GMDS_MOUSE
ID GMDS_MOUSE Reviewed; 372 AA.
AC Q8K0C9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=GDP-mannose 4,6 dehydratase;
DE EC=4.2.1.47 {ECO:0000250|UniProtKB:O60547};
DE AltName: Full=GDP-D-mannose dehydratase;
DE Short=GMD;
GN Name=Gmds;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Salivary gland;
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).
CC -!- FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-
CC deoxy-D-mannose. {ECO:0000250|UniProtKB:O60547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O;
CC Xref=Rhea:RHEA:23820, ChEBI:CHEBI:15377, ChEBI:CHEBI:57527,
CC ChEBI:CHEBI:57964; EC=4.2.1.47;
CC Evidence={ECO:0000250|UniProtKB:O60547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23821;
CC Evidence={ECO:0000250|UniProtKB:O60547};
CC -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC Evidence={ECO:0000250|UniProtKB:O60547};
CC -!- ACTIVITY REGULATION: Inhibited by GDP-fucose.
CC {ECO:0000250|UniProtKB:O60547}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via
CC de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.
CC {ECO:0000250|UniProtKB:O60547}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. GDP-mannose 4,6-dehydratase subfamily. {ECO:0000305}.
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DR EMBL; AL645643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031788; AAH31788.1; -; mRNA.
DR EMBL; BC093502; AAH93502.1; -; mRNA.
DR CCDS; CCDS26426.1; -.
DR RefSeq; NP_666153.1; NM_146041.2.
DR AlphaFoldDB; Q8K0C9; -.
DR SMR; Q8K0C9; -.
DR BioGRID; 229995; 8.
DR IntAct; Q8K0C9; 1.
DR STRING; 10090.ENSMUSP00000036696; -.
DR iPTMnet; Q8K0C9; -.
DR PhosphoSitePlus; Q8K0C9; -.
DR EPD; Q8K0C9; -.
DR MaxQB; Q8K0C9; -.
DR PaxDb; Q8K0C9; -.
DR PeptideAtlas; Q8K0C9; -.
DR PRIDE; Q8K0C9; -.
DR ProteomicsDB; 267731; -.
DR Antibodypedia; 24246; 214 antibodies from 29 providers.
DR DNASU; 218138; -.
DR Ensembl; ENSMUST00000041859; ENSMUSP00000036696; ENSMUSG00000038372.
DR GeneID; 218138; -.
DR KEGG; mmu:218138; -.
DR UCSC; uc007pzq.1; mouse.
DR CTD; 2762; -.
DR MGI; MGI:1891112; Gmds.
DR VEuPathDB; HostDB:ENSMUSG00000038372; -.
DR eggNOG; KOG1372; Eukaryota.
DR GeneTree; ENSGT00440000033640; -.
DR HOGENOM; CLU_007383_14_0_1; -.
DR InParanoid; Q8K0C9; -.
DR OMA; TDCLYLG; -.
DR OrthoDB; 877551at2759; -.
DR PhylomeDB; Q8K0C9; -.
DR TreeFam; TF300682; -.
DR Reactome; R-MMU-6787639; GDP-fucose biosynthesis.
DR UniPathway; UPA00128; UER00190.
DR BioGRID-ORCS; 218138; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Gmds; mouse.
DR PRO; PR:Q8K0C9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8K0C9; protein.
DR Bgee; ENSMUSG00000038372; Expressed in paneth cell and 237 other tissues.
DR ExpressionAtlas; Q8K0C9; baseline and differential.
DR Genevisible; Q8K0C9; MM.
DR GO; GO:0008446; F:GDP-mannose 4,6-dehydratase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0070401; F:NADP+ binding; ISS:UniProtKB.
DR GO; GO:0042351; P:'de novo' GDP-L-fucose biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019673; P:GDP-mannose metabolic process; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; ISS:UniProtKB.
DR HAMAP; MF_00955; GDP_Man_dehydratase; 1.
DR InterPro; IPR006368; GDP_Man_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43715; PTHR43715; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01472; gmd; 1.
PE 1: Evidence at protein level;
KW Acetylation; Lyase; NADP; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT CHAIN 2..372
FT /note="GDP-mannose 4,6 dehydratase"
FT /id="PRO_0000201706"
FT ACT_SITE 155
FT /evidence="ECO:0000250"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 179
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 30..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 55..58
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 86..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 108..112
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 123
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 209
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O60547"
FT MOD_RES 323
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60547"
SQ SEQUENCE 372 AA; 41985 MW; A53918200F1F4CE2 CRC64;
MAQAPAKCPS YPGSGDGEMG KLRKVALITG ITGQDGSYLA EFLLEKGYEV HGIVRRSSSF
NTGRIEHLYK NPQAHIEGNM KLHYGDLTDS TCLVKIINEV KPTEIYNLGA QSHVKISFDL
AEYTADVDGV GTLRLLDAIK TCGLINSVKF YQASTSELYG KVQEIPQKET TPFYPRSPYG
AAKLYAYWIV VNFREAYNLF AVNGILFNHE SPRRGANFVT RKISRSVAKI YLGQLECFSL
GNLDAKRDWG HAKDYVEAMW LMLQNDEPED FVIATGEVHS VREFVEKSFM HIGKTIVWEG
KNENEVGRCK ETGKVHVTVD LKYYRPTEVD FLQGDCSKAQ QKLNWKPRVA FDELVREMVQ
ADVELMRTNP NA
