ID A0A087XEM3_POEFO Unreviewed; 1071 AA.
AC A0A087XEM3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=PTK2 {ECO:0000313|Ensembl:ENSPFOP00000004226.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000004226.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000004226.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001149};
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004413}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; AYCK01010446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01010447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01010448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087XEM3; -.
DR STRING; 48698.ENSPFOP00000004226; -.
DR Ensembl; ENSPFOT00000004234.2; ENSPFOP00000004226.2; ENSPFOG00000003397.2.
DR eggNOG; KOG4257; Eukaryota.
DR GeneTree; ENSGT00940000155113; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005925; C:focal adhesion; 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:0008284; P:positive regulation of cell population proliferation; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13190; FERM_C_FAK1; 1.
DR CDD; cd05056; PTKc_FAK; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.5.540; Single helix bin; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR041390; FADK_N.
DR InterPro; IPR049385; FAK1-like_FERM_C.
DR InterPro; IPR041784; FAK1/PYK2_FERM_C.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR036137; Focal_adhe_kin_target_dom_sf.
DR InterPro; IPR005189; Focal_adhesion_kin_target_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46221; FERM AND PDZ DOMAIN-CONTAINING PROTEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR46221:SF11; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR Pfam; PF21477; FERM_C_FAK1; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF18038; FERM_N_2; 1.
DR Pfam; PF03623; Focal_AT; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF68993; FAT domain of focal adhesion kinase; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 67..388
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 472..730
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 747..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1071 AA; 121581 MW; 8D1B6DADD4D5318F CRC64;
MEGLYHDISR IAYYTEYDRH LAAAVSAGKT MATAYMDPNL NNAFLAGAKS RLSAGGSDRT
MAGSVDRVLK VFHYFETNTE HSFWSSNIRY GDATDVRGII QKILDINKVR WTSCFGLRLS
NSQSRDQLHW LHPDMGVSHI REKYEQARPN EEWRYELRIR YLPKGFVQQF TEDKPTLNYF
YHQVKNDYMT QYGDQVEQDV ALKLGCLEIR RFFKEMRGNA LDKKSNYELL EKDVGLRRFF
PKDLLDSVKA KTLRKLIQQT FKQVANLNDE QCILKFLEIL ASIYRYDKEL FKCALGSSWV
IQVELAIGPE EGISYLTDKG STPTHLANFN QVQSIQYSAM EEKDRKGMLQ LNVAGAAEPL
TVTTASLTTA ENLADLIDGY CRLVSMETHS FIVRVQKEGE RALPSIPKVS NNEKKLEAVR
SGVRTISVSE DLSGDETDDY AEIVDEEDTY TMPSMSYGVV EARDYEIQRD RIELGRCIGE
GQFGDVHQGV YSCPDKPPLP VAIKTCKNCT TDSVREKFLQ EALTMRQFDH PHIVKLIGVI
TENPVWIIME LCTLGELRSF LQVKKYSLDL ATLILFSYQL STALAYLESK RFVHRDIAAR
NVLVSSVDCV MLGDFGLSRY MEDSSYYKAS KGKLPIKWMA PESINFRRFT SASDVWMFGV
CMWEILMYGI KPFQGVKNND VIGRIENGER LAMPPQCPPT LYSLMTKCWS YDPSKRPRFT
ELKTQLSVIL TEEKGLQEER LREEMRRQVT VSWDSGGSDE APPKPSRPGY PSPRASESFF
SNHFQPSPGG VGGVGGSYSS SDSWNQLRPE HAPLWNPTME ERLDVNQALM EETLIKQQQE
MEEDRRWLEQ KESHMKPESR NSRGSIDRED GTLQTPGGSP HIYQPVGKPE HVAPPKKPPR
PGAHLPNLAN LSPVDSYNDG VKLQPQEISP PPTANLDRSN DKVYENVTGL VKAVIEMSNR
IQPAAPEEYV PMVKDVGLAL RTLLATVDET IPVLPASTHR EIEMAQKLLN SDLAELISKM
KLAQQYVMTS LQKDYKKQML MAAHALAVDA KNLLDVIDQS RLKMISQIRP Q
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