STK33_BOVIN
ID STK33_BOVIN Reviewed; 486 AA.
AC Q0VD22;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Serine/threonine-protein kinase 33;
DE EC=2.7.11.1;
GN Name=STK33;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine/threonine protein kinase which phosphorylates VIME.
CC May play a specific role in the dynamic behavior of the intermediate
CC filament cytoskeleton by phosphorylation of VIME (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: Interacts with VIME. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {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; BC119877; AAI19878.1; -; mRNA.
DR RefSeq; NP_001069376.1; NM_001075908.1.
DR AlphaFoldDB; Q0VD22; -.
DR SMR; Q0VD22; -.
DR STRING; 9913.ENSBTAP00000042938; -.
DR PaxDb; Q0VD22; -.
DR PRIDE; Q0VD22; -.
DR GeneID; 528309; -.
DR KEGG; bta:528309; -.
DR CTD; 65975; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q0VD22; -.
DR OrthoDB; 330091at2759; -.
DR TreeFam; TF314166; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; 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; IBA:GO_Central.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..486
FT /note="Serine/threonine-protein kinase 33"
FT /id="PRO_0000278476"
FT DOMAIN 116..381
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 39..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 122..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q924X7"
SQ SEQUENCE 486 AA; 54627 MW; 4428B459BAAAD4C7 CRC64;
MADSSCGKKS TKCPHCSSAS QKNALCICSC KTKLSPMSVV EMSQTSSTGS SEFIVSPEKR
KEKGASKDVT SGKDSPSKSS NIERKPSQQQ WGRGNFTEGK VPHIRMDNGA ALQEIYTFGR
ILGQGSFGMV IEAIDKERET KWAIKKVNKE KAGSSAVKLL EREVDILKSV KHEHIIHLEQ
VFETPKKMYL VMELCEDGEL KEILERKGHF SENETRWIIQ SLASAIAYLH NKDIVHRDLK
LENIMVKSSF IDANNEMNLN IKVTDFGLAV KKHGRSEVML QTTCGTPIYM APEVINAHDY
SQQCDIWSIG VIMYILLCGK APFMASSEEK LFELIKKGEL HFKNSIWNSI SDCAKSVLKQ
LMKVDPAHRI TAKELLDNQW LTGNTVSSAR PTNVLEMMKE WKNNPESDEE STTDQRDSRS
GQEESKVYQP SRNVPDVSNS SDEEEGKQVG RTNKTCRKNN CFISPNCEIP SQHLEHFCNS
FFVVGL
