GMPPA_MOUSE
ID GMPPA_MOUSE Reviewed; 420 AA.
AC Q922H4; Q3UCM2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Mannose-1-phosphate guanyltransferase alpha;
DE AltName: Full=GDP-mannose pyrophosphorylase A;
DE AltName: Full=GTP-mannose-1-phosphate guanylyltransferase alpha;
GN Name=Gmppa;
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; TISSUE=Bone marrow;
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 MRNA].
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and 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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=24035193; DOI=10.1016/j.ajhg.2013.08.002;
RA Koehler K., Malik M., Mahmood S., Giesselmann S., Beetz C., Hennings J.C.,
RA Huebner A.K., Grahn A., Reunert J., Nurnberg G., Thiele H., Altmuller J.,
RA Nurnberg P., Mumtaz R., Babovic-Vuksanovic D., Basel-Vanagaite L.,
RA Borck G., Bramswig J., Muhlenberg R., Sarda P., Sikiric A.,
RA Anyane-Yeboa K., Zeharia A., Ahmad A., Coubes C., Wada Y., Marquardt T.,
RA Vanderschaeghe D., Van Schaftingen E., Kurth I., Huebner A., Hubner C.A.;
RT "Mutations in GMPPA cause a glycosylation disorder characterized by
RT intellectual disability and autonomic dysfunction.";
RL Am. J. Hum. Genet. 93:727-734(2013).
CC -!- FUNCTION: May serve as a regulatory subunit and allow allosteric
CC feedback inhibition of GMPPB by GDP-mannose. {ECO:0000250}.
CC -!- SUBUNIT: Associates with GMPPB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:24035193}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC {ECO:0000305}.
CC -!- CAUTION: GMPPA is a close homolog of GMPPB, that has been shown to
CC catalyze the formation of GDP-mannose, an essential precursor of glycan
CC moieties of glycoproteins and glycolipids. It has been hypothesized
CC that GMPPA might serve as a regulatory subunit and allow allosteric
CC feedback inhibition of GMPPB by GDP-mannose. Alignment of GMPPAs and
CC GMPPBs from various species shows that GMPPAs are characterized by a 2
CC amino acid-insertion (residues 11-12) in a highly conserved motif that
CC borders the catalytic pocket and binds the nucleotide substrate in
CC homologous enzymes. This insertion might inactivate the ancestral
CC catalytic site, converting it to an allosteric site (PubMed:24035193).
CC {ECO:0000305|PubMed:24035193}.
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DR EMBL; AK150473; BAE29590.1; -; mRNA.
DR EMBL; BC008116; AAH08116.1; -; mRNA.
DR CCDS; CCDS15072.1; -.
DR RefSeq; NP_598469.1; NM_133708.3.
DR RefSeq; XP_006496599.1; XM_006496536.1.
DR RefSeq; XP_006496600.1; XM_006496537.2.
DR RefSeq; XP_006496601.1; XM_006496538.1.
DR AlphaFoldDB; Q922H4; -.
DR SMR; Q922H4; -.
DR BioGRID; 213216; 4.
DR STRING; 10090.ENSMUSP00000035564; -.
DR iPTMnet; Q922H4; -.
DR PhosphoSitePlus; Q922H4; -.
DR SwissPalm; Q922H4; -.
DR EPD; Q922H4; -.
DR jPOST; Q922H4; -.
DR MaxQB; Q922H4; -.
DR PaxDb; Q922H4; -.
DR PRIDE; Q922H4; -.
DR ProteomicsDB; 271407; -.
DR Antibodypedia; 34335; 131 antibodies from 23 providers.
DR DNASU; 69080; -.
DR Ensembl; ENSMUST00000037796; ENSMUSP00000035564; ENSMUSG00000033021.
DR Ensembl; ENSMUST00000113584; ENSMUSP00000109214; ENSMUSG00000033021.
DR GeneID; 69080; -.
DR KEGG; mmu:69080; -.
DR UCSC; uc007bpd.1; mouse.
DR CTD; 29926; -.
DR MGI; MGI:1916330; Gmppa.
DR VEuPathDB; HostDB:ENSMUSG00000033021; -.
DR eggNOG; KOG1460; Eukaryota.
DR GeneTree; ENSGT00940000157018; -.
DR HOGENOM; CLU_029499_3_0_1; -.
DR InParanoid; Q922H4; -.
DR OMA; MPVPNWW; -.
DR OrthoDB; 806744at2759; -.
DR PhylomeDB; Q922H4; -.
DR TreeFam; TF300832; -.
DR BioGRID-ORCS; 69080; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Gmppa; mouse.
DR PRO; PR:Q922H4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q922H4; protein.
DR Bgee; ENSMUSG00000033021; Expressed in saccule of membranous labyrinth and 255 other tissues.
DR ExpressionAtlas; Q922H4; baseline and differential.
DR Genevisible; Q922H4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..420
FT /note="Mannose-1-phosphate guanyltransferase alpha"
FT /id="PRO_0000327873"
FT CONFLICT 23
FT /note="E -> V (in Ref. 1; BAE29590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46244 MW; 31D8581EA51B2F60 CRC64;
MLKAVILIGG PQKGTRFRPL SFEVPKPLFP VAGVPMIQHH IEACAQVPGM QEILLIGFYQ
PDEALTQFLE AAQQEFNLPV RYLQEFAPLG TGGGLYHFRD QILAGAPEAF FVLNADVCSD
FPLSAMLEAH RRQRHPFLLL GTTANRTQSL NYGCIVENPQ THEVLHYVEK PSTFISDIIN
CGIYLFSPEA LKPLRDVFQR NQQDGQLEES PGSWPGAGTI RLEQDVFSAL AGQGQIYVHL
TDGIWSQIKS AGSALYASRL YLGRYQITHP ERLARHTPGG PRIRGNVYIH PTAKVAPSAV
LGPNVSIGKG VTIGEGVRLR ESIVLHGATL QEHTCVLHSI VGWGSTVGRW ARVEGTPNDP
NPNDPRARMD SESLFKDGKL LPAITILGCR VRIPAEVLIL NSIVLPHKEL SRSFTNQIIL
