ID K7FW08_PELSI Unreviewed; 823 AA.
AC K7FW08;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000632};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000632};
GN Name=FER {ECO:0000313|Ensembl:ENSPSIP00000012218.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000012218.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000012218.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|PIRNR:PIRNR000632};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|PIRNR:PIRNR000632}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily. {ECO:0000256|PIRNR:PIRNR000632}.
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DR EMBL; AGCU01125986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01125995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FW08; -.
DR STRING; 13735.ENSPSIP00000012218; -.
DR Ensembl; ENSPSIT00000012277.1; ENSPSIP00000012218.1; ENSPSIG00000010925.1.
DR eggNOG; KOG0194; Eukaryota.
DR GeneTree; ENSGT00940000154997; -.
DR HOGENOM; CLU_005265_0_0_1; -.
DR OMA; NQFQQLT; -.
DR TreeFam; TF315363; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:Ensembl.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IEA:Ensembl.
DR GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IEA:Ensembl.
DR GO; GO:0050904; P:diapedesis; IEA:Ensembl.
DR GO; GO:0035426; P:extracellular matrix-cell signaling; IEA:Ensembl.
DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0038109; P:Kit signaling pathway; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010762; P:regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0036119; P:response to platelet-derived growth factor; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR CDD; cd07686; F-BAR_Fer; 1.
DR CDD; cd05085; PTKc_Fer; 1.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR037452; Fer_F-BAR.
DR InterPro; IPR035849; Fes/Fps/Fer_SH2.
DR InterPro; IPR011009; Kinase-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; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016250; Tyr-prot_kinase_Fes/Fps.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF227; TYROSINE-PROTEIN KINASE FER; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF000632; TyrPK_fps; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000632, ECO:0000256|PIRSR:PIRSR000632-
KW 2};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|PIRNR:PIRNR000632};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR000632};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000632};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000632,
KW ECO:0000256|PIRSR:PIRSR000632-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000632};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000632}.
FT DOMAIN 1..259
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 459..549
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 562..818
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 386..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..167
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 316..380
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 685
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-1"
FT BINDING 568..576
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2"
FT BINDING 590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 823 AA; 94781 MW; 28F75B68D7128C61 CRC64;
MGFGSDLKYS HDALLKLQDW ELRLLETVKK FMAMRVKSDK EYASTLQNLC NQVDKESTSQ
LDYISNVSKS WLLMVQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYIGVHQQ
IEAEMFKVTK TELEKLKSSY RQLIKEVNSA KEKYKEAVAK GKETERAKDR YDKATMKLHM
LHNQYVLALK GAQLHQHQYY DTTLPLLLDS LQKMQEEMVN ALKGILDEYS QITSLVTEEI
VNVHKEIQTS VEQIDPSSEY SSFIEAHRSP ENVEQEIVFD TSLLEENENL QANEIMWNNL
TAESLQGMLK TVIEELVQTQ RTLLNKEELV LELEKKIEES STTCGKKSDI VLLLSQKQAL
EELKQTVQQL RCSEAKFTAQ KELLEQKVQE NDGKEPPPVV TYEEDDRSVT SMDKKDKVSR
FETSSKIHAG LFISKYLQWS VLFFDVISTS EKPLAEQDWY HGAIPRIEAQ ELLKQQGDFL
VRESHGKPGE YVLSVFSDGQ RRHFIIQYAD NQYRFEGTGF PTIPQLIEHH YTTKNVITKK
SGVVLLNPVV KDKKWVLNHE DVTLGELLGK GNFGEVYKGT LKDKTPVAVK TCKEDLPQEL
KIKFLSEARI LKQYDHPNIV KLIGVCTQRQ PIYIVMELIP GGDFLSFLRK KKDELKTKQL
VKFSLDAAAG MAYLESKNCI HRLRDLAARN CLVGENNVLK ISDFGMSRQE DDGVYSSSGL
KQIPIKWTAP EALNYGRYTS ESDVWSFGIL LWETFSLGVC PYPGMTNQQA REQVEKGYRM
PAPQKCPEEI YKIMQRCWDY KPENRPKFSE IQKELSSIKK KVT
//
