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Database: UniProt
Entry: G3SMD4_LOXAF
LinkDB: G3SMD4_LOXAF
Original site: G3SMD4_LOXAF 
ID   G3SMD4_LOXAF            Unreviewed;       475 AA.
AC   G3SMD4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=STK39 {ECO:0000313|Ensembl:ENSLAFP00000000662.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000000662.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000000662.2, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000662.2,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000000662.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000662.2};
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};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   AlphaFoldDB; G3SMD4; -.
DR   STRING; 9785.ENSLAFP00000000662; -.
DR   Ensembl; ENSLAFT00000000792.2; ENSLAFP00000000662.2; ENSLAFG00000000791.2.
DR   eggNOG; KOG0582; Eukaryota.
DR   GeneTree; ENSGT00940000154621; -.
DR   HOGENOM; CLU_000288_111_1_1; -.
DR   InParanoid; G3SMD4; -.
DR   OMA; CKFIQKA; -.
DR   TreeFam; TF105339; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0044297; C:cell body; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006884; P:cell volume homeostasis; IEA:Ensembl.
DR   GO; GO:0071474; P:cellular hyperosmotic response; IEA:Ensembl.
DR   GO; GO:0071476; P:cellular hypotonic response; IEA:Ensembl.
DR   GO; GO:0035865; P:cellular response to potassium ion; IEA:Ensembl.
DR   GO; GO:0038146; P:chemokine (C-X-C motif) ligand 12 signaling pathway; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0030644; P:intracellular chloride ion homeostasis; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR   GO; GO:0036438; P:maintenance of lens transparency; IEA:Ensembl.
DR   GO; GO:0090188; P:negative regulation of pancreatic juice secretion; IEA:Ensembl.
DR   GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Ensembl.
DR   GO; GO:0010820; P:positive regulation of T cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0070294; P:renal sodium ion absorption; IEA:Ensembl.
DR   GO; GO:1904044; P:response to aldosterone; IEA:Ensembl.
DR   GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IEA:Ensembl.
DR   CDD; cd06610; STKc_OSR1_SPAK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR48012:SF14; STE20_SPS1-RELATED PROLINE-ALANINE-RICH PROTEIN KINASE; 1.
DR   PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR   Pfam; PF12202; OSR1_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..268
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          292..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  52853 MW;  8E620380AE79B651 CRC64;
     GSGATAVVQA ALCKPRQERV AIKRINLEKC QTSMDELLKE IQAMSQCSHP NVVTYYTSFV
     VKDELWLVMK LLSGGSMLDI IKYIVNRGEH KNGVLEEAII ATILKEVLEG LDYLHRNGQI
     HRDLKAGNIL LGEDGSVQIA DFGVSAFLAT GGDVTRNKVR KTFVGTPCWM APEVMEQVRG
     YDFKADMWSF GITAIELATG AAPYHKYPPM KVLMLTLQND PPTLETGVED KEMMKKYGKS
     FRKLLSLCLQ KDPSKRPTAA ELLKCKFFQK AKNREYLIEK LLTRTPDIAQ RAKKVRRVPG
     SSGHLHKTED GDWEWSDDEM DEKSEEGKAA FSQEKSRRVK EENPEIAVNA SSIPEQIQSL
     SVQDSQGQPN ASEDYREASC VVNLVLRLRN SRKELNDIRF EFTPGRDTAD GVSQELFSAG
     LVDGHDVVIV AANLQKIVDD PKALKTLTFK LASGCDGSEI PDEVKLIGFA QLSVS
//
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