ID A0A7J8A3W9_MYOMY Unreviewed; 1120 AA.
AC A0A7J8A3W9;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE RecName: Full=Activated CDC42 kinase 1 {ECO:0000256|ARBA:ARBA00072244};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Tyrosine kinase non-receptor protein 2 {ECO:0000256|ARBA:ARBA00077194};
GN ORFNames=mMyoMyo1_019533 {ECO:0000313|EMBL:KAF6380700.1};
OS Myotis myotis (Greater mouse-eared bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6380700.1, ECO:0000313|Proteomes:UP000527355};
RN [1] {ECO:0000313|EMBL:KAF6380700.1, ECO:0000313|Proteomes:UP000527355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6380700.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6380700.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000256|ARBA:ARBA00004132}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}. Membrane, clathrin-coated pit
CC {ECO:0000256|ARBA:ARBA00004600}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00060742}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6380700.1}.
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DR EMBL; JABWUV010000002; KAF6380700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8A3W9; -.
DR VEuPathDB; HostDB:GeneID_118675417; -.
DR Proteomes; UP000527355; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IEA:TreeGrafter.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; IEA:TreeGrafter.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd05040; PTKc_Ack_like; 1.
DR CDD; cd09539; SAM_TNK-like; 1.
DR CDD; cd14274; UBA_ACK1; 1.
DR CDD; cd14328; UBA_TNK1; 1.
DR FunFam; 4.10.680.10:FF:000001; activated CDC42 kinase 1 isoform X1; 1.
DR FunFam; 1.10.8.10:FF:000048; activated CDC42 kinase 1 isoform X2; 1.
DR FunFam; 1.10.510.10:FF:000080; Putative activated CDC42 kinase 1; 1.
DR FunFam; 3.30.200.20:FF:000107; Putative activated CDC42 kinase 1; 1.
DR Gene3D; 4.10.680.10; Cdc42-like binding domain; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR055175; ACK/TNK-like_SAM.
DR InterPro; IPR030220; Ack1_UBA_dom.
DR InterPro; IPR015116; Cdc42-bd-like.
DR InterPro; IPR037085; Cdc42-bd-like_dom_sf.
DR InterPro; IPR052112; EGFR_SigReg_Kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021619; Mig-6.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR049587; TNK-like_SAM.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR14254; GENE 33 POLYPEPTIDE; 1.
DR PANTHER; PTHR14254:SF6; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR Pfam; PF09027; GTPase_binding; 1.
DR Pfam; PF11555; Inhibitor_Mig-6; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF22931; SAM_TNK; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR630220-
KW 2}; Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KAF6380700.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR630220-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000313|EMBL:KAF6380700.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000527355};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 205..464
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 467..527
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 14..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..830
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..864
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..893
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-1"
FT BINDING 211..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1120 AA; 123125 MW; 64EB6FBF78547847 CRC64;
MCFSGPALLL DSRLEDAQAR PRRTQGSDAA GAAGGAGAAG GRCSPPGLNA GSLGSMGERA
AYQRLTRGEE VLQRLGSSSM QPEEGTGWLL ELLSEVQLQQ YFLRLRDDLN VTRLSHFEYV
KNEDLEKIGM GRPGQRRLWE AVKRRKAMCK RKSWMSKVFS GKRLEAEFPP HHSQSAFPKT
SPTPGGPAGE GPLQSLTCLI GEKDLHLFEK LGDGSFGVVR RGEWDAPSGK TVSVAVKCLK
PDVLSQPEAM DDFIREVNAM HSLDHRNLIR LYGVVLTPPM KMVTELAPLG SLLDRLRKHQ
GHFLLGTLSR YAVQVAEGMG YLESKRFIHR DLAARNLLLA TRDLVKIGDF GLMRALPQND
DHYVMQEHRK VPFAWCAPES LKTRTFSHAS DTWMFGVTLW EMFTYGQEPW IGLNGSQILH
KIDKEGERLP RPEDCPQDIY NVMVQCWAHK PEDRPTFVAL RDFLLEAQPT DMRALQDFEE
PDKLHIQMND VITVIEGRAE NYWWRGQNTR TLCVGPFPRN VVTSVAGLSA QDISQPLQNS
FIHTGHGDSD PRHCWGFPDK IDELYLGNPM DPPDLLSVEL STSRPTQHLG RVKKPTYDPV
SEDQDPLSSD FKRLGVRKPG LPRGLWLTKP SARVSGTKTG RGGSSGAEVT LIDFGEEPVV
PSPRPCTPSL AQLAMDACSL LDKTPPQSPT RALPRPLHPT PVVDWDARPL PPPPAYDDVA
QDEDDFEVCS INSTLVGAGV SPGPSQGETN YGFVPEQARL LAPLEDNLFL PPQGGSKPPT
SAQTAEIFQA LQQECMLRLQ VPASSLVLSP SPVGEDKPQV PPRVPIPPRP TRPRGELSPA
PSGEEETGRW PGPASPPRVP PREPLSPQSS RTPSPLVPRG SSPLPPRLSS SPGKTMPTTQ
SFASDPKYAT PQVIQAPGPR AGPCILPIVR DGKKVSNTHY YLLPERPPYL ERYQRFLREA
QSPEEPAPLP VPLLPPPSTP APAAPTATVR PMPQAAPDPK ANFSTNNSNP GVRPPALRAT
AWLSQRGCPG DGPEAVRPTD KIQMLQAMVH GVTTEECQAA LQSHSWNVQR AAQYLKVEQL
FGLGLRPRGE CHKVLEMFDW NLEQAGCHLL GSCGPAHHKR
//
