STK25_BOVIN
ID STK25_BOVIN Reviewed; 426 AA.
AC Q3SWY6; Q6V9V8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Serine/threonine-protein kinase 25;
DE EC=2.7.11.1;
GN Name=STK25;
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 [MRNA].
RA Zhou G., Dang Y., Yu L.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxidant stress-activated serine/threonine kinase that may
CC play a role in the response to environmental stress. Targets to the
CC Golgi apparatus where it appears to regulate protein transport events,
CC cell adhesion, and polarity complexes important for cell migration (By
CC similarity). {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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Interaction with Golgi matrix protein GOLGA2 leads
CC to autophosphorylation on Thr-174, possibly as a consequence of
CC stabilization of dimer formation. The C-terminal non-catalytic region
CC inhibits the kinase activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with CTTNBP2NL. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Note=Localizes to the Golgi apparatus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ55285.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY346153; AAQ55285.1; ALT_FRAME; mRNA.
DR EMBL; BC104597; AAI04598.1; -; mRNA.
DR RefSeq; NP_899666.1; NM_183407.2.
DR AlphaFoldDB; Q3SWY6; -.
DR SMR; Q3SWY6; -.
DR STRING; 9913.ENSBTAP00000040234; -.
DR PaxDb; Q3SWY6; -.
DR PRIDE; Q3SWY6; -.
DR Ensembl; ENSBTAT00000012764; ENSBTAP00000012764; ENSBTAG00000009676.
DR Ensembl; ENSBTAT00000042598; ENSBTAP00000040234; ENSBTAG00000009676.
DR GeneID; 373543; -.
DR KEGG; bta:373543; -.
DR CTD; 10494; -.
DR VEuPathDB; HostDB:ENSBTAG00000009676; -.
DR VGNC; VGNC:35391; STK25.
DR eggNOG; KOG0201; Eukaryota.
DR GeneTree; ENSGT00940000153476; -.
DR InParanoid; Q3SWY6; -.
DR OMA; REFANQH; -.
DR OrthoDB; 967913at2759; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000009676; Expressed in retina and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
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:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0051683; P:establishment of Golgi localization; IEA:Ensembl.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR GO; GO:0090168; P:Golgi reassembly; IEA:Ensembl.
DR GO; GO:0036481; P:intrinsic apoptotic signaling pathway in response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd06642; STKc_STK25; 1.
DR Gene3D; 1.10.12.70; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR046409; PDC10_dimerisation_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR035060; STK_STK25.
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.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Golgi apparatus; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..426
FT /note="Serine/threonine-protein kinase 25"
FT /id="PRO_0000288841"
FT DOMAIN 20..270
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 292..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 26..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 174
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O00506"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2W1"
FT CONFLICT 344
FT /note="K -> N (in Ref. 1; AAQ55285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 48035 MW; 436AB21D7BE7FF8E CRC64;
MAHLRGFANQ HSRVDPEELF TKLDRIGKGS FGEVYKGIDN RTKEVVAIKI IDLEEAEDEI
EDIQQEITVL SQCDSPYITR YFGSYLKSTK LWIIMEYLGG GSALDLLKPG PLEETYIATI
LREILKGLDY LHSERKIHRD IKAANVLLSE QGDVKLADFG VAGQLTDTQI KRNTFVGTPF
WMAPEVIKQS AYDFKADIWS LGITAIELAK GEPPNSDLHP MRVLFLIPKN SPPTLEGHHS
KPFKEFVEAC LNKDPRFRPT AKELLKHKFI TRYTKKTSFL TELIDRYKRW RSEGHGEESS
SEDSDIDGDP EDGEQGPIWT FPPTIRPSPH GKLHKGTALH GPQKSAEPVK RQPRSQCLST
LVRPVFGELK EKHKQSGGGV GALEELENAF SLAEESCPGI SDKLMAHLVE RVQRFSHSRN
HLTSTR
