ID   MPI_RAT                 Reviewed;         423 AA.
AC   Q68FX1;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 126.
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;
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=Lung;
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: 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:0000250}.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; BC079111; AAH79111.1; -; mRNA.
DR   RefSeq; NP_001004081.1; NM_001004081.1.
DR   AlphaFoldDB; Q68FX1; -.
DR   SMR; Q68FX1; -.
DR   STRING; 10116.ENSRNOP00000025783; -.
DR   iPTMnet; Q68FX1; -.
DR   PhosphoSitePlus; Q68FX1; -.
DR   jPOST; Q68FX1; -.
DR   PaxDb; Q68FX1; -.
DR   PRIDE; Q68FX1; -.
DR   Ensembl; ENSRNOT00000025783; ENSRNOP00000025783; ENSRNOG00000018898.
DR   GeneID; 300741; -.
DR   KEGG; rno:300741; -.
DR   UCSC; RGD:3107; rat.
DR   CTD; 4351; -.
DR   RGD; 3107; Mpi.
DR   eggNOG; KOG2757; Eukaryota.
DR   GeneTree; ENSGT00390000016075; -.
DR   HOGENOM; CLU_026967_2_0_1; -.
DR   InParanoid; Q68FX1; -.
DR   OMA; DIGLFCG; -.
DR   OrthoDB; 1043197at2759; -.
DR   PhylomeDB; Q68FX1; -.
DR   TreeFam; TF312831; -.
DR   Reactome; R-RNO-446205; Synthesis of GDP-mannose.
DR   SABIO-RK; Q68FX1; -.
DR   UniPathway; UPA00126; UER00423.
DR   PRO; PR:Q68FX1; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000018898; Expressed in skeletal muscle tissue and 20 other tissues.
DR   Genevisible; Q68FX1; RN.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; ISO:RGD.
DR   GO; GO:0061611; P:mannose to fructose-6-phosphate metabolic process; ISO:RGD.
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   2: Evidence at transcript 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_0000194238"
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;  46424 MW;  69C6CE365535002B CRC64;
     MANPRVFPLS CVVQQYAWGK VGSKSEVACL LACSDPLTQI SEDKPYAELW MGAHPRGDAK
     ILDNRISQKT LGQWIAENQN SLGQKVKDTF NGKLPFLFKV LSVETALSIQ AHPNKELAEK
     LHLQAPEHYP DANHKPEMAI ALTPFQGLCG FRPVEEIVTF LKKVPEFQSL IGEDATAQLK
     KSMNEGSGAM ASALKNCFSH LMKSEKKVVV EQLNLLVKRI SQQISNGNSM DDICGELLLQ
     LHQQYPGDIG CFAIYLLNLI TLKPGEAMFL EANVPHAYLK GDCVECMACS DNTVRAGLTP
     KFIDVSTLCE MLDYTPSPSK DRLFAPTLSQ DDPYLSIYDP PVPDFTVMKI EVPGSVTEYK
     VLTLDSASIL LLVQGTVTAI IPSVQGEIPL SRGGVLFIGA NETVLLKLTV PKNLLIFRAC
     CLL