ID   PIM3_XENLA              Reviewed;         323 AA.
AC   Q91822;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Serine/threonine-protein kinase pim-3;
DE            EC=2.7.11.1;
DE   AltName: Full=Pim-1;
GN   Name=pim3; Synonyms=pim1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT SER-4; SER-190 AND
RP   THR-205.
RX   PubMed=9099695; DOI=10.1074/jbc.272.16.10514;
RA   Palaty C.K., Kalmar G., Tai G., Oh S., Amankawa L., Affolter M.,
RA   Aebersold R., Pelech S.L.;
RT   "Identification of the autophosphorylation sites of the Xenopus laevis Pim-
RT   1 proto-oncogene-encoded protein kinase.";
RL   J. Biol. Chem. 272:10514-10521(1997).
CC   -!- FUNCTION: Proto-oncogene with serine/threonine kinase activity that can
CC       prevent apoptosis and promote cell survival and protein translation.
CC       {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:9099695}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. PIM subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was originally called Pim-1 but seems to represent the protein
CC       pim3. {ECO:0000305|PubMed:9099695}.
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; L29495; AAA85389.1; -; mRNA.
DR   RefSeq; NP_001081037.1; NM_001087568.1.
DR   AlphaFoldDB; Q91822; -.
DR   SMR; Q91822; -.
DR   iPTMnet; Q91822; -.
DR   GeneID; 394343; -.
DR   KEGG; xla:394343; -.
DR   CTD; 394343; -.
DR   Xenbase; XB-GENE-17343708; pim3.S.
DR   OrthoDB; 930292at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 394343; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017348; PIM1/2/3.
DR   InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Proto-oncogene; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..323
FT                   /note="Serine/threonine-protein kinase pim-3"
FT                   /id="PRO_0000086537"
FT   DOMAIN          40..291
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        168
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"
FT   MOD_RES         4
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:9099695"
FT   MOD_RES         190
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:9099695"
FT   MOD_RES         205
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:9099695"
SQ   SEQUENCE   323 AA;  36964 MW;  AB4DD61E7A99A38F CRC64;
     MLLSKFGSLA HICNPSNMEH LPVKILQPVK VDKEPFEKVY QVGSVVASGG FGTVYSDSRI
     ADGQPVAVKH VAKERVTEWG TLNGVMVPLE IVLLKKVPTA FRGVINLLDW YERPDAFLIV
     MERPEPVKDL FDYITEKGPL DEDTARGFFR QVLEAVRHCY NCGVVHRDIK DENLLVDTRN
     GELKLIDFGS GALLKDTVYT DFDGTRVYSP PEWVRYHRYH GRSATVWSLG VLLYDMVYGD
     IPFEQDEEIV RVRLCFRRRI STECQQLIKW CLSLRPSDRP TLEQIFDHPW MCKCDLVKSE
     DCDLRLRTID NDSSSTSSSN ESL