OXSR1_MOUSE
ID OXSR1_MOUSE Reviewed; 527 AA.
AC Q6P9R2; Q8BVZ9; Q8C0B9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
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:0000312|MGI:MGI:1917378};
GN Synonyms=Osr1 {ECO:0000312|EMBL:AAH60645.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAH60645.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH60645.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH60645.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-527.
RC STRAIN=C57BL/6J; TISSUE=Head, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305}
RP INTERACTION WITH SLA12A1; SLC12A2 AND SLC12A6.
RX PubMed=12386165; DOI=10.1074/jbc.m208108200;
RA Piechotta K., Lu J., Delpire E.;
RT "Cation chloride cotransporters interact with the stress-related kinases
RT Ste20-related proline-alanine-rich kinase (SPAK) and oxidative stress
RT response 1 (OSR1).";
RL J. Biol. Chem. 277:50812-50819(2002).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=14707132; DOI=10.1074/jbc.m313562200;
RA Chen W., Yazicioglu M., Cobb M.H.;
RT "Characterization of OSR1, a member of the mammalian Ste20p/germinal center
RT kinase subfamily.";
RL J. Biol. Chem. 279:11129-11136(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Interacts with chloride
CC channel proteins SLC12A6 isoform 2, SLC12A1 and SLC12A2 but not with
CC SLC12A4 and SLC12A7, possibly establishing sensor/signaling modules
CC that initiate the cellular response to environmental stress
CC (PubMed:12386165). Interacts with RELL1, RELL2 and RELT (By
CC similarity). Interacts with PLSCR1 in the presence of RELT (By
CC similarity). {ECO:0000250|UniProtKB:O95747,
CC ECO:0000269|PubMed:12386165}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95747}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined,
CC except thymus. {ECO:0000269|PubMed:14707132}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27551.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC35996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC060645; AAH60645.1; -; mRNA.
DR EMBL; AK031790; BAC27551.1; ALT_INIT; mRNA.
DR EMBL; AK075837; BAC35996.1; ALT_INIT; mRNA.
DR CCDS; CCDS57714.1; -.
DR RefSeq; NP_598746.2; NM_133985.2.
DR RefSeq; XP_006511982.1; XM_006511919.3.
DR AlphaFoldDB; Q6P9R2; -.
DR SMR; Q6P9R2; -.
DR BioGRID; 224395; 6.
DR ELM; Q6P9R2; -.
DR IntAct; Q6P9R2; 3.
DR STRING; 10090.ENSMUSP00000042155; -.
DR iPTMnet; Q6P9R2; -.
DR PhosphoSitePlus; Q6P9R2; -.
DR EPD; Q6P9R2; -.
DR jPOST; Q6P9R2; -.
DR MaxQB; Q6P9R2; -.
DR PaxDb; Q6P9R2; -.
DR PeptideAtlas; Q6P9R2; -.
DR PRIDE; Q6P9R2; -.
DR ProteomicsDB; 294356; -.
DR Antibodypedia; 2101; 548 antibodies from 37 providers.
DR DNASU; 108737; -.
DR Ensembl; ENSMUST00000040853; ENSMUSP00000042155; ENSMUSG00000036737.
DR GeneID; 108737; -.
DR KEGG; mmu:108737; -.
DR UCSC; uc009sap.2; mouse.
DR CTD; 9943; -.
DR MGI; MGI:1917378; Oxsr1.
DR VEuPathDB; HostDB:ENSMUSG00000036737; -.
DR eggNOG; KOG0582; Eukaryota.
DR GeneTree; ENSGT00940000162134; -.
DR HOGENOM; CLU_000288_111_1_1; -.
DR InParanoid; Q6P9R2; -.
DR OMA; TSNCKQG; -.
DR OrthoDB; 855861at2759; -.
DR PhylomeDB; Q6P9R2; -.
DR TreeFam; TF105339; -.
DR BioGRID-ORCS; 108737; 14 hits in 77 CRISPR screens.
DR ChiTaRS; Oxsr1; mouse.
DR PRO; PR:Q6P9R2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6P9R2; protein.
DR Bgee; ENSMUSG00000036737; Expressed in hindlimb stylopod muscle and 240 other tissues.
DR ExpressionAtlas; Q6P9R2; baseline and differential.
DR Genevisible; Q6P9R2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IGI:ParkinsonsUK-UCL.
DR GO; GO:0071476; P:cellular hypotonic response; IGI:ParkinsonsUK-UCL.
DR GO; GO:1990869; P:cellular response to chemokine; IMP:BHF-UCL.
DR GO; GO:0038116; P:chemokine (C-C motif) ligand 21 signaling pathway; IMP:BHF-UCL.
DR GO; GO:0038146; P:chemokine (C-X-C motif) ligand 12 signaling pathway; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IGI:ParkinsonsUK-UCL.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IGI:ParkinsonsUK-UCL.
DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IGI:ParkinsonsUK-UCL.
DR GO; GO:0007231; P:osmosensory signaling pathway; ISO:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IGI:ParkinsonsUK-UCL.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; IMP:BHF-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IGI:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
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 1: Evidence at protein 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..527
FT /note="Serine/threonine-protein kinase OSR1"
FT /id="PRO_0000086457"
FT DOMAIN 17..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 313..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..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:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
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 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95747"
FT CONFLICT 201
FT /note="V -> F (in Ref. 2; BAC27551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 58214 MW; 72A09F0D732375E1 CRC64;
MSEDSSALPW SINRDDYELQ EVIGSGATAV VQAAYCAPKK ERVAIKRINL EKCQTSMDEL
LKEIQAMSQC HHPNIVSYYT SFVVKDELWL VMKLLSGGSV LDIIKHIVAK GEHKSGVLDE
PTIATILREV LEGLEYLHKN GQIHRDVKAG NILLGEDGSV QIADFGVSAF LATGGDITRN
KVRKTFVGTP CWMAPEVMEQ VRGYDFKADI WSFGITAIEL ATGAAPYHKY PPMKVLMLTL
QNDPPSLETG VQDKEMLKKY GKSFRKMISL CLQKDPEKRP TAAELLRHKF FQKAKNKEFL
QEKILQRAPT ISERSKKVRR VPGSSGRLHK TEDGGWEWSD DEFDEESEEG RAAISQLRSP
RVKDSLSSSE LFAAAEPMGT LLQVPEQISA HLPQPAGQMP TQPAQVSLLP PAEPAKPAQA
QSSGERSQET KIPISLVLRL RNSKKELNDI RFEFTPGRDT AEGVSQELIS AGLVDGRDLV
IVAANLQKIV EEPQSNRSVT FKLASGVEGS DIPDDGKLIG FAQLSIS
