ID   GMPPA_PIG               Reviewed;         420 AA.
AC   I3LUP1;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 2.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Mannose-1-phosphate guanyltransferase alpha;
DE   AltName: Full=GDP-mannose pyrophosphorylase 43-kDa subunit;
DE   AltName: Full=GDP-mannose pyrophosphorylase A;
DE            Short=GMPP-alpha;
DE   AltName: Full=GTP-mannose-1-phosphate guanylyltransferase alpha;
GN   Name=GMPPA;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver, Ovary, and Uterus;
RX   PubMed=14681463; DOI=10.1093/nar/gkh037;
RA   Uenishi H., Eguchi T., Suzuki K., Sawazaki T., Toki D., Shinkai H.,
RA   Okumura N., Hamasima N., Awata T.;
RT   "PEDE (Pig EST Data Explorer): construction of a database for ESTs derived
RT   from porcine full-length cDNA libraries.";
RL   Nucleic Acids Res. 32:D484-D488(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 127-139, INTERACTION WITH GMPPB, TISSUE SPECIFICITY,
RP   AND BLOCKAGE OF N-TERMINUS.
RC   TISSUE=Liver;
RX   PubMed=7688733; DOI=10.1016/s0021-9258(17)46796-2;
RA   Szumilo T., Drake R.R., York J.L., Elbein A.D.;
RT   "GDP-mannose pyrophosphorylase. Purification to homogeneity, properties,
RT   and utilization to prepare photoaffinity analogs.";
RL   J. Biol. Chem. 268:17943-17950(1993).
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 (in vivo).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the liver (at protein level).
CC       {ECO:0000269|PubMed:7688733}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       {ECO:0000305}.
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DR   EMBL; AK232621; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK239909; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK395123; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; FP565246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; I3LUP1; -.
DR   SMR; I3LUP1; -.
DR   STRING; 9823.ENSSSCP00000027841; -.
DR   PaxDb; I3LUP1; -.
DR   PeptideAtlas; I3LUP1; -.
DR   eggNOG; KOG1460; Eukaryota.
DR   HOGENOM; CLU_029499_3_0_1; -.
DR   InParanoid; I3LUP1; -.
DR   TreeFam; TF300832; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; I3LUP1; SS.
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; Direct protein sequencing; Reference proteome.
FT   CHAIN           1..420
FT                   /note="Mannose-1-phosphate guanyltransferase alpha"
FT                   /id="PRO_0000425103"
FT   CONFLICT        182
FT                   /note="G -> D (in Ref. 1; AK395123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="T -> A (in Ref. 1; AK232621/AK239909/AK395123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196..197
FT                   /note="KF -> EV (in Ref. 1; AK232621/AK239909/AK395123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="Y -> N (in Ref. 1; AK232621/AK239909/AK395123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="G -> D (in Ref. 1; AK232621/AK239909/AK395123)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        283
FT                   /note="I -> V (in Ref. 1; AK232621)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   420 AA;  46173 MW;  A0A2F43D1650DFB2 CRC64;
     MLKAVILIGG PQKGTRFRPL SFEVPKPLFP VAGVPMIQHH IEACAQVPGM QEILLIGFYQ
     PDEPLTRFLE AAQQEFNLPI RYLQEFAPLG TGGGLYHFRD QILAGGPEAF FVLNADVCSD
     FPLSAMLDAH RHRPHPFLLL GTTANRTQSL NYGCIVENPQ THEVLHYVEK PSTFVSDIIN
     CGIYLFSPET LKPLGKFFQR YQQGGQLEDS SVLWPGAGTI RLEQDVFAAL AGQGQIYVHL
     TDGIWSQIKS AGSALYASRL YLSQYQLTHP ERLAKHTPGG PRIRGNVYIH PTAKVAPSAV
     LGPNVSIGEG VTVGEGVRLR ESIVLHGATL QEHTCVLHSI VGWGSTVGRW ARVEGTPNDP
     NPNDPRAHMD SESLFKDGKL LPAITILGCR VRIPAEVLIL NSIVLPHKEL SRSFTNQIIL