OXSR1_PIG
ID OXSR1_PIG Reviewed; 529 AA.
AC Q863I2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Serine/threonine-protein kinase OSR1;
DE EC=2.7.11.1;
DE AltName: Full=Oxidative stress-responsive 1 protein;
GN Name=OXSR1 {ECO:0000250|UniProtKB:O95747}; Synonyms=OSR1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000312|EMBL:AAP32466.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15561286; DOI=10.1016/j.transproceed.2004.07.058;
RA Hu W., Cheng J., Lu X., Li S., Zeng L., Li Y.;
RT "The novel molecule porcine OSR1 up-regulated expression on porcine
RT endothelial cell by human peripheral blood mononuclear cell activation.";
RL Transplant. Proc. 36:2475-2477(2004).
CC -!- FUNCTION: Phosphorylates RELL1, RELL2, RELT and PAK1. Phosphorylates
CC PLSCR1 in the presence of RELT. {ECO:0000250|UniProtKB:O95747}.
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:O95747};
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:O95747};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O95747};
CC -!- ACTIVITY REGULATION: By autophosphorylation on threonine.
CC {ECO:0000250|UniProtKB:O95747}.
CC -!- SUBUNIT: Interacts with PAK1. Interacts with chloride channel proteins
CC SLC12A6 isoform 2, SLC12A1 and SLC12A2 but not with SLC12A4 and
CC SLC12A7, possibly establishing sensor/signaling modules that initiate
CC the cellular response to environmental stress. Interacts with RELL1,
CC RELL2 and RELT. Interacts with PLSCR1 in the presence of RELT.
CC {ECO:0000250|UniProtKB:O95747, ECO:0000250|UniProtKB:Q6P9R2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95747}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O95747}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AY271356; AAP32466.1; -; mRNA.
DR RefSeq; NP_001302601.1; NM_001315672.1.
DR RefSeq; NP_999507.1; NM_214342.1.
DR AlphaFoldDB; Q863I2; -.
DR SMR; Q863I2; -.
DR STRING; 9823.ENSSSCP00000011997; -.
DR PaxDb; Q863I2; -.
DR PeptideAtlas; Q863I2; -.
DR Ensembl; ENSSSCT00005015647; ENSSSCP00005009337; ENSSSCG00005009949.
DR Ensembl; ENSSSCT00070024629; ENSSSCP00070020382; ENSSSCG00070012557.
DR GeneID; 106505565; -.
DR GeneID; 397618; -.
DR KEGG; ssc:397618; -.
DR CTD; 9943; -.
DR eggNOG; KOG0582; Eukaryota.
DR InParanoid; Q863I2; -.
DR OMA; TSNCKQG; -.
DR OrthoDB; 855861at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 13.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR028749; Oxsr1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF1; PTHR48012:SF1; 1.
DR Pfam; PF12202; OSR1_C; 1.
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 Acetylation; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95747"
FT CHAIN 2..529
FT /note="Serine/threonine-protein kinase OSR1"
FT /id="PRO_0000086458"
FT DOMAIN 17..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 315..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W9,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 23..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W9,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O95747,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O95747"
FT MOD_RES 310
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95747"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95747"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95747"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95747"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95747"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95747"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95747"
SQ SEQUENCE 529 AA; 58233 MW; 3B93703147C5E963 CRC64;
MSEDSSALPW SINKDDYELQ EVIGSGATAV VQAAYCTPKK EKVAIKRINL EKCQTSMDEL
LKEIQAMSQC HHPNIVSYYT SFVVKDELWL VMKLLSGGSV LDIIKHIVAK GEHKSGVLDE
ATIATILREV LEGLEYLHKN GQIHRDVKAG NILLGEDGSV QIADFGVSAF LATGGDITRN
KVRKTFVGTP CWMAPEVMEQ VRGYDFKADI WSFGITAIEL ATGAAPYHKY PPMKVLMLTL
QNDPPSLETG VQDKEMLKKY GKSFRKMISL CLQKDPEKRP TAAELLRHKF FQKAKNKEYL
QEKILQRAPT ISERAKKVRR VPGSSGRLHK TEDGGWEWSD DEFDEESEEG KAAISQLRSP
RVKESLTNSE LFSTTHPVGT LLQVPEQISA HLPQSAGQMP AQLTPVSLPP AAELAPVQAA
QAQSSGAGSQ ETKIPISLVL RLRNSKKELN DIRFEFTPGR DTAEGVSQEL ISAGLVDGRD
LVIVAANLQK IVEEPQSNRS VTFKLASGVE GSDIPDDSKL IGFAQLSIS
