FER_CANLF
ID FER_CANLF Reviewed; 823 AA.
AC Q9TTY2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tyrosine-protein kinase Fer;
DE EC=2.7.10.2;
DE AltName: Full=Proto-oncogene c-Fer;
DE AltName: Full=p94-Fer;
GN Name=FER;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Prostate;
RX PubMed=10687853; DOI=10.1016/s0303-7207(99)00205-1;
RA Allard P., Zoubeidi A., Nguyen L.T., Tessier S., Tanguay S., Chevrette M.,
RA Aprikian A., Chevalier S.;
RT "Links between Fer tyrosine kinase expression levels and prostate cell
RT proliferation.";
RL Mol. Cell. Endocrinol. 159:63-77(2000).
CC -!- FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface
CC receptors for growth factors and plays a role in the regulation of the
CC actin cytoskeleton, microtubule assembly, lamellipodia formation, cell
CC attachment and cell migration. Acts downstream of EGFR, PDGFRA and
CC PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and
CC cell proliferation. Acts downstream of the activated FCER1 receptor and
CC plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-
CC mediated signaling in mast cells. Plays a role in the regulation of
CC mast cell degranulation. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1,
CC PECAM1 and PTPN11 (By similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Homotrimer. Interacts with CTNND1, EGFR, FLT3, IRS1, PECAM1,
CC PIK3R1 and PDGFR. Interacts (via SH2 domain) with CTTN. Component of a
CC complex that contains at least FER, CTTN and PTK2/FAK1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection
CC {ECO:0000250}. Cell junction {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cell cortex
CC {ECO:0000250}. Note=Associated with the chromatin. Detected on
CC microtubules in polarized and motile vascular endothelial cells.
CC Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1
CC and CTNND1 at nascent cell-cell contacts (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The coiled coil domains mediate homooligomerization and are
CC required for location at microtubules. {ECO:0000250}.
CC -!- DOMAIN: The N-terminal region including the first coiled coil domain
CC mediates interaction with phosphoinositide-containing membranes.
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF187884; AAF00543.1; -; mRNA.
DR RefSeq; NP_001003141.1; NM_001003141.1.
DR AlphaFoldDB; Q9TTY2; -.
DR SMR; Q9TTY2; -.
DR STRING; 9615.ENSCAFP00000011047; -.
DR PaxDb; Q9TTY2; -.
DR GeneID; 403754; -.
DR KEGG; cfa:403754; -.
DR CTD; 2241; -.
DR eggNOG; KOG0194; Eukaryota.
DR InParanoid; Q9TTY2; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; 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-KW.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:InterPro.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:InterPro.
DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IEA:InterPro.
DR CDD; cd07686; F-BAR_Fer; 1.
DR CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028539; Fer.
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 InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418:SF227; PTHR24418:SF227; 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 SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell junction; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Kinase; Lipid-binding; Membrane;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; SH2 domain; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..823
FT /note="Tyrosine-protein kinase Fer"
FT /id="PRO_0000260824"
FT DOMAIN 1..259
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 460..550
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 563..816
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..300
FT /note="Important for interaction with membranes containing
FT phosphoinositides"
FT /evidence="ECO:0000250"
FT COILED 123..185
FT /evidence="ECO:0000255"
FT COILED 301..390
FT /evidence="ECO:0000255"
FT ACT_SITE 684
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 569..577
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 402
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P16591"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16591"
FT MOD_RES 615
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P70451"
FT MOD_RES 714
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P70451"
SQ SEQUENCE 823 AA; 94611 MW; 33E88A6A15B37897 CRC64;
MGFGSDLKNS HEAVLKLQDW ELRLLETVKK FMALRIKSDK EYASTLQNLC NQVDKESTVQ
MNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSFIGVHQQ
IEAEMIKVTK TELEKLKSSY RQLIKEMNSA KEKYKEALAK GKETEKAKER YDKATMKLHV
LHNQYVLALK GAQLHQNQYY DTTLPLLLDS LQKMQEEMIK ALKGIFDEYS QITSLVTEEI
VNVHKEIQMS VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL
TAESLQVMLK TLAEELIQTQ QMLVNKEEAV LELEKRIEES SKTCEKKSDI VLLLSQKQTL
EELKQSVQQL RCTEAKFTAQ KELLEQKVQE NEGKEPPPVV NYEEDARSVT SMERKERLSK
FESIRHSIAG IIRSPKSALG SSTFSDTIPI SEKPLAEQDW YHGAIPRIEA QDLLKQQGDF
LVRESHGKPG EYVLSVYSDG QRRHFIIQFV DNLYRFEGTG FSNIPQLIDH HYTTKQVITK
KSGVVLLNPI PKDKKWVLNH EDVTLGELLG KGNFGEVYKG ILKDKTAVAV KTCKEDLPQE
LKIKFLQEAK ILKQYDHPNI VKLIGVCTQR QPIYIIMELV PGGDFLSFLR KKKDEIKLKQ
LVKFSLDAAS GMSYLESKNC IHRDLAARNC LVGENNVLKI SDFGMSRQED GGVYSSSGLK
QIPIKWTAPE ALNYGRYSSE SDVWSFGILL WETFSLGVCP YPGMTNQQAT EQVERGYRIS
APQHCPEDIF KIMMKCWDYK PENRPKFSEL QKELTVIKKK VTQ
