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Database: UniProt
Entry: A0A2I2ZGK4_GORGO
LinkDB: A0A2I2ZGK4_GORGO
Original site: A0A2I2ZGK4_GORGO 
ID   A0A2I2ZGK4_GORGO        Unreviewed;       817 AA.
AC   A0A2I2ZGK4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=DCLK3 {ECO:0000313|Ensembl:ENSGGOP00000046395.1};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000046395.1, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000046395.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000046395.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000046395.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; CABD030020746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2ZGK4; -.
DR   STRING; 9593.ENSGGOP00000046395; -.
DR   Ensembl; ENSGGOT00000054355.1; ENSGGOP00000046395.1; ENSGGOG00000016779.3.
DR   GeneTree; ENSGT00940000159476; -.
DR   InParanoid; A0A2I2ZGK4; -.
DR   OMA; GHHCGET; -.
DR   Proteomes; UP000001519; Chromosome 3.
DR   Bgee; ENSGGOG00000016779; Expressed in testis and 1 other cell type or tissue.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR   GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR   CDD; cd16111; DCX_DCLK3; 1.
DR   CDD; cd14185; STKc_DCKL3; 1.
DR   Gene3D; 3.10.20.230; Doublecortin domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24347:SF427; SERINE_THREONINE-PROTEIN KINASE DCLK3; 1.
DR   Pfam; PF03607; DCX; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00537; DCX; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF89837; Doublecortin (DC); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50309; DC; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT   DOMAIN          95..175
FT                   /note="Doublecortin"
FT                   /evidence="ECO:0000259|PROSITE:PS50309"
FT   DOMAIN          525..782
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         554
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   817 AA;  92523 MW;  5B671AF85034599E CRC64;
     MPAATPAPQP PPPPARPAPA CPARPAPGQQ GLCDHSLKYL SSRITERKLQ GSWLPASRGN
     LEKPFLGPRG PVVPLFCPRN GLHSAHPENS PLKPRVVTVV KLGGQRPRKI TLLLNRRSVQ
     TFEQLLADIS EALSSPRWKN DRVRKLFNLK GREIRSVSDF FREGDAFIAM GKEPLTLKSI
     QVAVEELYPN KARALTLAQH SRAPSPRLRS RLFSKALKGD HRCGETETPK SCSEVAGCKA
     AMRHQGKIPE ELSLDDRART QKKWGRGKWE PEPSSKPPRE ATLEERHARG EKHLGVEIEK
     TSGEIIRCEK CKRERELQQS LERERLSLGT SELDMGKGPM YDMEKLVRTR SCRRSPEANS
     ASGEEGWKGD SHRSSPRNPT QELRRPSKSM DKKEDRGPED QESHAQGAAK AKKDLVEVLP
     VTEEGLREVK KDTRPMSRSK HGGWLLREHQ AGFEKLRRTR GEEKEAEKEK KPFMSGGRRM
     TLRDDQPAKL EKEPKTRPEE NKPERPSGRK PRPMGIIAAN VEKHYETGRV IGDGNFAVVK
     ECRHRETRQA YAMKIIDKSR LKGKEDMVDS EILIIQSLSH PNIVKLHEVY ETDMEIYLIL
     EYVQGGDLFD AIIESVKFPE PDAALMIMDL CKALVHMHDK SIVHRDLKPE NLLVQRNEDK
     STTLKLADFG LAKHVVRPIF TVCGTPTYVA PEILSEKGYG LEVDMWAAGV ILYILLCGFP
     PFRSPERDQD ELFNIIQLGH FEFLPPYWDN ISDAAKDLVS RLLVVDPKKR YTAHQVLQHP
     WIETAGKTNT VKRQKQVSPS SEGHFRSQHK RVVEQVS
//
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