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Database: UniProt
Entry: K7C9T1_PANTR
LinkDB: K7C9T1_PANTR
Original site: K7C9T1_PANTR 
ID   K7C9T1_PANTR            Unreviewed;       539 AA.
AC   K7C9T1; A0A2J8NUA1;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=calcium/calmodulin-dependent protein kinase {ECO:0000256|ARBA:ARBA00012434};
DE            EC=2.7.11.17 {ECO:0000256|ARBA:ARBA00012434};
GN   Name=CAMK2G {ECO:0000313|EMBL:JAA20985.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000082005.1,
GN   ECO:0000313|VGNC:VGNC:11683};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA20985.1};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000082005.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA20985.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA03756.1}, Skin
RC   {ECO:0000313|EMBL:JAA24055.1}, and Smooth vascular
RC   {ECO:0000313|EMBL:JAA20985.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000082005.1}
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=2.7.11.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000902};
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=2.7.11.17; Evidence={ECO:0000256|ARBA:ARBA00000517};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CaMK subfamily. {ECO:0000256|ARBA:ARBA00005354}.
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DR   EMBL; AACZ04050451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABC01007582; JAA03756.1; -; mRNA.
DR   EMBL; GABF01001160; JAA20985.1; -; mRNA.
DR   EMBL; GABD01009045; JAA24055.1; -; mRNA.
DR   RefSeq; XP_016774124.1; XM_016918635.1.
DR   Ensembl; ENSPTRT00000099404.1; ENSPTRP00000082005.1; ENSPTRG00000002643.7.
DR   GeneID; 738330; -.
DR   CTD; 818; -.
DR   VGNC; VGNC:11683; CAMK2G.
DR   GeneTree; ENSGT00940000156481; -.
DR   OrthoDB; 1121238at2759; -.
DR   Proteomes; UP000002277; Chromosome 10.
DR   Bgee; ENSPTRG00000002643; Expressed in primary visual cortex and 21 other cell types or tissues.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14086; STKc_CaMKII; 1.
DR   Gene3D; 3.10.450.50; -; 1.
DR   Gene3D; 6.10.140.620; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032710; NTF2-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:SF441; CALCIUM_CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT GAMMA; 1.
DR   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54427; NTF2-like; 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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Kinase {ECO:0000313|EMBL:JAA20985.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Transferase {ECO:0000313|EMBL:JAA20985.1}.
FT   DOMAIN          14..272
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          344..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   539 AA;  60201 MW;  24989285F7564529 CRC64;
     MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL SARDHQKLER
     EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIHQI
     LESVNHIHQH DIVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGEQQA WFGFAGTPGY
     LSPEVLRKDP YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT
     VTPEAKNLIN QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL
     KGAILTTMLV SRNFSVGRQS SAPASPAASA AGLAGQAAKS LLNKKSDGGV KPQSNNKNSL
     VSPAQEPAPL QTAMEPQTTV VHNATDGIKG STESCNTTTE DEDLKVRKQE IIKITEQLIE
     AINNGDFEAY TKICDPGLTS FEPEALGNLV EGMDFHKFYF ENLLSKNSKP IHTTILNPHV
     HVIGEDAACI AYIRLTQYID GQGRPRTSQS EETRVWHRRD GKWLNVHYHC SGAPAAPLQ
//
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