PKN2_DANRE
ID PKN2_DANRE Reviewed; 977 AA.
AC A7MBL8;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Serine/threonine-protein kinase N2;
DE EC=2.7.11.13;
DE AltName: Full=PKN gamma;
DE AltName: Full=Protein kinase C-like 2;
DE AltName: Full=Protein-kinase C-related kinase 2;
GN Name=pkn2; Synonyms=prk2, prkcl2; ORFNames=zgc:153916;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pkc-related serine/threonine-protein kinase and Rho/Rac
CC effector protein that participates in specific signal transduction
CC responses in the cell. May play a role in the regulation of cell cycle
CC progression, actin cytoskeleton assembly, cell migration, cell adhesion
CC and transcription activation signaling processes (By similarity).
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=2.7.11.13;
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=2.7.11.13;
CC -!- ACTIVITY REGULATION: Kinase activity is activated upon binding to GTP-
CC bound Rho/Rac GTPases. Activated by lipids, particularly cardiolipin
CC and to a lesser extent by other acidic phospholipids and unsaturated
CC fatty acids. Two specific sites, Thr-809 (activation loop of the kinase
CC domain) and Thr-951 (turn motif), may be needed to be phosphorylated
CC for its full activation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cleavage furrow {ECO:0000250}.
CC Midbody {ECO:0000250}. Cell junction {ECO:0000250}.
CC -!- PTM: Autophosphorylated. Phosphorylated. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; BC151829; AAI51830.1; -; mRNA.
DR RefSeq; NP_001277108.1; NM_001290179.1.
DR AlphaFoldDB; A7MBL8; -.
DR SMR; A7MBL8; -.
DR STRING; 7955.ENSDARP00000100346; -.
DR PaxDb; A7MBL8; -.
DR PeptideAtlas; A7MBL8; -.
DR PRIDE; A7MBL8; -.
DR GeneID; 567134; -.
DR KEGG; dre:567134; -.
DR CTD; 567134; -.
DR ZFIN; ZDB-GENE-061013-393; pkn2b.
DR eggNOG; KOG0694; Eukaryota.
DR InParanoid; A7MBL8; -.
DR OrthoDB; 520651at2759; -.
DR PhylomeDB; A7MBL8; -.
DR Reactome; R-DRE-5625740; RHO GTPases activate PKNs.
DR Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR Reactome; R-DRE-9013106; RHOC GTPase cycle.
DR Reactome; R-DRE-9013149; RAC1 GTPase cycle.
DR PRO; PR:A7MBL8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11622; HR1_PKN_1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037784; C2_PKN.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 3.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 3.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell adhesion; Cell cycle; Cell division; Cell junction;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..977
FT /note="Serine/threonine-protein kinase N2"
FT /id="PRO_0000415276"
FT DOMAIN 24..100
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 114..194
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 200..280
FT /note="REM-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 298..468
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 650..909
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 910..977
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 342..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 775
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 656..664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 977 AA; 110657 MW; 612AD83A4269DAC6 CRC64;
MAADSVQNDA RGPMVSGRLD FDQNLDFSDT MVQKNLDEIK DQIKREIRKE LKIKEGAENL
RKVTTDKKSL AYVDNMLKKS NKKVEELHQE LQELNAHIVV KDPEEVEEYP LTPDTPKSET
RMSTNSNRLA ALKKQADIEL KVKQGAEDMI QMYSNGSSKD RKLLAAAQQM LQDSKTKIEF
IRMQILKASQ TSEINYENND VTTSKPIISP LDLRIEELRH HYRIESAVAD GAKNVMKLLG
TGKVTEKKAH SEAQARLNES SQKLDLLKFS LEQRLSELPK NHPKGTLIME ELAMVASPPN
SPRQSIMSTS NQYSTVAKPA ALTGTLDVRL MGCQDLLENV PGRSKTASVS LPGWSPSEAR
SSFMSRGNKN KSGSSRTLSK SDDLSNEISA VLKLDNTVVG QTHWKPVSNQ SWDQKFTLEL
DRSRELEIAV YWRDWRSLCA VKFLRLEDFL DNQRHGMCLY LEPQGTLFAE VTFFNPVIER
RPKLQRQKKI FSKQQGKTFL RAPQMNINIA TWGRLVRRAI PSVNTSFSPQ AADLGSAMSH
ETAPMGHPDA HSLPSDPTVT KLDFDKAVTP PSKRNSIEVE IEETAPPDKI SDGKEVQDAL
ATFDFLNNTV AKPDYDSLVE HEQPGLELTE IQRKTEIREE EEVQFSLSDF KCVAVLGRGH
FGKVLLADYK TTGEMFAIKA LKKGDIVARD EVDSLMCEKR IFETVNSVRH PFLVNLFACF
QTKEHVCFVM EYAAGGDLMM HIHADVFSET RSVFYAACVV LGLQFLHDHK IVYRDLKLDN
LLLDTEGYVK IADFGLCKEG MGFKDRTSTF CGTPEFLAPE VLTETSYTRA VDWWGLGVLI
FEMLVGESPF PGDDEEEVFD SIVNDEVRYP KYLSTEAISI MRRLLRRNPE RRLGAGERDA
EEVKRHPFFR DMDWPGLLAK KIRPPFVPTI TSREDVSNFD DEFTSEAPIL TPPREPRILT
LGEQDLFADF DYIADWC
