SRPK3_MOUSE
ID SRPK3_MOUSE Reviewed; 565 AA.
AC Q9Z0G2;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=SRSF protein kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=Muscle-specific serine kinase 1;
DE Short=MSSK-1;
DE AltName: Full=Serine/arginine-rich protein-specific kinase 3;
DE Short=SR-protein-specific kinase 3;
DE AltName: Full=Serine/threonine-protein kinase 23;
GN Name=Srpk3; Synonyms=Mssk1, Stk23;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Muscle;
RA Brenner V., Rosenthal A.;
RT "Cloning and sequencing of a new muscle-specific serine kinase gene in
RT human and mouse.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., Rosenthal A.;
RT "Comparative sequence analysis of the mouse L1cam locus and the
RT corresponding region of human Xq28.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16140986; DOI=10.1101/gad.1338705;
RA Nakagawa O., Arnold M., Nakagawa M., Hamada H., Shelton J.M., Kusano H.,
RA Harris T.M., Childs G., Campbell K.P., Richardson J.A., Nishino I.,
RA Olson E.N.;
RT "Centronuclear myopathy in mice lacking a novel muscle-specific protein
RT kinase transcriptionally regulated by MEF2.";
RL Genes Dev. 19:2066-2077(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-328, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Spleen;
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: Serine/arginine-rich protein-specific kinase which
CC specifically phosphorylates its substrates at serine residues located
CC in regions rich in arginine/serine dipeptides, known as RS domains.
CC Phosphorylates the SR splicing factor SRSF1 and the lamin-B receptor
CC (LBR) in vitro. Required for normal muscle development.
CC {ECO:0000269|PubMed:16140986}.
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 -!- TISSUE SPECIFICITY: Exclusively expressed in skeletal and heart muscle.
CC {ECO:0000269|PubMed:16140986}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryogenesis to adulthood.
CC {ECO:0000269|PubMed:16140986}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable to adulthood but display defects
CC in skeletal muscle growth including reduced muscle mass, marked
CC increase in centrally placed nuclei and disorganized intermyofibrillar
CC network. {ECO:0000269|PubMed:16140986}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF043289; AAD02248.1; -; Genomic_DNA.
DR EMBL; AF043288; AAD02247.1; -; mRNA.
DR EMBL; AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30211.1; -.
DR RefSeq; NP_062658.1; NM_019684.2.
DR AlphaFoldDB; Q9Z0G2; -.
DR SMR; Q9Z0G2; -.
DR BioGRID; 208023; 1.
DR STRING; 10090.ENSMUSP00000002081; -.
DR iPTMnet; Q9Z0G2; -.
DR PhosphoSitePlus; Q9Z0G2; -.
DR MaxQB; Q9Z0G2; -.
DR PaxDb; Q9Z0G2; -.
DR PRIDE; Q9Z0G2; -.
DR ProteomicsDB; 263347; -.
DR Antibodypedia; 30953; 172 antibodies from 26 providers.
DR DNASU; 56504; -.
DR Ensembl; ENSMUST00000002081; ENSMUSP00000002081; ENSMUSG00000002007.
DR GeneID; 56504; -.
DR KEGG; mmu:56504; -.
DR UCSC; uc009tmo.1; mouse.
DR CTD; 26576; -.
DR MGI; MGI:1891338; Srpk3.
DR VEuPathDB; HostDB:ENSMUSG00000002007; -.
DR eggNOG; KOG1290; Eukaryota.
DR GeneTree; ENSGT00940000157877; -.
DR HOGENOM; CLU_000288_81_9_1; -.
DR InParanoid; Q9Z0G2; -.
DR OMA; IEKYEWP; -.
DR OrthoDB; 290680at2759; -.
DR PhylomeDB; Q9Z0G2; -.
DR TreeFam; TF105334; -.
DR BioGRID-ORCS; 56504; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q9Z0G2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z0G2; protein.
DR Bgee; ENSMUSG00000002007; Expressed in temporalis muscle and 147 other tissues.
DR ExpressionAtlas; Q9Z0G2; baseline and differential.
DR Genevisible; Q9Z0G2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0060537; P:muscle tissue development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Differentiation; Kinase; Myogenesis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..565
FT /note="SRSF protein kinase 3"
FT /id="PRO_0000086710"
FT DOMAIN 78..563
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 84..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 565 AA; 62365 MW; 34976D08141C5DC8 CRC64;
MSANAGGSGS VDCGGSSSSS QTSCGPESSG SELTPATPAP RLLQGLLGSD DEEQEDPKDY
CKGGYYPVKI GDLFNGRYHV VRKLGWGHFS TVWLCWDIQR KRFVALKVVK SAGHYTETAV
DEIKLLKCVR DSDPSDPKRE TIVQLIDDFR ISGVNGVHVC MVLEVLGHQL LKWIIKSNYQ
GLPVPCVKSI VRQVLHGLDY LHTKCKIIHT DIKPENILLC VGDAYIRRLA AEATEWQQSG
AQPPSRSTVS TAPQEVLIGK LSKNKRKKMR RKRKQQKRLL EERLRDLQRL EAMEAAVQAE
DSSSRLERGS GSTSSSGCHP EGTRAGPSPA SSSPVPGGER SLSPSSQTSG FSGSLFSTAS
CSILSGSSNQ RETGGLLSPS TPFGASNLLV NPLEPQNADK IKIKIADLGN ACWVHKHFTE
DIQTRQYRAV EVLIGAEYGP PADIWSTACM AFELATGDYL FEPHSGEDYS RDEDHIAHIV
ELLGDIPPAF ALSGRYSREF FNRRGELRHI PNLKHWGLYE VLMEKYEWPL EQATQFSAFL
LPMMEYIPEK RASAADCLQH PWLNP
