ID A0A5F9D844_RABIT Unreviewed; 848 AA.
AC A0A5F9D844;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000632};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000632};
GN Name=FES {ECO:0000313|Ensembl:ENSOCUP00000042379.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000042379.1, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000042379.1, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000042379.1}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000042379.1};
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface
CC receptors and plays a role in the regulation of the actin cytoskeleton,
CC microtubule assembly, cell attachment and cell spreading. Plays a role
CC in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated
CC signaling in mast cells. Acts down-stream of the activated FCER1
CC receptor and the mast/stem cell growth factor receptor KIT. Plays a
CC role in the regulation of mast cell degranulation. Plays a role in the
CC regulation of cell differentiation and promotes neurite outgrowth in
CC response to NGF signaling. Plays a role in cell scattering and cell
CC migration in response to HGF-induced activation of EZR. Phosphorylates
CC BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1,
CC PECAM1, STAT3 and TRIM28. {ECO:0000256|ARBA:ARBA00058669}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00051245,
CC ECO:0000256|PIRNR:PIRNR000632};
CC -!- SUBUNIT: Homooligomer. Interacts with BCR. Interacts (when activated,
CC via coiled coil domain) with TRIM28. Interacts (via SH2 domain) with
CC phosphorylated EZR, MS4A2/FCER1B and HCLS1/HS1. Interacts with
CC phosphorylated KIT. Interacts with FLT3. Interacts (via F-BAR domain)
CC with soluble tubulin. Interacts (via SH2 domain) with microtubules.
CC {ECO:0000256|ARBA:ARBA00065982}.
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 AlphaFoldDB; A0A5F9D844; -.
DR Ensembl; ENSOCUT00000064243.1; ENSOCUP00000042379.1; ENSOCUG00000002188.4.
DR GeneTree; ENSGT00940000158881; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000002188; Expressed in blood and 18 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; 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 CDD; cd07685; F-BAR_Fes; 1.
DR CDD; cd10361; SH2_Fps_family; 1.
DR FunFam; 1.10.287.160:FF:000006; Tyrosine-protein kinase; 1.
DR FunFam; 1.10.510.10:FF:000212; Tyrosine-protein kinase; 1.
DR FunFam; 1.20.1270.60:FF:000030; Tyrosine-protein kinase; 1.
DR FunFam; 3.30.200.20:FF:000089; Tyrosine-protein kinase; 1.
DR FunFam; 3.30.505.10:FF:000020; Tyrosine-protein kinase; 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; 3.30.200.20; Phosphorylase Kinase, domain 1; 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; IPR035849; Fes/Fps/Fer_SH2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR050198; Non-receptor_tyrosine_kinases.
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; TYROSINE-PROTEIN KINASE; 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; PR00109; TYRKINASE.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00219; TyrKc; 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; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000632};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000632};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
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..258
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 486..575
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 587..848
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 393..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 133..160
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 709
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-1"
FT BINDING 593..601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2"
FT BINDING 616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 848 AA; 96374 MW; ED7420B64D24FAEA CRC64;
MGFSSELCSP QGHGAVQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH MSTQDGGGQS
RGPDSPISQS WAEITSQTEG LSRLLRQHAE DLNSGPLSKL SLLIRERQQL RKTYSEQWQQ
LQQELTKTHS QDIEKLKSQY RALARDSAQA RRKYQEASKD KDRDKAKDKY VRSLWKLFAQ
HNRYVLGVRA AQLHHQHHYQ LLLPGLLQSL QDLHEEMARV LKEILQEYLE ISSLVQEEVV
AIHREMAAAA ARIQPEAEYQ GFLRQYGSVP DIPPCVTFDE SLLEEGEQLE PGELQLNELT
VESVQHTLTS VTDELATASQ VVLSRQEVVT QLQRELQEEE QNTHPRARVQ LLGKKQALQE
ALQGLQGALC TQAKLQAQQE LLQAKLEQLG PGEPPPVLLL QDDRHSTSSS VSRRRCRCAR
RPPPPQAWPP ADVYPWPQEQ EREGGRTPTL EILRTHISGI FRPKFSLPPP LQLVPEVQKP
LHEQLWYHGA IPRAEVAELL THCGDFLVRE SQGKQEAVLS VLWDGLPRHF IIQSSDNLYR
LEGDGFPSIP LLIDHLLRSQ QPLTKKSGVV LRRAVPKDKW VLKHEDLVLG EQIGRGNFGE
VFSGRLRADN TLVAVKSCRE TLPPDLKAKF LQEARILKQY SHPNIVRLIG VCTQKQPIYI
VMELVQGGDF LTFLRTEGGR LRVKTLLQMV GDAAAGMEYL ESKCCIHRDL AARNCLVTEK
HVLKISDFGM SREEADGIYA ASGGLRQVPV KWTAPEALNY GRYSSESDVW SFGILLWETF
SLGASPYPNL SNQQTREFVE KGGRLPCPEL CPDAVFRLME QCWAHEPGQR PNFSTIYQEL
QSIRRRHR
//
