE
ID PIGT_MOUSE Reviewed; 582 AA.
AC Q8BXQ2; A2A5G2; Q3U2X2; Q99JA3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=GPI transamidase component PIG-T;
DE AltName: Full=Neuronal development-associated protein 7;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class T protein;
DE Flags: Precursor;
GN Name=Pigt; Synonyms=Ndap7;
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Retina;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-582.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=11700951; DOI=10.1023/a:1012317520937;
RA Li Z., Li Q., Sun C.X., Hertz L., Yu A.C.H.;
RT "Cloning and identification of differentially expressed transcripts in
RT primary culture of GABAergic neurons.";
RL Neurochem. Res. 26:1101-1105(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-582.
RC 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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-168.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the GPI transamidase complex. Essential for
CC transfer of GPI to proteins, particularly for formation of carbonyl
CC intermediates (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with PIGK/GPI8, PIGS, PIGU and GPAA1/GAA1. Has
CC a critical role in maintaining the complex by stabilizing the
CC expression of GPAA1 and GPI8 and linking them to PIGS (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein.
CC -!- PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for
CC normal enzyme activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34175.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK32809.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB39711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC34729.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK044499; BAC31951.1; -; mRNA.
DR EMBL; AK155057; BAE33018.1; -; mRNA.
DR EMBL; AL591478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ308886; CAC34729.1; ALT_INIT; mRNA.
DR EMBL; AF361435; AAK32809.1; ALT_INIT; mRNA.
DR EMBL; AB057593; BAB39711.1; ALT_INIT; mRNA.
DR EMBL; BC034175; AAH34175.1; ALT_INIT; mRNA.
DR CCDS; CCDS17038.2; -.
DR RefSeq; NP_598540.2; NM_133779.2.
DR RefSeq; XP_006500484.2; XM_006500421.3.
DR AlphaFoldDB; Q8BXQ2; -.
DR SMR; Q8BXQ2; -.
DR BioGRID; 219713; 5.
DR STRING; 10090.ENSMUSP00000099390; -.
DR GlyConnect; 2361; 1 N-Linked glycan (1 site).
DR GlyGen; Q8BXQ2; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8BXQ2; -.
DR PhosphoSitePlus; Q8BXQ2; -.
DR SwissPalm; Q8BXQ2; -.
DR EPD; Q8BXQ2; -.
DR MaxQB; Q8BXQ2; -.
DR PaxDb; Q8BXQ2; -.
DR PRIDE; Q8BXQ2; -.
DR ProteomicsDB; 288158; -.
DR Antibodypedia; 27619; 154 antibodies from 24 providers.
DR DNASU; 78928; -.
DR Ensembl; ENSMUST00000103101; ENSMUSP00000099390; ENSMUSG00000017721.
DR GeneID; 78928; -.
DR KEGG; mmu:78928; -.
DR UCSC; uc008nvc.1; mouse.
DR CTD; 51604; -.
DR MGI; MGI:1926178; Pigt.
DR VEuPathDB; HostDB:ENSMUSG00000017721; -.
DR eggNOG; KOG2407; Eukaryota.
DR GeneTree; ENSGT00390000018558; -.
DR HOGENOM; CLU_021459_2_0_1; -.
DR InParanoid; Q8BXQ2; -.
DR OMA; LWAWIDA; -.
DR OrthoDB; 887370at2759; -.
DR PhylomeDB; Q8BXQ2; -.
DR TreeFam; TF105921; -.
DR Reactome; R-MMU-162791; Attachment of GPI anchor to uPAR.
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 78928; 10 hits in 73 CRISPR screens.
DR ChiTaRS; Pigt; mouse.
DR PRO; PR:Q8BXQ2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BXQ2; protein.
DR Bgee; ENSMUSG00000017721; Expressed in embryonic brain and 94 other tissues.
DR ExpressionAtlas; Q8BXQ2; baseline and differential.
DR Genevisible; Q8BXQ2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IDA:UniProtKB.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IMP:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IDA:MGI.
DR InterPro; IPR007245; PIG-T.
DR PANTHER; PTHR12959; PTHR12959; 1.
DR Pfam; PF04113; Gpi16; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..582
FT /note="GPI transamidase component PIG-T"
FT /id="PRO_0000024108"
FT TOPO_DOM 26..525
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 186
FT /note="Interchain (with C-92 in PIGK/GPI8)"
FT /evidence="ECO:0000250"
FT CONFLICT 346
FT /note="P -> Q (in Ref. 1; BAC31951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 65705 MW; 39FF3CF98D3F9322 CRC64;
MAAAMPLGLP LRLLVLLLVG RGCCGCAEGP RDSLREELVI TPLPSGDVAA TFQFRTRWDS
DLQREGVSHY RLFPKALGQL ISKYSLRELH LSFTQGFWRT RYWGPPFLQA PSGAELWVWF
QDTVTDVDKS WRELSNVLSG IFCASLNFID ATNTVTPTAS FKPLGLANDT DDYFLRYAVL
PREVVCTENL TPWKKLLPCS SKAGLSVLLK ADRLFHTSYH SQAVHIRPIC RNAHCTSISW
ELRQTLSVVF DAFITGQGKK DWSLFRMFSR TLTEACPLAS QSLVYVDITG YSQDNETLEV
SPPPTSTYQD VILGTRKTYA VYDLFDTAMI NNSRNLNIQL KWKRPPDNEA LPVPFLHAQR
YVSGYGLQKG ELSTLLYNSH PYRAFPVLLL DVVPWYLRLY VHTLTITSKG KENKPSYIHY
QPAQDRQQPH LLEMLIQLPA NSVTKVSIQF ERALLKWTEY TPDPNHGFYV SPSVLSALVP
SVVAAKPVDW EGSPLFNTLF PVSDGSSYFV RLYTEPLLVN LPTPDFSMPY NVICLTCTVV
AVCYGSFYNL LTRTFHIEEP KSGGLAKRLA NLIRRARGVP PL
