SRPK3_PIG
ID SRPK3_PIG Reviewed; 566 AA.
AC B8Y466;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Landrace; TISSUE=Muscle;
RX PubMed=20127522; DOI=10.1007/s11033-010-9952-1;
RA Xu Y., Yu W., Xiong Y., Xie H., Ren Z., Xu D., Lei M., Zuo B., Feng X.;
RT "Molecular characterization and expression patterns of serine/arginine-rich
RT specific kinase 3 (SPRK3) in porcine skeletal muscle.";
RL Mol. Biol. Rep. 38:2903-2909(2011).
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 (By similarity).
CC {ECO:0000250}.
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: Highly expressed in skeletal muscle, heart, uterus
CC and parorchis. Weakly expressed in brain, stomach, small intestine and
CC ovary. {ECO:0000269|PubMed:20127522}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; FJ477853; ACK77781.1; -; mRNA.
DR EMBL; GQ428209; ACU57054.1; -; mRNA.
DR EMBL; GQ450279; ACV85727.1; -; Genomic_DNA.
DR RefSeq; NP_001137591.1; NM_001144119.1.
DR AlphaFoldDB; B8Y466; -.
DR SMR; B8Y466; -.
DR STRING; 9823.ENSSSCP00000021611; -.
DR PaxDb; B8Y466; -.
DR PRIDE; B8Y466; -.
DR GeneID; 100240720; -.
DR KEGG; ssc:100240720; -.
DR CTD; 26576; -.
DR eggNOG; KOG1290; Eukaryota.
DR InParanoid; B8Y466; -.
DR OrthoDB; 290680at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0060537; P:muscle tissue development; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Developmental protein; Differentiation; Kinase; Myogenesis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..566
FT /note="SRSF protein kinase 3"
FT /id="PRO_0000406987"
FT DOMAIN 79..564
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..279
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 85..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0G2"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0G2"
SQ SEQUENCE 566 AA; 61905 MW; ADC68F4E294CB6EC CRC64;
MSASTGGGGG GDSGSSSSSS SQASCGPEPS GSELAPPTPA PRMLQGLLGS DDEEQEDPKD
YCKGGYYPVK IGDLFNGRYH VVRKLGWGHF STVWLCWDIQ RKRFVALKVV KSAGHYTETA
VDEIKLLKCV RDSDPSDPKR ETIVQLIDDF RISGVNGVHV CMVLEVLGHQ LLKWIIKSNY
QGLPVPCVKS IVRQVLHGLD YLHTKCKIIH TDIKPENILL CVGDAYIRRL AAEATEWQQS
GAPPPSRSTV STAPQEVLSG KLSKNKRKKM RRKRKQQKRL LEERLRDLQR LEAMEAAAQA
EDSGSRLEGG SGSTSSSGCH PGGAGPGPSP ASSSPAPGGD RSLSPGSQTS GFSGSLFSPA
SCSILSGSSN QRETGGLLSP STPFGASNLL VNPLEPQNAD KIRIKIADLG NACWVHKHFT
EGIQTRQYRA VEVLIGAEYG PPADIWSTAC MAFELATGDY LFEPHSGEDY SRDEDHIAHI
VELLGDIPPA FALSGRYSRE FFNRRGELRH IHNLKHWGLY EVLMEKYEWP LEQATQFSAF
LLPMMEYIPE KRASAADCLQ HPWLNP
