PIM3_RAT
ID PIM3_RAT Reviewed; 326 AA.
AC O70444;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Serine/threonine-protein kinase pim-3;
DE EC=2.7.11.1;
DE AltName: Full=Kinase induced by depolarization;
DE AltName: Full=Protein kinase Kid-1;
GN Name=Pim3; Synonyms=Kid1;
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].
RC STRAIN=Sprague-Dawley;
RA Konietzko U., Kuhl D.;
RT "Pim-3 is a member of the pim kinase family.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY, AND
RP AUTOPHOSPHORYLATION.
RX PubMed=9632723; DOI=10.1074/jbc.273.26.16535;
RA Feldman J.D., Vician L., Crispino M., Tocco G., Marcheselli V.L.,
RA Bazan N.G., Baudry M., Herschman H.R.;
RT "KID-1, a protein kinase induced by depolarization in brain.";
RL J. Biol. Chem. 273:16535-16543(1998).
CC -!- FUNCTION: Proto-oncogene with serine/threonine kinase activity that can
CC prevent apoptosis and promote cell survival and protein translation.
CC May contribute to tumorigenesis through: the delivery of survival
CC signaling through phosphorylation of BAD which induces release of the
CC anti-apoptotic protein Bcl-X(L), the regulation of cell cycle
CC progression and protein synthesis and by regulation of MYC
CC transcriptional activity. Additionally to this role on tumorigenesis,
CC can also negatively regulate insulin secretion by inhibiting the
CC activation of MAPK1/3 (ERK1/2), through SOCS6. Involved also in the
CC control of energy metabolism and regulation of AMPK activity in
CC modulating MYC and PPARGC1A protein levels and cell growth (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with BAD. Interacts with PPP2CA; this interaction
CC promotes dephosphorylation of PIM3, ubiquitination and proteasomal
CC degradation. Interacts with SOCS6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in various tissues, including brain.
CC {ECO:0000269|PubMed:9632723}.
CC -!- INDUCTION: By membrane depolarization or forskolin.
CC {ECO:0000269|PubMed:9632723}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Interaction with PPP2CA promotes dephosphorylation
CC (By similarity). Autophosphorylated (in vitro). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PIM subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC68900.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF086624; AAC68900.1; ALT_INIT; mRNA.
DR EMBL; AF057026; AAC36065.1; -; mRNA.
DR RefSeq; NP_072124.1; NM_022602.1.
DR AlphaFoldDB; O70444; -.
DR SMR; O70444; -.
DR STRING; 10116.ENSRNOP00000045396; -.
DR BindingDB; O70444; -.
DR ChEMBL; CHEMBL3638335; -.
DR PhosphoSitePlus; O70444; -.
DR PaxDb; O70444; -.
DR Ensembl; ENSRNOT00000043461; ENSRNOP00000045396; ENSRNOG00000029698.
DR GeneID; 64534; -.
DR KEGG; rno:64534; -.
DR CTD; 415116; -.
DR RGD; 620462; Pim3.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000153394; -.
DR InParanoid; O70444; -.
DR OrthoDB; 930292at2759; -.
DR PhylomeDB; O70444; -.
DR PRO; PR:O70444; -.
DR Proteomes; UP000002494; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016572; P:histone phosphorylation; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017348; PIM1/2/3.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037993; STPK_Pim-1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cell cycle; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Proto-oncogene; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..326
FT /note="Serine/threonine-protein kinase pim-3"
FT /id="PRO_0000086535"
FT DOMAIN 40..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 326 AA; 36002 MW; DD6C9BF4635F851E CRC64;
MLLSKFGSLA HLCGPGGVDH LPVKILQPAK ADKESFEKVY QVGAVLGSGG FGTVYAGSRI
ADGLPVAVKH VVKERVTEWG SLGGMAVPLE VVLLRKVGAA GGARGVIRLL DWFERPDGFL
LVLERPEPAQ DLFDFITERG ALDEPLARRF FAQVLAAVRH CHNCGVVHRD IKDENLLVDL
RSGELKLIDF GSGAVLKDTV YTDFDGTRVY SPPEWIRYHR YHGRSATVWS LGVLLYDMVC
GDIPFEQDEE ILRGRLFFRR RVSPECQQLI EWCLSLRPSE RPSLDQIAAH PWMLGTEGSV
PENCDLRLCA LDTDDGASTT SSSESL
