STK36_PONAB
ID STK36_PONAB Reviewed; 1315 AA.
AC Q5RAJ5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Serine/threonine-protein kinase 36;
DE EC=2.7.11.1;
DE AltName: Full=Fused homolog;
GN Name=STK36 {ECO:0000250|UniProtKB:Q9NRP7};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAH91215.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:CAH91215.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine/threonine protein kinase which plays an important role
CC in the sonic hedgehog (Shh) pathway by regulating the activity of GLI
CC transcription factors. Controls the activity of the transcriptional
CC regulators GLI1, GLI2 and GLI3 by opposing the effect of SUFU and
CC promoting their nuclear localization. GLI2 requires an additional
CC function of STK36 to become transcriptionally active, but the enzyme
CC does not need to possess an active kinase catalytic site for this to
CC occur. Required for postnatal development, possibly by regulating the
CC homeostasis of cerebral spinal fluid or ciliary function. Essential for
CC construction of the central pair apparatus of motile cilia (By
CC similarity). {ECO:0000250|UniProtKB:Q69ZM6}.
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:0000250|UniProtKB:P23647};
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:0000250|UniProtKB:P23647};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with SPAG16 and KIF27. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NRP7}. Nucleus
CC {ECO:0000250|UniProtKB:Q9NRP7}. Cytoplasm, cytoskeleton, cilium
CC axoneme. Note=Low levels also present in the nucleus.
CC {ECO:0000250|UniProtKB:Q9NRP7}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CR859020; CAH91215.1; -; mRNA.
DR AlphaFoldDB; Q5RAJ5; -.
DR SMR; Q5RAJ5; -.
DR STRING; 9601.ENSPPYP00000014729; -.
DR eggNOG; KOG0597; Eukaryota.
DR InParanoid; Q5RAJ5; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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:0001222; F:transcription corepressor binding; ISS:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0007228; P:positive regulation of hh target transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045193; Fused-like.
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; PTHR22983; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Developmental protein; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1315
FT /note="Serine/threonine-protein kinase 36"
FT /id="PRO_0000229022"
FT DOMAIN 4..254
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 312..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P23647,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23647,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23647,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1315 AA; 143909 MW; 07E1E008D146FCEA CRC64;
MEKYHVLEMI GEGSFGRVYK GRRKYSAQVV ALKFIPKLGR SEKELRNLQR EIEIMRGLRH
PNIVHMLDSF ETDKEVVVVT DYAEGELLQI LEDDGKLPED QVQAIAAQLV SALYYLHSHR
ILHRDMKPQN ILLAKGGGIK LCDFGFARAM STNTMVLTSI KGTPLYMSPE LVEERPYDHT
ADLWSVGCIL YELAVGTPPF YATSIFQLVS LILKDPVRWP STISPCFKNF LQGLLTKDPR
QRLSWPDLLY HPFIAGHVTI ITETAGPDLG TPFTSRLPPE LQVLKDKQAH RLSPKGNQSR
ILTQAYERMA EEAMQKKHQN TGPALEQEDK TSKVAPGTAP LPRLGATPQE SSLLAGILAS
ELKSSWAESG TGEAPSAPRE NRTTPDCERA FPEERPEVLG QRSTDAVDLE DEEPDSDNEW
QHLLETTEPV PIQLKAPLTL LCNPDFCQRI QSQLHEAGGQ ILKGILEGAS HILPAFRVLS
SLLSSCSDSV ALYSFCREAG LPGLLLSLLR HSQESNSLQQ QSWYGTFLQD LMAVIQAYFA
CTFNLERSQT SDSLQVFQEA ANLFLDLLGK LLAQPDDSER TLRRDNLMCF TVLCEAMDGN
SRAISKAFYS SLLTTKQVVL DGLLRGLTVP QLPVHTPPGA PQVSQPLREQ SEDIPGAISS
ALAAICTAPV GLPDCWDGKE QVCWHLANQL TEDSSQLRPS LVSGLQHPIL CLHLLKVLYS
CCLVSERLCR LLGQEPLALE SLFMLVQGKV KVVDWEESTE VTLYFLSLLV FRLQNLPCGM
EKLGSDVATL FTHSHVASLV SAAACLLGQL GQQGVTFDLQ PMEWMAAATH ALSAPAEVRL
TPPGSCGFYD GLLILLLQLL TEQGKASLIR DMSSSEMWTV LRHRFSMVLR LPKEASAQEG
ELSLSNPPSP EPDWTLISPQ GMAALLSLAM ATFAQEPQLC LSCLSQHGSI LMSILKHLLC
PSFLNQLRQA PHGSEFLPVV VLSVCQLLCF PFALDMDADL LIGVLADLRD SEVAAHLLQV
CCYHLPLTQV ELPISLLTRL ALTDPTSLNQ FVNTVAASPR TIISFLSVAL LSDQPLLTSD
LLSLLAHTAR VLSPSHLSFI QELLAGSDES YQSLRSLLGH PENSVRAHTY RLLGHLLQHS
MALRGALQSQ SGLLSLLLLG LGDKDPVVRC SASFAVGNAA YQAGPLGPAL AAAVPSMTQL
LGDPQAGIRR NVASALGNLG LEGLGEELLQ CQVPQRLLEM ACGDPQPNVK EAALIALRSL
QQEPGIRQVL VSLGASEKLA LLSLGNQLLP HSSPRPASAK HCRKLIHLLR PAHSM
