ID A0A2D0PWC1_ICTPU Unreviewed; 492 AA.
AC A0A2D0PWC1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Serine/threonine-protein kinase 3 {ECO:0000256|ARBA:ARBA00039973};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=stk3 {ECO:0000313|RefSeq:XP_017309716.1,
GN ECO:0000313|RefSeq:XP_017309717.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017309716.1};
RN [1] {ECO:0000313|RefSeq:XP_017309716.1, ECO:0000313|RefSeq:XP_017309717.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017309716.1,
RC ECO:0000313|RefSeq:XP_017309717.1};
RG RefSeq;
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_017309716.1; XM_017454227.2.
DR RefSeq; XP_017309717.1; XM_017454228.2.
DR STRING; 7998.ENSIPUP00000002440; -.
DR Ensembl; ENSIPUT00000002574; ENSIPUP00000002440; ENSIPUG00000001766.
DR Ensembl; ENSIPUT00000002580; ENSIPUP00000002446; ENSIPUG00000001766.
DR GeneID; 108256932; -.
DR KEGG; ipu:108256932; -.
DR CTD; 6788; -.
DR OMA; QRMANLD; -.
DR OrthoDB; 152877at2759; -.
DR Proteomes; UP000221080; Chromosome 24.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd21888; SARAH_MST2; 1.
DR CDD; cd06612; STKc_MST1_2; 1.
DR Gene3D; 1.10.287.4270; -; 1.
DR Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024205; Mst1_2_SARAH_domain.
DR InterPro; IPR049568; Mst2_SARAH.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011524; SARAH_dom.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF23; SERINE_THREONINE-PROTEIN KINASE 3; 1.
DR Pfam; PF11629; Mst1_SARAH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50951; SARAH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_017309716.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 26..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 438..485
FT /note="SARAH"
FT /evidence="ECO:0000259|PROSITE:PS50951"
FT REGION 300..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 492 AA; 56230 MW; E4B854DBF63CB1A0 CRC64;
MEQPVPKNKL KKLSEDSLTK QPEEVFDVLE KLGEGSYGSV FKAIHKESGQ VVAIKQVPVE
SDLQEIIKEI SIMQQCDSPY VVKYYGSYFK NTDLWIVMEY CGAGSVSDII RLRNKTLTED
EIATILKSTL KGLEYLHFMR KIHRDIKAGN ILLNTEGHAK LADFGVAGQL TDTMAKRNTV
IGTPFWMAPE VIQEIGYNCV ADIWSLGITS IEMAEGKPPY ADIHPMRAIF MIPTNPPPTF
RKPELWSDEF TDFVKKCLVK NPEQRATATQ LLQHPFITSA KPVTILRDLI TEAMEMKVKR
QQEQQRELEE EDDNSEEEVE VDSHTMVKSG SESAGTMRAT GTMSDGAQTM IEHGSTMLES
DLGTMVINSD EEDEDEDVGS MRRNPTVPQA QRPSFMDYFD KQDSNKAQES YNHNQQDPYH
MPKTAFPDNW KVPQDGDFDF LKNLDFEELQ MRLSALDPMM EREIEELRQR YTAKRQPILD
AMDAKKRRQQ NF
//