DCLK2_AILME
ID DCLK2_AILME Reviewed; 784 AA.
AC D2I3C6;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Serine/threonine-protein kinase DCLK2;
DE EC=2.7.11.1;
DE AltName: Full=CaMK-like CREB regulatory kinase 2;
DE Short=CL2;
DE Short=CLICK-II;
DE Short=CLICK2;
DE AltName: Full=Doublecortin-like and CAM kinase-like 2;
DE AltName: Full=Doublecortin-like kinase 2;
GN Name=DCLK2; Synonyms=DCAMKL2, DCK2; ORFNames=PANDA_020009;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- FUNCTION: Protein kinase with a significantly reduced Ca(2+)/CAM
CC affinity and dependence compared to other members of the CaMK family.
CC May play a role in the down-regulation of CRE-dependent gene activation
CC probably by phosphorylation of the CREB coactivator CRTC2/TORC2 and the
CC resulting retention of TORC2 in the cytoplasm (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=2.7.11.1;
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: Binds to and stabilizes microtubules. Interacts with
CC MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK9/JNK2, PPP1R9B/NEURABIN-2 and
CC actin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes with
CC microtubules. {ECO:0000250}.
CC -!- DOMAIN: The doublecortin domains are involved in the colocalization
CC with microtubules. {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; GL194290; EFB15487.1; -; Genomic_DNA.
DR RefSeq; XP_011236055.1; XM_011237753.2.
DR AlphaFoldDB; D2I3C6; -.
DR SMR; D2I3C6; -.
DR STRING; 9646.ENSAMEP00000009704; -.
DR Ensembl; ENSAMET00000010124; ENSAMEP00000009704; ENSAMEG00000009231.
DR Ensembl; ENSAMET00000042834; ENSAMEP00000039822; ENSAMEG00000009231.
DR GeneID; 100474420; -.
DR KEGG; aml:100474420; -.
DR CTD; 166614; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000154895; -.
DR InParanoid; D2I3C6; -.
DR OMA; LMTECKV; -.
DR OrthoDB; 330091at2759; -.
DR TreeFam; TF318770; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; 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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF03607; DCX; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00537; DCX; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..784
FT /note="Serine/threonine-protein kinase DCLK2"
FT /id="PRO_0000393223"
FT DOMAIN 72..158
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 197..280
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 411..668
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..765
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 532
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 417..425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N568"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N568"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5MPA9"
FT MOD_RES 683
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5MPA9"
SQ SEQUENCE 784 AA; 85284 MW; A224D90105BD0B0C CRC64;
MASTRSIELE HFEERDKRPR PGSRRGAPSS SGGSSSSGPK GNGLIPSPAH SAHCSFYRTR
TLQALSSEKK AKKARFYRNG DRYFKGLVFA ISSDRFRSFD ALLMELTRSL SDNVNLPQGV
RTIYTIDGSR KVTSLDELLE GESYVCASNE PFRKVDYTKN INPNWSVNIK GGTARALAAP
SSVKSEVKES KDFIKPKLVT VIRSGVKPRK AVRILLNKKT AHSFEQVLTD ITEAIKLDSG
VVKRLCTLDG KQVTCLQDFF GDDDVFIACG PEKFRYAQDD FVLDHSECRV LKSSYSRSSA
VKYSGSKSPG PSRRSKSPAS VKRGGHHASA YSAARSPVNG TPSSQLSTPK STKSSSSSPT
SPGSFRGLKQ ISAHGRSSSN VNGGPELARC LSPEGVNGNR CSESSTLLEK YKIGKVIGDG
NFAVVKECMD RSTGKEFALK IIDKAKCCGK EHLIENEVSI LRRVKHPNII MLVEEMETAT
ELFLVMELVK GGDLFDAITS STKYTERDGS AMVYNLANAL RYLHGLSIVH RDIKPENLLV
CEYPDGTKSL KLGDFGLATV VEGPLYTVCG TPTYVAPEII AETGYGLKVD IWAAGVITYI
LLCGFPPFRS ENNLQEDLFD QILAGKLEFP APYWDNITDS AKELISQMLQ VNVEARCTAG
EILSHPWVSD DASQENNMQA EVTGKLKQHF NNALPKQNST TTGVSVIMNT ALDKEGQIFC
SKHCQDSSRP GMELTSPVPP SASAEEPPVS APAAAPAPLE SPTPPGTPAA SGCERAGTWR
RHRD
