ID   DUSTY_STRPU             Reviewed;         953 AA.
AC   A2CI35;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Dual serine/threonine and tyrosine protein kinase {ECO:0000303|PubMed:17123648};
DE            EC=2.7.12.1 {ECO:0000250|UniProtKB:P16879};
DE   AltName: Full=Dusty protein kinase {ECO:0000303|PubMed:17123648};
DE            Short=Dusty PK {ECO:0000303|PubMed:17123648};
DE   AltName: Full=Receptor-interacting serine/threonine-protein kinase 5 {ECO:0000250|UniProtKB:Q6XUX3};
GN   Name=DSTYK {ECO:0000250|UniProtKB:Q6XUX3};
GN   Synonyms=RIPK5 {ECO:0000250|UniProtKB:Q6XUX3};
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1] {ECO:0000312|EMBL:ABD77594.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=17123648; DOI=10.1016/j.bbaexp.2006.10.004;
RA   Peng J., Dong W., Chen Y., Mo R., Cheng J.-F., Hui C.-C., Mohandas N.,
RA   Huang C.-H.;
RT   "Dusty protein kinases: primary structure, gene evolution, tissue specific
RT   expression and unique features of the catalytic domain.";
RL   Biochim. Biophys. Acta 1759:562-572(2006).
CC   -!- FUNCTION: May act as a positive regulator of ERK phosphorylation
CC       downstream of fibroblast growth factor-receptor activation. May induce
CC       both caspase-dependent apoptosis and caspase-independent cell death.
CC       May play a role in the embryonic development.
CC       {ECO:0000250|UniProtKB:Q4VSN1, ECO:0000250|UniProtKB:Q6XUX3}.
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=2.7.12.1;
CC         Evidence={ECO:0000250|UniProtKB:P16879};
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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:P16879};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC         Evidence={ECO:0000250|UniProtKB:P16879};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6XUX1}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q6XUX1}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q6XUX1}. Cell junction
CC       {ECO:0000250|UniProtKB:Q6XUX1}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; DQ419946; ABD77594.1; -; mRNA.
DR   RefSeq; NP_001091920.1; NM_001098450.1.
DR   AlphaFoldDB; A2CI35; -.
DR   SMR; A2CI35; -.
DR   STRING; 7668.SPU_008966-tr; -.
DR   EnsemblMetazoa; NM_001098450; NP_001091920; LOC581730.
DR   GeneID; 581730; -.
DR   KEGG; spu:581730; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_014116_0_0_1; -.
DR   InParanoid; A2CI35; -.
DR   OMA; SWLERIQ; -.
DR   OrthoDB; 254886at2759; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IBA:GO_Central.
DR   GO; GO:0048568; P:embryonic organ development; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR   GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; 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; 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.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell junction; Cell membrane; Cytoplasm;
KW   Developmental protein; Kinase; Membrane; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..953
FT                   /note="Dual serine/threonine and tyrosine protein kinase"
FT                   /id="PRO_0000374059"
FT   DOMAIN          665..926
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          932..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        791
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT                   ProRule:PRU10027"
FT   BINDING         671..679
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         694
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   953 AA;  108380 MW;  1769C6082B6BD2EA CRC64;
     MSSRRLGSSR ARGRDLAHEV KHFGGLTKHL KKIIFDSNNC LTELKTSDHF EEEVISTLVL
     PPVADEIVGK VTKNPPALVI FGQTYTSKAT LVNKIFREDL FQIVDDSDNN KTWRAVHLKY
     GSQRNTRLTL TNSFELLNEE PGSPVMRNSW TGIPRVEMLV KEEHQKDACM LSATTEATLN
     HPLLQCKLQI LVTPHNCPGI SISQAYNVCT HNVLPVLLYC FDKDQLSEEN LRDLQELQNC
     AGTLPILFVD CREPSEPLVA HRERRLVEDA HEDFDDDSAY DTDERIEGER ERHNGLDARL
     RRRCRPTPND RPSVIDQLSR AGFISSPEEN GRMRGVLDVF TIVNQVEDLH NSAAIVQFIR
     RSLQYYLIRC CTAMHDLHQH CMNLFITTAF DMQRDILVTP KRIEYARQRE NELFDSLKDL
     TNQKQEQLRS LIQSTVADMT EDLLEQAGNY RFTDLEVSQE GKIQSQKDIK RCTEQIQDLV
     LARLNACVVE KLIGSVELLR ESFLGTLQRC LASLEKIDGD LETSTTVALR QILNAAYQVE
     VSVRTSSSVV RIIWERMKEF FQSIKPFKTP TRVDTEWKRK VAQTMINNLD ESKLAKSICS
     QFRSRLNNSH ESFSTSLRQL EQKHSGRLEK TEEQRMKVRK VYAPRLARLA LESTSLRDMV
     LYGMPKLERE IGRGQYGVVY SCRSWGGVTH CAVKSVVPPD DKHWNDLAME FHYTRSIAEH
     DRIVAVIGSV IDHGYGGMGC SPAVLLLMER MQRDLHTAIK ANMELPERLH VALDVAEGVR
     YLHSLGLVHR DIKLKNVLLD KHDRGKITDL GFCKPEAMMS GSIVGTPIHM APELFSGKYD
     NSVDTYAFGI LLWYVCAGHV KLPQAFEQCA NKDHLWTSVK KGVRPERLRP QFDDASWNLM
     KSSWAGEPSE RPLLGEVQSK LQDIYTKALA KREAEGGGGG GAKEQQNLKS DTL