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IPPK_RAT
ID   IPPK_RAT                Reviewed;         489 AA.
AC   Q5PXE9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Inositol-pentakisphosphate 2-kinase;
DE            EC=2.7.1.158;
DE   AltName: Full=Inositol-1,3,4,5,6-pentakisphosphate 2-kinase;
DE   AltName: Full=Ins(1,3,4,5,6)P5 2-kinase;
DE            Short=InsP5 2-kinase;
DE            Short=rIPK1;
GN   Name=Ippk;
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 [MRNA], FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15528195; DOI=10.1074/jbc.m412006200;
RA   Fujii M., York J.D.;
RT   "A role for rat inositol polyphosphate kinases, rIpk2 and rIpk1, in
RT   inositol pentakisphosphate and inositol hexakisphosphate production in Rat-
RT   1 cells.";
RL   J. Biol. Chem. 280:1156-1164(2005).
CC   -!- FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form
CC       Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many
CC       processes such as mRNA export, non-homologous end-joining, endocytosis,
CC       ion channel regulation. It also protects cells from TNF-alpha-induced
CC       apoptosis. {ECO:0000269|PubMed:15528195}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-
CC         inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC         ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158;
CC         Evidence={ECO:0000269|PubMed:15528195};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15528195}. Nucleus
CC       {ECO:0000305|PubMed:15528195}.
CC   -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC       kinases of both family 1 and 2.
CC   -!- SIMILARITY: Belongs to the IPK1 type 2 family. {ECO:0000305}.
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DR   EMBL; AY823319; AAV76010.1; -; mRNA.
DR   RefSeq; NP_001008556.1; NM_001008556.1.
DR   AlphaFoldDB; Q5PXE9; -.
DR   SMR; Q5PXE9; -.
DR   STRING; 10116.ENSRNOP00000021022; -.
DR   PaxDb; Q5PXE9; -.
DR   GeneID; 306808; -.
DR   KEGG; rno:306808; -.
DR   CTD; 64768; -.
DR   RGD; 1311271; Ippk.
DR   eggNOG; KOG4749; Eukaryota.
DR   InParanoid; Q5PXE9; -.
DR   OrthoDB; 1195478at2759; -.
DR   PhylomeDB; Q5PXE9; -.
DR   BRENDA; 2.7.1.158; 5301.
DR   Reactome; R-RNO-1855167; Synthesis of pyrophosphates in the cytosol.
DR   Reactome; R-RNO-1855191; Synthesis of IPs in the nucleus.
DR   PRO; PR:Q5PXE9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; ISS:HGNC-UCL.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0052746; P:inositol phosphorylation; ISS:BHF-UCL.
DR   GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:RGD.
DR   Gene3D; 3.30.200.110; -; 1.
DR   InterPro; IPR009286; Ins_P5_2-kin.
DR   InterPro; IPR043001; IP5_2-K_N_lobe.
DR   PANTHER; PTHR14456; PTHR14456; 1.
DR   Pfam; PF06090; Ins_P5_2-kin; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..489
FT                   /note="Inositol-pentakisphosphate 2-kinase"
FT                   /id="PRO_0000110531"
FT   MOTIF           136..140
FT                   /note="EXKPK motif"
SQ   SEQUENCE   489 AA;  55634 MW;  4C710CBA57BFA215 CRC64;
     MEEGKMDENE WSYHGEGNKS LVVAHAQRCV VLRFLKFPPN KKKTSEEILQ HLQNIVDFGK
     NVMKDFLGEN YVHCGEVVQL PLEFVKQLCL KIQCERPESR CDKDLDTLSG YAMCLPNLTR
     LQTFPFAEHR PILCVEIKPK CGFIPFSNGV THEMKHKVCR YCMHQHLKVA TGKWKKISKY
     CPLDLYSGNK QRMHFALKSL LQEAQNNLRI FKNGELIYGC ADARSPVADL KALAHHLKPF
     FFPSNGLASG PQCTRAVIRE LVHVITRVLL STSDKGRAGA LRLGLQGARV CEASPFSRSL
     HHQGKNTPEH SGLPKGCLLY KTLQVQMLDQ LDIEGLYPLY NRVEQYLEEF PEERKTLQID
     GPYDEVFYQK LLDLSTEDDG TVAFALTKVQ QYRVAMTAKD CSIMIALSPC LQGASSDQRP
     VIPSSRSRLA FSVSVLDLDL KPYESIPHQY KLDSKIVSYY SKTVHAKDDT VRSTRFKEHE
     DCTLVLHKV
 
 
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