7TMK1_DICDI
ID 7TMK1_DICDI Reviewed; 691 AA.
AC Q54N73;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Seven transmembrane domain-containing tyrosine-protein kinase 1;
DE EC=2.7.10.1;
GN Name=7tmk1; ORFNames=DDB_G0285463;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Tyr protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000079; EAL64569.1; -; Genomic_DNA.
DR RefSeq; XP_638070.1; XM_632978.1.
DR AlphaFoldDB; Q54N73; -.
DR SMR; Q54N73; -.
DR STRING; 44689.DDB0229939; -.
DR PaxDb; Q54N73; -.
DR EnsemblProtists; EAL64569; EAL64569; DDB_G0285463.
DR GeneID; 8625116; -.
DR KEGG; ddi:DDB_G0285463; -.
DR dictyBase; DDB_G0285463; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_398728_0_0_1; -.
DR InParanoid; Q54N73; -.
DR OMA; NCIVTEY; -.
DR PhylomeDB; Q54N73; -.
DR Reactome; R-DDI-3295583; TRP channels.
DR Reactome; R-DDI-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-DDI-5675482; Regulation of necroptotic cell death.
DR PRO; PR:Q54N73; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; SSF56112; 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; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN 1..691
FT /note="Seven transmembrane domain-containing tyrosine-
FT protein kinase 1"
FT /id="PRO_0000355144"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..144
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..176
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..691
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 363..634
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 493
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 369..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 691 AA; 77496 MW; 9F6ED2E94AAA1706 CRC64;
MDTSCVSINQ CGFCTYLFNR SIPLAGEGDG AIMFNTMVDS MALGYIFSAL YLLFRLQRSY
TYLQKSSNNN NGNGNGNGSS NNDIISINSS NGLNRSGVKI SQDTLWDKNF GISIDHPRII
NSTYFKYTLF VSLWLAFEGL LLLFLPPNSL AYPAFVIIVG TGHIVTDNWV LVFLYGKEDD
RFSARRSFYS CTLLYLIICC TTLASFFDDQ TMCKKNDCQT FMFQDEYTSL AITVASLVVY
TIVLGMTIKR SFLRPTGRIW LLFLMGYNCI SSVGALLNIL DVDAGYCFLG IAAIIYSFSY
GPLLFRTCGN DTNLLRARGE FLPLLTNFQE YTSLFGRESI STSGEGATTA LQLSAFYIRF
NEFKFGQVIG EGYFGEVRKA VWKGAVVAVK ILHRNSFRNT DGNKEENVFL KEVAILSILR
HPNVLQFLGV CSETNLNGIV TEYMGGGSLD RLLTDRYFLI KQNPILAWNM AISIARGMFY
LHDWKPNPIL HRDLSTKNIL LDESLTIAKV ADFGLSKEQG FEMTSTVGHL CYQAPEVFIG
ELYTPKADVY SFGLLVWCII TGEQPNQNLQ PLKMAHLAAY ENYRPPMPQP MDPMWENLGK
LIEMCWKKSP EERPSFSFIL DFLEANVPIS NTYVPPLKCI SDNSVSNNFN NNNNTLNNGS
TNNLGLLTLS FSTLNLQKQG GGAEEFHYID G
