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Serine/threonine-protein kinase DCLK2 (EC 2.7.11.1) (CaMK-like CREB regulatory kinase 2) (CL2) (CLICK-II) (CLICK2) (Doublecortin-like and CAM kinase-like 2) (Doublecortin-like kinase 2)

 DCLK2_RAT               Reviewed;         767 AA.
Q5MPA9; Q5MPA7; Q5MPA8; Q5MPB0;
23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 2.
07-NOV-2018, entry version 122.
RecName: Full=Serine/threonine-protein kinase DCLK2;
EC=2.7.11.1;
AltName: Full=CaMK-like CREB regulatory kinase 2;
Short=CL2;
Short=CLICK-II;
Short=CLICK2;
AltName: Full=Doublecortin-like and CAM kinase-like 2;
AltName: Full=Doublecortin-like kinase 2;
Name=Dclk2; Synonyms=Dcamkl2, Dck2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE
[MRNA] OF 269-386 (ISOFORM 3), INTERACTION WITH MICROTUBULES,
SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-438.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=15611072; DOI=10.1074/jbc.M411027200;
Edelman A.M., Kim W.Y., Higgins D., Goldstein E.G., Oberdoerster M.,
Sigurdson W.;
"Doublecortin kinase-2, a novel doublecortin-related protein kinase
associated with terminal segments of axons and dendrites.";
J. Biol. Chem. 280:8531-8543(2005).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND THR-681, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
-!- FUNCTION: Protein kinase with a significantly reduced Ca(2+)+/CAM
affinity and dependence compared to other members of the CaMK
family. May play a role in the down-regulation of CRE-dependent
gene activation probably by phosphorylation of the CREB
coactivator CRTC2/TORC2 and the resulting retention of TORC2 in
the cytoplasm (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with MAPK8IP1/JIP-1, MAPK8IP2/JIP-2,
MAPK9/JNK2, PPP1R9B/NEURABIN-2 and actin (By similarity). Binds to
and stabilizes microtubules; binding affinity is strongly reduced
by autophosphorylation. {ECO:0000250,
ECO:0000269|PubMed:15611072}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:15611072}. Note=Colocalizes with microtubules.
When overexpressed in sympathetic neurons, localizes to cell body
and to the terminal segments of axons and dendrites.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q5MPA9-1; Sequence=Displayed;
Name=2;
IsoId=Q5MPA9-2; Sequence=VSP_038898, VSP_038899;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q5MPA9-3; Sequence=VSP_038897;
-!- DOMAIN: The doublecortin domains are involved in the binding to
microtubules.
-!- PTM: Autophosphorylated.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. CaMK subfamily. {ECO:0000305}.
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EMBL; AY673997; AAV85461.1; -; mRNA.
EMBL; AY673998; AAV85462.1; -; mRNA.
EMBL; AY673999; AAV85463.1; -; mRNA.
EMBL; AY674000; AAV85464.1; -; mRNA.
RefSeq; NP_001009691.3; NM_001009691.3. [Q5MPA9-1]
RefSeq; NP_001182761.1; NM_001195832.1. [Q5MPA9-2]
RefSeq; XP_006232741.1; XM_006232679.3. [Q5MPA9-1]
RefSeq; XP_006232743.1; XM_006232681.3. [Q5MPA9-3]
RefSeq; XP_017446402.1; XM_017590913.1. [Q5MPA9-2]
UniGene; Rn.23327; -.
ProteinModelPortal; Q5MPA9; -.
SMR; Q5MPA9; -.
STRING; 10116.ENSRNOP00000053894; -.
iPTMnet; Q5MPA9; -.
PhosphoSitePlus; Q5MPA9; -.
PaxDb; Q5MPA9; -.
PRIDE; Q5MPA9; -.
Ensembl; ENSRNOT00000057062; ENSRNOP00000053894; ENSRNOG00000016550. [Q5MPA9-1]
Ensembl; ENSRNOT00000066004; ENSRNOP00000062805; ENSRNOG00000016550. [Q5MPA9-1]
Ensembl; ENSRNOT00000079954; ENSRNOP00000075203; ENSRNOG00000016550. [Q5MPA9-2]
Ensembl; ENSRNOT00000089339; ENSRNOP00000074906; ENSRNOG00000016550. [Q5MPA9-2]
GeneID; 310698; -.
KEGG; rno:310698; -.
UCSC; RGD:1308384; rat. [Q5MPA9-1]
CTD; 166614; -.
RGD; 1308384; Dclk2.
eggNOG; KOG0615; Eukaryota.
eggNOG; ENOG410YA63; LUCA.
GeneTree; ENSGT00930000150819; -.
HOGENOM; HOG000230855; -.
HOVERGEN; HBG003790; -.
InParanoid; Q5MPA9; -.
KO; K08805; -.
OMA; CERAGTW; -.
OrthoDB; EOG091G02RF; -.
PhylomeDB; Q5MPA9; -.
TreeFam; TF318770; -.
PRO; PR:Q5MPA9; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000016550; Expressed in 9 organ(s), highest expression level in brain.
ExpressionAtlas; Q5MPA9; baseline and differential.
Genevisible; Q5MPA9; RN.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0021860; P:pyramidal neuron development; IEA:Ensembl.
CDD; cd01617; DCX; 2.
Gene3D; 3.10.20.230; -; 2.
InterPro; IPR003533; Doublecortin_dom.
InterPro; IPR036572; Doublecortin_dom_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF03607; DCX; 2.
Pfam; PF00069; Pkinase; 1.
SMART; SM00537; DCX; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF89837; SSF89837; 2.
PROSITE; PS50309; DC; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Kinase; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 767 Serine/threonine-protein kinase DCLK2.
/FTId=PRO_0000393224.
DOMAIN 72 158 Doublecortin 1. {ECO:0000255|PROSITE-
ProRule:PRU00072}.
DOMAIN 196 279 Doublecortin 2. {ECO:0000255|PROSITE-
ProRule:PRU00072}.
DOMAIN 409 666 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 415 423 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 292 377 Ser-rich.
COMPBIAS 739 751 Pro-rich.
ACT_SITE 530 530 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 438 438 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 61 61 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8N568}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N568}.
MOD_RES 662 662 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 681 681 Phosphothreonine.
{ECO:0000244|PubMed:16641100}.
VAR_SEQ 320 335 Missing (in isoform 3).
{ECO:0000303|PubMed:15611072}.
/FTId=VSP_038897.
VAR_SEQ 707 715 NTALDKEGQ -> VQGHEHGSR (in isoform 2).
{ECO:0000303|PubMed:15611072}.
/FTId=VSP_038898.
VAR_SEQ 716 767 Missing (in isoform 2).
{ECO:0000303|PubMed:15611072}.
/FTId=VSP_038899.
MUTAGEN 438 438 K->A: Loss of autophosphorylation.
{ECO:0000269|PubMed:15611072}.
CONFLICT 126 126 V -> I (in Ref. 1; AAV85464).
{ECO:0000305}.
CONFLICT 308 308 P -> L (in Ref. 1; AAV85464).
{ECO:0000305}.
CONFLICT 387 387 R -> C (in Ref. 1; AAV85461/AAV85462).
{ECO:0000305}.
SEQUENCE 767 AA; 84016 MW; 2348331B01FF5B79 CRC64;
MASTRSIELE HFEERDKRPR PGSRRGAPSS SGGSSISGPK GNGLIPSPAH SAHCSFYRTR
TLQALSSEKK AKKARFYRNG DRYFKGLVFA ISSDRFRSFD ALLIELTRSL SDNVNLPQGV
RTIYTVDGSR KVTSLDELLE GESYVCASNE PFRKVDYTKN VNPNWSVNIK GGTTRTLAVA
SAKSEVKESK DFIKPKLVTV IRSGVKPRKA VRILLNKKTA HSFEQVLTDI TEAIKLDSGV
VKRLCTLDGK QVTCLQDFFG DDDVFIACGP EKYRYAQDDF VLDHSECRVL KSSYSRASAA
KYSGSRSPGL SRRSKSPASV KRAGHSSAYS TAKSPVNGTP SSQLSTPKST KSSSSSPTSP
GSFRGLKQIS AQGRSSSNVN GGPELDRCMS PEGVNGNRCS ESFTLLEKYR IGKVIGDGNF
AVVKECMDRS TGKEFALKII DKAKCCGKEH LIENEVSILR RVKHPNIIML VEEMETTTEL
FLVMELVKGG DLFDAITSST KYTERDGSAM VYNLASALRY LHGLSIVHRD IKPENLLVCE
YPDGTKSLKL GDFGLATVVE GPLYTVCGTP TYVAPEIIAE TGYGLKVDVW AAGVITYILL
CGFPPFRSEN NLQEDLFDQI LAGKLEFPAP YWDNITDSAK ELISQMLQVN VEARCTAGEI
LSHPWVSDDA SQENNMQAEV TGKLKQHFNN ALPKQNSTTT GVSVIMNTAL DKEGQVFCSK
HCRDSSKSSR EQTSAREAPP PPESPRPPGP PATSGCDPAG TWRRHRD


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