ID K7DNJ5_PANTR Unreviewed; 1315 AA.
AC K7DNJ5; A0A2J8NGF0; H2QJF4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=STK36 {ECO:0000313|EMBL:JAA42320.1,
GN ECO:0000313|Ensembl:ENSPTRP00000022091.5, ECO:0000313|VGNC:VGNC:2874};
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:JAA42320.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000022091.5, 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:JAA42320.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA05383.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA42320.1}, and Smooth vascular
RC {ECO:0000313|EMBL:JAA19091.1};
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:ENSPTRP00000022091.5}
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; AACZ04056565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01005955; JAA05383.1; -; mRNA.
DR EMBL; GABF01003054; JAA19091.1; -; mRNA.
DR EMBL; GABE01002419; JAA42320.1; -; mRNA.
DR RefSeq; XP_016805994.1; XM_016950505.1.
DR STRING; 9598.ENSPTRP00000022091; -.
DR PaxDb; 9598-ENSPTRP00000022091; -.
DR Ensembl; ENSPTRT00000023958.5; ENSPTRP00000022091.5; ENSPTRG00000012926.6.
DR GeneID; 459948; -.
DR CTD; 27148; -.
DR VGNC; VGNC:2874; STK36.
DR eggNOG; KOG0597; Eukaryota.
DR GeneTree; ENSGT00940000158375; -.
DR OrthoDB; 275383at2759; -.
DR TreeFam; TF105340; -.
DR Proteomes; UP000002277; Chromosome 2B.
DR Bgee; ENSPTRG00000012926; Expressed in testis and 20 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl.
DR GO; GO:0035082; P:axoneme assembly; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR CDD; cd14002; STKc_STK36; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
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; PTHR22983; PROTEIN KINASE RELATED; 1.
DR PANTHER; PTHR22983:SF6; SERINE_THREONINE-PROTEIN KINASE 36; 1.
DR Pfam; PF13646; HEAT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; ARM repeat; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:JAA42320.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..254
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 312..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1315 AA; 144026 MW; 8BDA2B757DA9B4AF CRC64;
MEKYHVLEMI GEGSFGRVYK GRRKYSAQVV ALKFIPKLGR SEKELRNLQR EIEIMRGLRH
PNIVHMLDSF ETDKEVVVVT DYAEGELFQI LEDDGKLPED QVQAIAAQLV SALYYLHSHR
ILHRDMKPQN ILLAKGGGIK LCDFGFARAM STNTMVLTSI KGTPLYMSPE LVEERPYDHT
ADLWSVGCIL YELAVGTPPF YATSIFQLVS LILKDPVRWP STISPCFKNF LQGLLTKDPR
QRLSWPDLLY HPFIAGHVTI ITESAGPDLG TPFTSRLPPE LQVLKDEQAH RLAPKGNQSR
ILTQAYKRMA EEAMQKKHQN TGPALEQEDK TSKVAPGTAP LPRLGATPQE SSLLAGILAS
ELKSSWAESG TGEVPSAPRE NRTTPDCERA FPEERPEVLG QRSTDVVDLE NEEPDSDNEW
QHLLETTEPV PIQLKAPLTL LCNPDFCQRI QSQLHEAGGQ ILKGILEGAS HILPAFRVLS
SLLSSCSDSV ALYSFCREAG LPGLLLSLLR HSQESNSLQQ QSWYGTFLRD LMAVIQAYFA
CTFNLERSQT NDSLQVFQEA ANLFLDLLGK LLAQPDDSEQ TLRRDSLMCF TVLCEAMDGN
SRAISKAFYS SLLTTQQVVL DGLLHGLTVP QLPVHTPPGA PQVSQPLREQ SEDIPGAISS
ALAAICTAPV GLPDCWDAKE QVCWHLANQL TEDSSQLRPS LISGLQHPIL CLHLLKVLYS
CCLVSEGLCR LLGQEPLALE SLFMLIQGKV KVVDWEESTE VTLYFLSLLV FRLQNLPCGM
EKLGSDVATL FTHSHVVSLV SAAACLLGQL GQQGVTFDLQ PMEWMAAATH ALSAPAEVRL
TPPGSCGFYD GLLILLLQLL TEQGKASLIR DMCSSEMWTV LWHRFSMVLR LPEEASAQEG
ELSLSSPPSP EPDWTLISPQ GMAALLSLAM ATFTQEPQLC LSCLSQHGSI LMSILKHLLC
PSFLNQLRQA PHGSEFLPVV VLSVCQLLCF PFALDMDADL LIGVLADLRD SEVAAHLLQV
CCYHLPLMQV ELPISLLTRL ALMDPTSLNQ FVNTVSASPR TIVSFLSVAL LSDQPLLTSD
LLSLLAHTAR VLSPSHLSFI QELLAGSDES YRPLRSLLGH PENSVRAHTY RLLGHLLQHS
MALRGALQSQ SGLLSLLLLG LGDKDPVVRC SASFAVGNAA YQAGPLGPAL AAAVPSMTQL
LGDPQAGIRR NVASALGNLG PEGLGEELLQ CEVPQRLLEM ACGDPQPNVK EAALIALRSL
QQEPGIHQVL VSLGASEKLS LLSLGNQSLP HSSPRPASAK HCRKLIHLLR PAHSM
//
