DUSTY_APIME
ID DUSTY_APIME Reviewed; 969 AA.
AC Q1L6Q1; Q1L6Q0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
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, ECO:0000312|EMBL:AAY81955.1};
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 Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAY81955.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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 -!- 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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:17123648};
CC IsoId=Q1L6Q1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:17123648};
CC IsoId=Q1L6Q1-2; Sequence=VSP_053089, VSP_053090;
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; DQ013067; AAY81955.1; -; mRNA.
DR EMBL; DQ013068; AAY81956.1; -; mRNA.
DR RefSeq; NP_001071281.1; NM_001077813.1. [Q1L6Q1-1]
DR AlphaFoldDB; Q1L6Q1; -.
DR SMR; Q1L6Q1; -.
DR STRING; 7460.GB40067-PA; -.
DR PaxDb; Q1L6Q1; -.
DR EnsemblMetazoa; NM_001077813; NP_001071281; GeneID_412747. [Q1L6Q1-1]
DR GeneID; 412747; -.
DR KEGG; ame:412747; -.
DR CTD; 412747; -.
DR eggNOG; KOG0192; Eukaryota.
DR InParanoid; Q1L6Q1; -.
DR OrthoDB; 254886at2759; -.
DR PhylomeDB; Q1L6Q1; -.
DR Proteomes; UP000005203; Unplaced.
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 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 Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..969
FT /note="Dual serine/threonine and tyrosine protein kinase"
FT /id="PRO_0000374060"
FT DOMAIN 632..894
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 904..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..37
FT /evidence="ECO:0000255"
FT COMPBIAS 904..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 760
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 638..646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 662
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6XUX3,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17123648"
FT /id="VSP_053089"
FT VAR_SEQ 39..41
FT /note="FPE -> MFT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17123648"
FT /id="VSP_053090"
SQ SEQUENCE 969 AA; 110428 MW; CBE73908BE56C06D CRC64;
MVSKLPQEFR RYLRNRNQLQ HVLEETQQAL ELINLENFFP EENVVEELLS PLTLNRITHI
LANSPAIIIL GQDSKAKAIV VNTLISNDIL PVCNGLWRWI RLTYGQTNHI SLTLDLEYEL
VENLQANEKP WSTLPIEDLT KSDNEDITYP TVLEVQLNLP ILKDGVQIFI APNNGAVKVL
ANEFLSILPI FLYALGEQPL TEQNLEELRD LKETYPFNPV LFISSLENIS LNGIDPELTE
SEQHRLQNRL YTNDSTSSKT DDDSIDFDRM NSLGLSWLDQ LTNLGFLGMK ESVEVDQLSW
LGSGQYISDF VGSCRKTDQI LYFIRGCLQT YLINASTYLN EVHTASLRKF ILSAFDMARI
IQITPKRIQY AQHKENELYA NLMKIVHEKQ QEITGLIQNI IQEMKNDVLL SNNDVYLYQN
TMSNNNQRTE WSATVKAAIS EVQRVVLGRL CEKVAKQLVN SVNCLRESFI GTLQRCLLSL
EKTYERDTCL LASDALKQIL SAAYNVELHN SSPFSIYSFL ERLNLIFMSS SLQWSSTHTL
DVAWRRKVTI EILNSLSATK LSKIILMQFG DKLESSHDSF QAALRSIENY YSGKLERTEE
QRIALRKYHA PRLAKLALES TSMIDVVRYG KPHCAEEIGR GQYGIVFACD GWGGKAGPCA
IKSVVPSDES HWNDLAMEFY YNRSIPDHKR IVKLRGSIID HSYGGGFGFG SAVLLISDRL
SRDLYCGIRA GLSWLERIQI ALDVLEGIRY LHSQGLVHRD VKLKNVLLDI ENRAKLTDFG
FCITEVMMLG SIVGTPVHMA PELLSGHYDS SVDVYAFGIL FWYLCAGHVR LPYTFEQFHN
KELLWTSVKK ALMIVGIRPE RLPSFDDECW RLMEQCWSGE PSKRPLLGAI VPVLESIQQK
AKRSKSLQEV SSDKLQESST DSRNPALALA EPYNQRGTVV SPPPTKRRTM KVVKYHLFLT
NLYIQMREL
