ID A0A2K5LPX7_CERAT Unreviewed; 757 AA.
AC A0A2K5LPX7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:ENSCATP00000014983.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000014983.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000014983.1}
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|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 AlphaFoldDB; A0A2K5LPX7; -.
DR Ensembl; ENSCATT00000039132.1; ENSCATP00000014983.1; ENSCATG00000031329.1.
DR GeneTree; ENSGT00940000158881; -.
DR OMA; QNTENMY; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000031329; Expressed in spleen and 10 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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07685; F-BAR_Fes; 1.
DR CDD; cd05084; PTKc_Fes; 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; 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; 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; 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 PANTHER; PTHR24418:SF197; TYROSINE-PROTEIN KINASE FES_FPS; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000632; TyrPK_fps; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000632, ECO:0000256|PIRSR:PIRSR000632-
KW 2}; Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000632};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR000632};
KW Kinase {ECO:0000256|PIRNR:PIRNR000632};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000632,
KW ECO:0000256|PIRSR:PIRSR000632-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Transferase {ECO:0000256|PIRNR:PIRNR000632};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000632}.
FT DOMAIN 1..265
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 496..757
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 399..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 618
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-1"
FT BINDING 502..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000632-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 757 AA; 85816 MW; BD06A49FD94A2DCE CRC64;
MGFSSELCTP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH MSVQDSGGQS
RGISPDSPIS QSWAEITSQT EGLSRLLRQH AEDLNSGPLS KLSLLIRERQ QLRKTYSEQW
QQLQQELTKT HSQDIEKLKS QYRALARDSA QAKRKYQEAS KGSWLPFADL SLGTQRYVRS
LWKLFAHHNR YVLGVRAAQL HHQHHHQLLL PGLLRSLQDL HEEMACILKE ILQEYLEISS
LVQDEVVAIH REMAAAAARI QPEAEYQGFL RQYGSAPDVP PCVTFDESLL EEGEPLEPGE
LQLNELTVES VQHTLTSVTD ELAVATEMVF RRQEMVTQLQ QELRNEEENT HPRGRVQLLG
KRQALQEALQ GLQVARCSQA KLQAQQELLQ TKLEQLGPGE PPPVLLLQDD RHSTSSSEQE
REGGRTPTLE ILKSHISGIF RPKFSNLYRL EGEGFPSIPL LIDHLLSTQQ PLTKKSGVVL
HRAVPKDKWV LNHEDLVLGE QIGRGNFGEV FSGRLRADNT LVAVKSCRET LPPDIKAKFL
QEARILKQYS HPNIVRLIGV CTQKQPIYIV MELVQGGDFL TFLRTEGARL RVKTLLQMVG
DAAAGMEYLE SKCCIHRDLA ARNCLVTEKN VLKISDFGMS REEADGVYAA SGGLRQVPVK
WTAPEALNYG RYSSESDVWS FGILLWETFS LGASPYPNLS NQQTREFVEK GGRLPCPELC
PDAVFRLMEQ CWAYEPGQRP SFSTIYQELQ SIRKRHR
//
