ID   PDPK2_HUMAN             Reviewed;         396 AA.
AC   Q6A1A2;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   08-NOV-2023, entry version 128.
DE   RecName: Full=Putative 3-phosphoinositide-dependent protein kinase 2;
DE            EC=2.7.11.1;
DE   AltName: Full=3-phosphoinositide-dependent protein kinase 2 pseudogene {ECO:0000305};
GN   Name=PDPK2P {ECO:0000312|HGNC:HGNC:49897};
GN   Synonyms=PDPK2 {ECO:0000303|Ref.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Pingzhang W., Xin W., Tianjing C., Jun W., Ying L.;
RT   "A novel member of human 3-phosphoinositide dependent protein kinase-1
RT   family, PDPK2.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylates and activates not only PKB/AKT, but also PKA,
CC       PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling
CC       processes and in development (By 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The PIF-pocket is a small lobe in the catalytic domain required
CC       by the enzyme for the binding to the hydrophobic motif of its
CC       substrates. It is an allosteric regulatory site that can accommodate
CC       small compounds acting as allosteric inhibitors.
CC       {ECO:0000250|UniProtKB:O15530}.
CC   -!- PTM: Phosphorylated on tyrosine and serine/threonine. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PDPK1 subfamily. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR   EMBL; AJ785968; CAH05056.1; -; mRNA.
DR   AlphaFoldDB; Q6A1A2; -.
DR   SMR; Q6A1A2; -.
DR   IntAct; Q6A1A2; 1.
DR   GlyCosmos; Q6A1A2; 1 site, 1 glycan.
DR   GlyGen; Q6A1A2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6A1A2; -.
DR   BioMuta; HGNC:49897; -.
DR   DMDM; 74757401; -.
DR   jPOST; Q6A1A2; -.
DR   MassIVE; Q6A1A2; -.
DR   MaxQB; Q6A1A2; -.
DR   PeptideAtlas; Q6A1A2; -.
DR   Pumba; Q6A1A2; -.
DR   AGR; HGNC:49897; -.
DR   GeneCards; PDPK2P; -.
DR   HGNC; HGNC:49897; PDPK2P.
DR   neXtProt; NX_Q6A1A2; -.
DR   InParanoid; Q6A1A2; -.
DR   PhylomeDB; Q6A1A2; -.
DR   SignaLink; Q6A1A2; -.
DR   SIGNOR; Q6A1A2; -.
DR   ChiTaRS; PDPK2P; human.
DR   Pharos; Q6A1A2; Tdark.
DR   PRO; PR:Q6A1A2; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q6A1A2; Protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; 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; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05581; STKc_PDK1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR039046; PDPK1.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24356:SF163; 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1-RELATED; 1.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   5: Uncertain;
KW   ATP-binding; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..396
FT                   /note="Putative 3-phosphoinositide-dependent protein kinase
FT                   2"
FT                   /id="PRO_0000341967"
FT   DOMAIN          55..315
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..130
FT                   /note="PIF-pocket"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         65..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         133..135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
SQ   SEQUENCE   396 AA;  44765 MW;  A0661913B473D8DF CRC64;
     MVRTQTESST PPGIPGGSRQ GPAMDGTAAE PRPGAGSLQH AQPPPQPRKK RPEDFKFGKI
     LGEGSFSTVV LARELATSRE YAIKILEKRH IIKENKVPYV TRERDVMSRL DHPFFVKLYF
     TFQDDEKLYF GLSYAKNGEL LKYIRKIGSF DETCTRFYTA EIVSALEYLH GKGIIHRDLK
     PENILLNEDM YIQITDFGTA KVLSPESKQA RANSFVGTAQ YVSPELLTEK SACKSSDLWA
     LGCIIYQLVA GLPPFRAGNE YLIFQKIIKL EYDFPEKFFP KARDLVEKLL VLDATKRLGC
     EEMEGYGPLK AHPFFESVTW ENLHQQTPPK LTAYLPAMSE DDEDCYGNVS WPGWRARQVA
     LGPPCTGLHA RAPDPRVICS RKGRVSVPLR QACWWL
//