RTK2_GEOCY
ID RTK2_GEOCY Reviewed; 605 AA.
AC P42159;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Class II receptor tyrosine kinase;
DE EC=2.7.10.1;
DE AltName: Full=GCTK;
GN Name=TK;
OS Geodia cydonium (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Tetractinellida; Astrophorina; Geodiidae; Geodia.
OX NCBI_TaxID=6047;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7920862; DOI=10.3109/09687689409162227;
RA Schaecke H., Schroeder H.C., Gamulin V., Rinkevich B., Mueller I.M.,
RA Mueller W.E.G.;
RT "Molecular cloning of a tyrosine kinase gene from the marine sponge Geodia
RT cydonium: a new member belonging to the receptor tyrosine kinase class II
RT family.";
RL Mol. Membr. Biol. 11:101-107(1994).
RN [2]
RP SEQUENCE REVISION.
RA Mueller W.E.G.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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: Cell membrane; Single-pass membrane protein.
CC -!- PTM: Phosphorylated.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X72622; CAA51198.1; -; mRNA.
DR PIR; S67815; S67815.
DR AlphaFoldDB; P42159; -.
DR SMR; P42159; -.
DR BRENDA; 2.7.10.1; 2415.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Glycoprotein; Immunoglobulin domain; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN 1..605
FT /note="Class II receptor tyrosine kinase"
FT /id="PRO_0000058930"
FT TOPO_DOM 1..84
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..605
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..67
FT /note="Ig-like C2-type"
FT DOMAIN 346..605
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 209..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 496
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 352..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 527
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 605 AA; 67773 MW; E494D0BBDBFC9066 CRC64;
MWSSPGRNLE SGRFNITPRY TGTLSNGSVS SSDKVALSQL TIFNVTVADE GEYTCSVDGE
SASFRVDLGD SNSSGSNSGV IAGVLITLLL LIALIIILIC VFWVVWRYRR RGKFDLGSCR
ELSCSSCSCV PLLAALKGVK LPTRHRENLN KNGTRLRLNE RNHIADTNTE IYSVVQKPLK
KISKSPPPLP PLTLTETELN ELMSIDEKEE LSPIQEKPTR RNTGLSTYSQ SGTIPKLAKL
TKLRKFKMKE NPIYQSADEL ELELELQVDN TLYALPSKPN STRNSASFTD DLASDPIYSV
AINPSMFTKR SSTIGNDDDL HPYGPIYARP IKQKMRQPLN VSVDNIREVK QIGVGQFGAV
VLAEMTGLSG SERCVPTKRD PSMLNGVALV AVKKLKPDVS EEVRQSFDKE IKFVSQLQHD
SIVQLLAVCT HSKHPFIVME YMENGDLNQF LQKYQMVDDD SALYSNQIPP STLLYMAVQI
ASGMVYLSSL NYVHRDLATR NCLVGSNFRI KISDFGMSRN LYERVYYRVR GRAMLPIRWM
ATESFYGRFS EKSDAWAYGV TVWEIYTLGK KQPYEELDDQ DMIQDAIRGT GRRIMGRPRG
VAGCV
