ID K7FGT3_PELSI Unreviewed; 477 AA.
AC K7FGT3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Serine/threonine-protein kinase OSR1 {ECO:0000256|ARBA:ARBA00040079};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Oxidative stress-responsive 1 protein {ECO:0000256|ARBA:ARBA00042936};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000007243.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000007243.1}
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 EMBL; AGCU01068487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01068488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01068489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01068490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01068491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01068492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01068493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FGT3; -.
DR Ensembl; ENSPSIT00000007284.1; ENSPSIP00000007243.1; ENSPSIG00000006561.1.
DR GeneTree; ENSGT00940000154621; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:SF1; SERINE_THREONINE-PROTEIN KINASE OSR1; 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:UP000007267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..235
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 260..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 477 AA; 52324 MW; 489EC0D197CC6484 CRC64;
MDELLKEIQA MSQCHHPNIV SYYTSFVVKD ELWLVMKLLS GGSVLDVIKH IVAKGEHKNG
VLDEPNIATI LKEVLEGLDY LHKNGQIHRD VKAGNILLGE DGSVQIADFG VSAFLATGGD
ITRNKVRKTF VGTPCWMAPE VMEQVRGYDF KADIWSFGIT AIELATGAAP YHKYPPMKVL
MLTLQNDPPS LETGVQDKEM LKKYGKSFRK MISSCLQKDP EKRPTAAELL RHKFFTKAKN
KEFLQEKMLQ RAPTITERAK KVRRVPGSSG RLHKTEDGGW EWSDDELDEE SEEGRAAISQ
LRSPRVKESL QNSELFPPAE PTGHLLHVPA QTAELPQPAG QTPAQPSQIA VPPSVQMPAA
ALAAGQAPPA PAVAPVQEDV KVPISLVLRL RNSKKELNDI RFEFTPGRDT ADGVSQELIS
AGLVDGRDLV IVAANLQKIV EEPQANRSVT FKLASGVEGS DIPDDGKLIG FAQLSIS
//
