ID W5MJ89_LEPOC Unreviewed; 1107 AA.
AC W5MJ89;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Tyrosine kinase, non-receptor, 2b {ECO:0000313|Ensembl:ENSLOCP00000008448.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008448.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000008448.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AHAT01015249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01015250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MJ89; -.
DR STRING; 7918.ENSLOCP00000008448; -.
DR Ensembl; ENSLOCT00000008458.1; ENSLOCP00000008448.1; ENSLOCG00000006982.1.
DR eggNOG; KOG0199; Eukaryota.
DR GeneTree; ENSGT00940000165248; -.
DR InParanoid; W5MJ89; -.
DR OMA; KSWMSKX; -.
DR Proteomes; UP000018468; Linkage group LG14.
DR Bgee; ENSLOCG00000006982; Expressed in bone element and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; IBA:GO_Central.
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; cd00174; SH3; 1.
DR CDD; cd14274; UBA_ACK1; 1.
DR CDD; cd14328; UBA_TNK1; 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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR030220; Ack1_UBA_dom.
DR InterPro; IPR015116; Cdc42-bd-like.
DR InterPro; IPR037085; Cdc42-bd-like_dom_sf.
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; PF14604; SH3_9; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 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.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR630220-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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 Reference proteome {ECO:0000313|Proteomes:UP000018468};
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}.
FT DOMAIN 142..401
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 404..464
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1054..1099
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-1"
FT BINDING 148..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1107 AA; 124487 MW; 8EB433D3E09F52AE CRC64;
MNCSDRKSFV TESQQKKLGS SMQSDEGTEW LLELLMEVQL QQYFLRIRDD LNVTRLSHFD
YVKNEDLEKI GMGRPGQRRL WEAVKRRKAM CKRKSWMSKV FSGKRPESEF QPQPATTFRK
ISTPPPPEGQ QALTCLISEK DLSLFEKLGD GSFGVVKRGE WSAPNGKVIH VAVKCLKTDV
LNQPDALDDF IREVNAMHSL DHQNLIRLYG VVLTHPMKMV TELAPLGSML DRLRKNQGHF
LISTLCQYAI QISNGMAYLE SKRFIHRDLA ARNILLAAND LVKIGDFGLM RALPKNDDHY
VMQEHRKVPF AWCAPESLKT RTFSHASDTW MFGVTLWEMF TYGQEPWLGL NGSQILHKID
KEGERLSKPE DCPQDIYNVM LQCWAQKPDD RPTFVALREF LVETMPTDMR ALQDFEEPDK
LEIQIDDVIT IIEGRAENYW WRGQNKRTLN VSQFPRNTVT SVAGLSAHDI SRPLKNSFIH
TGHGDTNPHR SWGFPDKIDD LYLGNPMDPP DVLGMDFNTA RPTQLPGRAK KEPPPRPPQP
VILVKKPCYD PVTEEDDLTA SGLKKLYLKK PGSVKGLKLA KPAAWVSATK TGDRQSCGAR
SAGANEVSLI DFEEEVPPST PSPVVEKQIP VLAKLVLEAD SILDKTPPQS PTRILPRPLH
PTPVVDWDSK PLPAPPAYDD VAQDEEDIEV SSINSSEPSL LDDPSKYRLA RAQKVKESGE
PSVSFVQEGD TVDKPKVEDN LFLPCRQNPQ NNFSQSAEIF EELQQECMKR LNVPVVTSLP
SSPSPNSLDV HKHIVLSFSE DKPQIPPRIP IPPRPMKRND YGRWSGDLSP SSGGEEDKDK
PPQIPPRDPL SQPNSRTPSP MSLHVGSPQQ RTSLCSAASF GSYLSTSPSK LMPTTQSFAS
DPKYATPKVI QAQGKDCAKG PCILPIVKDG KKVSSTHYYL LPERPPYLDK YEKFFKEAES
PEDSSSRRTV TTATVRPMMQ QSDLRANFSS NNSNTHGVKT TAKTPYSLQR VNCDGQAGKS
ESARSMDKVK LVQDAVHGVT IEECRAALHN HGWNVQKAVH YLKVEQLFCL GLKTRAECLK
MLETYDWNLE LASSQLLDSY GTVRQRR
//
