ID   GMPPA_RAT               Reviewed;         420 AA.
AC   Q5XIC1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 117.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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: 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   -!- 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. {ECO:0000305}.
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DR   EMBL; BC083763; AAH83763.1; -; mRNA.
DR   RefSeq; NP_001020227.1; NM_001025056.1.
DR   RefSeq; XP_006245333.1; XM_006245271.2.
DR   AlphaFoldDB; Q5XIC1; -.
DR   SMR; Q5XIC1; -.
DR   BioGRID; 272474; 1.
DR   STRING; 10116.ENSRNOP00000027064; -.
DR   jPOST; Q5XIC1; -.
DR   PaxDb; Q5XIC1; -.
DR   PRIDE; Q5XIC1; -.
DR   Ensembl; ENSRNOT00000027064; ENSRNOP00000027064; ENSRNOG00000019946.
DR   GeneID; 501167; -.
DR   KEGG; rno:501167; -.
DR   UCSC; RGD:1560644; rat.
DR   CTD; 29926; -.
DR   RGD; 1560644; Gmppa.
DR   eggNOG; KOG1460; Eukaryota.
DR   GeneTree; ENSGT00940000157018; -.
DR   HOGENOM; CLU_029499_3_0_1; -.
DR   InParanoid; Q5XIC1; -.
DR   PhylomeDB; Q5XIC1; -.
DR   TreeFam; TF300832; -.
DR   PRO; PR:Q5XIC1; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000019946; Expressed in pancreas and 20 other tissues.
DR   ExpressionAtlas; Q5XIC1; baseline and differential.
DR   Genevisible; Q5XIC1; RN.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase activity; TAS:Reactome.
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   2: Evidence at transcript level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..420
FT                   /note="Mannose-1-phosphate guanyltransferase alpha"
FT                   /id="PRO_0000327875"
SQ   SEQUENCE   420 AA;  46191 MW;  4433A234E92BA083 CRC64;
     MLKAVILIGG PQKGTRFRPL SFEVPKPLFP VAGVPMIQHH IEACAQVPGM QEILLIGFYQ
     PDEALTQFLE AAQQEFNLPV RYLQEFTPLG TGGGLYHFRD QILAGAPEAF FVLNADVCSD
     FPLSAMLDAH RLQRHPFLLL GTTANRTQSL NYGCIVENPQ THEVLHYVEK PSTFISDIIN
     CGIYLFSPEA LKPLRDVFQR NQQDGQLEES PGSWPGAGTI RLEQDVFSAL AGQGQIYVHL
     TDGIWSQIKS AGSALYASRL YLGRYQITHP ERLARHTAGG PRIRGNVYIH PTAKVAPSAV
     LGPNVSIGKG VTIGEGVRLR ESIVLHGATL QEHTCVLHSI VGWGSTVGRW ARVEGTPNDP
     NPNDPRARMD SESLFKDGKL LPAITILGCR VRIPAEVLIL NSIVLPHKEL SRSFTNQIIL