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Database: UniProt
Entry: A0A2K6R316_RHIRO
LinkDB: A0A2K6R316_RHIRO
Original site: A0A2K6R316_RHIRO 
ID   A0A2K6R316_RHIRO        Unreviewed;       821 AA.
AC   A0A2K6R316;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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:ENSRROP00000035433.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000035433.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000035433.1}
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|ARBA:ARBA00001149,
CC         ECO:0000256|PIRNR:PIRNR000632};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC       cytoskeleton {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; A0A2K6R316; -.
DR   Ensembl; ENSRROT00000059887.1; ENSRROP00000035433.1; ENSRROG00000041148.1.
DR   GeneTree; ENSGT00940000158881; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; 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: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   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; 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; 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   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; 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|PIRNR:PIRNR000632, ECO:0000256|PIRSR:PIRSR000632-
KW   2};
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   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:UP000233200};
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..548
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          560..821
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          393..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        682
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000632-1"
FT   BINDING         566..574
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000632-2"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000632-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   821 AA;  93260 MW;  DD4F0FFD212151B2 CRC64;
     MGFSSELCTP QGHGVLQQMQ EAELRLLEGM RKWMAQRVKS DREYAGLLHH MSVQDSGGQS
     RGISPDSPIS QSWMEITSQT EGLSRLLRQH AEDLNSGPLS KLSLLIRERQ QLRKTYSEQW
     QQLQQELTKT HSQDIEKLKS QYRALARDSA QAKRKYQEAS KGRESKASDK YVRSLWKLFA
     HHNRYVLGVR AAQLHHQHHH QLLLPGLLRS LQDLHEEMAC ILKEILQEYL EISSLVQDEV
     VAIHREMAAA AARIQPEAEY QGFLRQYGSA PDVPPCVTFD ESLLEEGEPL EPGELQLNEL
     TVESVQHTLT SVTDELAVAT EMVFRRQEMV TQLQQELRNE EENTHPRGRV QLLGKRQALQ
     EALQGLQVAR CNQAKLQAQQ ELLQTKLEQL GPGEPPPVLL LQDDRHSTSS SEQEREGGRT
     PTLEILKSHI SGIFRPKFSL PPPLQLVPEV QKPLHEQLWY HGAIPRAEVA ELLVHSGDFL
     VRESQGKQEY VLSVLWDGLP RHFIIQSLDN LYRLEGEGFP SIPLLIDHLL STQQPLTKKS
     GVVLHRAVPK DKWVLNHEDL VLGEQIGRGN FGEVFSGRLR ADNTLVAVKS CRETLPPDLK
     AKFLQEARIL KQYSHPNIVR LIGVCTQKQP IYIVMELVQG GDFLTFLRTE GARLRVKILL
     QMVGDAAAGM EYLESKCCIH RDLAARNCLV TEKNVLKISD FGMSREEADG VYAASGGLRQ
     VPVKWTAPEA LNYGRYSSES DVWSFGILLW ETFSLGASPY PNLSNQQTRE FVEKGGRLPC
     PELCPDAVFR LMEQCWAYEP GQRPSFSTIY QELQSIRKRH R
//
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