ID A0A3P8WN09_CYNSE Unreviewed; 1059 AA.
AC A0A3P8WN09;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Tyrosine kinase, non-receptor, 2b {ECO:0000313|Ensembl:ENSCSEP00000028838.1};
OS Cynoglossus semilaevis (Tongue sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC Cynoglossinae; Cynoglossus.
OX NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000028838.1, ECO:0000313|Proteomes:UP000265120};
RN [1] {ECO:0000313|Ensembl:ENSCSEP00000028838.1, ECO:0000313|Proteomes:UP000265120}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24487278;
RA Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA Zhao Y., Schartl M., Tang Q., Wang J.;
RT "Whole-genome sequence of a flatfish provides insights into ZW sex
RT chromosome evolution and adaptation to a benthic lifestyle.";
RL Nat. Genet. 46:253-260(2014).
RN [2] {ECO:0000313|Ensembl:ENSCSEP00000028838.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3P8WN09; -.
DR Ensembl; ENSCSET00000029233.1; ENSCSEP00000028838.1; ENSCSEG00000018456.1.
DR GeneTree; ENSGT00940000165248; -.
DR Proteomes; UP000265120; Chromosome 20.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd05040; PTKc_Ack_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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR630220-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
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:UP000265120};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 70..331
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 334..394
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 442..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-1"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1059 AA; 117527 MW; F16BC1236F94A3F8 CRC64;
MCKRKSWMSK VFSAKRLDGG DFPQQGQLAS SFRKLSPTPP LSLGDAVLSP QTGSEGQQQA
LTCLILEKDL TLFEKLGDGS FGVVKRGEWL TPAGRVVNVA VKCLKTDVLS QPDALEDFIC
EVNAMHSLDH QNLIRLYGVV LTHPMKMVTE LAPLGSLLCR LRRVHPQGPV LIHTLCQYAV
QVACGMAYLE QRRFIHRDLA ARNILLASAQ TVKIGDFGLM RALPNNHEHY VMQEHRKVPF
AWCAPESLKT RTFSHATDTW MFGVTLWEMF TQGQEPWVGL NGSQILHKLD KEGERLPKPE
DCPQDVYNVM SQCWAQKPED RPTFVALREF LLETMATDMC ALQDFSEADK LLIQVNDVIT
IIEGRAENYW WRGQNKRTTK VGQFPRNVVT SVAGLSAHDI SRPLKNSFIH TGHGETNPHR
CWGFPDRIDD LYLGNPMNPP DVLGLDVTSA QQPQPPGGTK KPCYDPVNED DNHTSAGLKR
LSLRKTGSMR ALKIKPSVRV SGSKQGSTSS SGHNQNSEPS LIDFGEEFLP STSCSSPVVE
IQIPFLAKLA LEAENILDRT PPQSPSKSLP RPLHPTPIVD WDARPLPPPP AYDDVAQDED
DMEVSSINRA EQRLEKEHRD VFNQDETGLY SGPKMQIEAH VSRDPGLEDN LFRPNKRSGG
LSASFSQSVE IFQELQQECM RRLNVPKGLT ARSCTPPQTL TLCPLTSQTL QTPEEDRESV
PSSGENKPQI PPRIPIPPRP VKRGDYTSVR WSGDLSLSPT PANATENISA PDQNLPPQIP
PRDPLSQSGS RTPSPMGLIV GSPQQRPYPV NHTAVHSPTH TYGTYLSTSP SKLMATTHSF
TSDPKYAAPK VIQSQGRDPA AKGPCILPIV RDGRKVSNTH YYLLPERPPY LDRYNRFLRK
AESLSLPSVE DRQEQQQAAN TATVRPMVIS SSSSSSSSSS RPTSQGHIQV PGLFYPDGLT
TAVVGAPCTK TDGGENSAEK IKMVQEAVHG VTIEECQAAL WKHKWNVQRA VQFLKVEQLF
CLGLRSRAEC LQLLATCDWN LELASTQMLD NYGSSRQRR
//