7TMK2_DICDI
ID 7TMK2_DICDI Reviewed; 704 AA.
AC Q54U65;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Seven transmembrane domain-containing serine/threonine-protein kinase 2;
DE EC=2.7.11.1;
GN Name=7tmk2; ORFNames=DDB_G0281331;
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-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000040; EAL66962.1; -; Genomic_DNA.
DR RefSeq; XP_640911.1; XM_635819.1.
DR AlphaFoldDB; Q54U65; -.
DR STRING; 44689.DDB0220006; -.
DR PaxDb; Q54U65; -.
DR PRIDE; Q54U65; -.
DR EnsemblProtists; EAL66962; EAL66962; DDB_G0281331.
DR GeneID; 8622973; -.
DR KEGG; ddi:DDB_G0281331; -.
DR dictyBase; DDB_G0281331; -.
DR eggNOG; KOG0197; Eukaryota.
DR HOGENOM; CLU_392034_0_0_1; -.
DR InParanoid; Q54U65; -.
DR OMA; FMEYIPH; -.
DR PRO; PR:Q54U65; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..704
FT /note="Seven transmembrane domain-containing
FT serine/threonine-protein kinase 2"
FT /id="PRO_0000362005"
FT TOPO_DOM 1..5
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..76
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..704
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 317..682
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 506
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 323..331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 704 AA; 80382 MW; B7C0D02A3387EA5B CRC64;
MPSKEFIIPL ILLCFYSVNG FVAVISSLVE LFIHKASWNS IKIFFYSLLI LQCLCRCIII
GWGMIETVQG GEFYSNFPSL LFISYAGLVA LQMIQFLPND NQYLLLSEGK KNNHKVKVGT
NILIFFNLFM YFGMFLLFGI AEKQVGNSTS FNHHGNHNST TSTSTDEIPL VSTEVGELYL
FGDKDPIYIV LDCFYFVCLL LLLIFHSYVG WKTYKRNKDL FGIKLNVIHL ILLICIFIRS
LLVIIDPSSP NNSILHIDTE SWLIYIYTIS YYVVGEIIPG MLLIVIEFLL PYHKRKDFIN
IGGELSSYQD VWKSENIAIH ELLGMGGSGA MVHKCTVKKG PLRGGTFAVK VMKDCTNEDI
ESLENEIRVY EKLKSPYIVS YQGSSKVVGS SGQIFEIRLF MEYIPHTLDK YLLARSVCGD
SNGGGSSRNL KNYFLHMQEY QSSPQSSISY YQNNNNNNNN SPLIQPQQQQ QYVYPYYFRY
SQVVWYLYQI SIGLDNLHAN KIAHRDLKSN NIFVTLSESE VKICKIGDFD ISRSFNNPKV
LNVLSNPTAL QQQKLNNFFQ SATTTTTTEQ TTEPIEVAAT TTPQTIHSAF QHDILSFGFI
VLDFLTLSNY SCFDSKFDTS NYYDDDKFNN KSNTKIKKPD LPDYIKKDEK LWEPVIQLYK
SCTSDDPNKR PSSLGVKFHL ANLYKDIIES GTEVWSIEKD SSSK
