MPI_MOUSE
ID MPI_MOUSE Reviewed; 423 AA.
AC Q924M7;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Mannose-6-phosphate isomerase;
DE EC=5.3.1.8;
DE AltName: Full=Phosphohexomutase;
DE AltName: Full=Phosphomannose isomerase;
DE Short=PMI;
GN Name=Mpi; Synonyms=Mpi1, Pmi;
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 [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=12122025; DOI=10.1093/glycob/cwf060;
RA Davis J.A., Wu X.H., Wang L., DeRossi C., Westphal V., Wu R., Alton G.,
RA Srikrishna G., Freeze H.H.;
RT "Molecular cloning, gene organization, and expression of mouse Mpi encoding
RT phosphomannose isomerase.";
RL Glycobiology 12:435-442(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Involved in the synthesis of the GDP-mannose and dolichol-
CC phosphate-mannose required for a number of critical mannosyl transfer
CC reactions. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC EC=5.3.1.8;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12122025}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF244360; AAK69388.1; -; mRNA.
DR EMBL; BC051163; AAH51163.1; -; mRNA.
DR CCDS; CCDS40650.1; -.
DR RefSeq; NP_080113.1; NM_025837.2.
DR AlphaFoldDB; Q924M7; -.
DR SMR; Q924M7; -.
DR BioGRID; 225310; 1.
DR IntAct; Q924M7; 1.
DR MINT; Q924M7; -.
DR STRING; 10090.ENSMUSP00000034856; -.
DR iPTMnet; Q924M7; -.
DR PhosphoSitePlus; Q924M7; -.
DR REPRODUCTION-2DPAGE; Q924M7; -.
DR EPD; Q924M7; -.
DR jPOST; Q924M7; -.
DR MaxQB; Q924M7; -.
DR PaxDb; Q924M7; -.
DR PRIDE; Q924M7; -.
DR ProteomicsDB; 291487; -.
DR Antibodypedia; 2008; 414 antibodies from 32 providers.
DR Ensembl; ENSMUST00000034856; ENSMUSP00000034856; ENSMUSG00000032306.
DR GeneID; 110119; -.
DR KEGG; mmu:110119; -.
DR UCSC; uc009pvd.1; mouse.
DR CTD; 4351; -.
DR MGI; MGI:97075; Mpi.
DR VEuPathDB; HostDB:ENSMUSG00000032306; -.
DR eggNOG; KOG2757; Eukaryota.
DR GeneTree; ENSGT00390000016075; -.
DR HOGENOM; CLU_026967_2_0_1; -.
DR InParanoid; Q924M7; -.
DR OMA; DIGLFCG; -.
DR OrthoDB; 1043197at2759; -.
DR PhylomeDB; Q924M7; -.
DR TreeFam; TF312831; -.
DR Reactome; R-MMU-446205; Synthesis of GDP-mannose.
DR UniPathway; UPA00126; UER00423.
DR BioGRID-ORCS; 110119; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Mpi; mouse.
DR PRO; PR:Q924M7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q924M7; protein.
DR Bgee; ENSMUSG00000032306; Expressed in spermatocyte and 239 other tissues.
DR ExpressionAtlas; Q924M7; baseline and differential.
DR Genevisible; Q924M7; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IMP:MGI.
DR GO; GO:0061619; P:glycolytic process from mannose through fructose-6-phosphate; IC:MGI.
DR GO; GO:0061611; P:mannose to fructose-6-phosphate metabolic process; IMP:MGI.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR001250; Man6P_Isoase-1.
DR InterPro; IPR016305; Mannose-6-P_Isomerase.
DR InterPro; IPR018050; Pmannose_isomerase-type1_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR10309; PTHR10309; 1.
DR Pfam; PF01238; PMI_typeI; 1.
DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1.
DR PRINTS; PR00714; MAN6PISMRASE.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR00218; manA; 1.
DR PROSITE; PS00965; PMI_I_1; 1.
DR PROSITE; PS00966; PMI_I_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isomerase; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P34949"
FT CHAIN 2..423
FT /note="Mannose-6-phosphate isomerase"
FT /id="PRO_0000194237"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P34949"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34949"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34949"
SQ SEQUENCE 423 AA; 46575 MW; 3A49506D1249B670 CRC64;
MASPRVFPLS CVVQQYAWGK VGSKSEVACL LASSDPLAQI SEDKPYAELW MGTHPRGDAK
ILDNRISQKT LGQWIAENPD CLGSKVKNTF NGKLPFLFKV LSVDTALSIQ AHPNKELAEK
LHLQAPEHYP DANHKPEMAI ALTSFQGLCG FRPVEEIVTF MKKVPEFQLL IGDDATAQLK
ESVGGDTEAM ASALRNCFSH LMKSEKKVVV EQLNLLVKRI SQQVFDGNNM EDIYGKLLLQ
LHQQHPGDIG CFAIYFLNLL TLKPGEAMFL DANVPHAYLK GDCVECMACS DNTVRAGLTP
KFIDVPTLCE MLNYTPSPSN NRLFAPAQSQ DDPYLSIYDP PVPDFTVMKM EVPSSVTEYK
VSTLDSASIL LMVQGTVTAI IPSAHAEIPL YRGGVLFIAA NESVLLKITV PKDLLIFRAC
CLL
