ID F2US09_SALR5 Unreviewed; 2061 AA.
AC F2US09;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=PTSG_11059 {ECO:0000313|EMBL:EGD80414.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) 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:0000256|ARBA:ARBA00001171};
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DR EMBL; GL832993; EGD80414.1; -; Genomic_DNA.
DR RefSeq; XP_004987978.1; XM_004987921.1.
DR STRING; 946362.F2US09; -.
DR EnsemblProtists; EGD80414; EGD80414; PTSG_11059.
DR GeneID; 16068505; -.
DR KEGG; sre:PTSG_11059; -.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; F2US09; -.
DR OrthoDB; 2659618at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
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 InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR24416:SF611; TYROSINE-PROTEIN KINASE TRANSMEMBRANE RECEPTOR ROR; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000313|EMBL:EGD80414.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:EGD80414.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..2061
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003288795"
FT TRANSMEM 1565..1586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1357..1460
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1461..1553
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1650..1915
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 485..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1987..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..866
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1993..2011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2061 AA; 216251 MW; DE378EE3F0ACD47C CRC64;
MSAPAKPAMA PTRLLLLVVV VLALVGVSAQ DVVAVVAAED GAHTPPPPLI WPCSQDAATA
VGTTTALWLT GSTIQACRDP STGGGDTCCS VDSYPADSFN NLTAPIVWHN GRLQPLPSTR
TSAVCFASSL PCTGGLNETT AIFAVAPYQS DRSFVTAAQL RQVTAQALAS NTLVAFVHRD
GSDAATLRTS LTTPDAIGPV LAADTAALEV TTQALDLASD LDGSLHTSGY ISTSAVATPS
SLLLQITLAL PPNLSPAAVG ALQNSSVRVN TSVFVDGFLA VQGPLTFTPS VASSSSSSPS
MLLRLVSTNI AATLPQYLFS RVRIDARMDL ASSAFPRVLL PTSAANVTVS VLAGNLRPLT
LARTATVVWF PNSTNCSEIS NNGQQQQPQQ VPVFWNVPVG VCSPVPADPS THMHVTVTRA
NVTVRVYDDD DTCSSPAVLE ASLPRHEATA SVFVSPPSPA AQQRHLPFCL AGAASSLLFA
GLDPASAASN SSSNNNDDDT DNTNDDGLSE SISYATITPM TAFAAAQTVV AQIHRPGDLR
VPIAGESTGE LTVPVVPRPS RLPTNGGGGG GDLWFVGARA DLEAAAGGSN PPITLRSQIM
TVTAPVRVAG VHAVHVRGTC LHGTATVCFT GPVVDVVVPC QPGSDTLRWH YHVATVNVLP
SDVRAGQASF TMRMCQTRML FDTIAISPLY SLGPLNTAAA TTSIPSSSEA ETSATNSTMC
TASWPAAVCS QRGCRYDERR RLCHHRNAHA CWFVAESACT PDIGCAWSAT ISACINDDGD
YAGGVVDSPL PFTSPIAVDV TAGGSGVYET VRVPVAWHTG ETRAFVLYPS HHAALPHIML
VYGLAPSSSS PSPSPSPSPS PSPSPSSSSD SPAWAEWRAV SGVTAAALLQ SNAFLDTGVI
AAATHRIPAP SDASPLLPAP LHANLQVTCS LLPVVSVTGD TASDEEISAT RAAVAVRVLD
VTASTIRVQL SVPFATTTAP WPLAFTASPP AAAVHAAPTA QAHDPTAVLS TSVTATTTEA
GATVLTAEVT GLSPATPYRI GVSASLCGAL TLANDDDNGN DGSSDRIAGR VVTATTLPST
GPAPPPLLPL TASNRVEQLG WRLSSEGLHV SWFVHGQPPT DEYDAVLTHG STQQTITVAA
NALDLSSALL SHESFDAATG TMRTPVSVNS LRAGRCATAT CQDGGHCTVP VYSEPHRQSV
LFPYTGAFQP TMALQVRLRR GQQLLHEASA TVTGAAGVPA APTSLGATAG VDLLVVEWAP
VPGAVDYELQ ANVTATNAPI SIISPTTLVR LPSLPRETPV SVRVRARARV ASGATAGLAC
QRALGDVCAG NAAALVLAGP WSAAVTTRTL GNPPQAEPGA VRVVSLTDTT ATVAVDVLPG
DPRALVVYAI TERTRANGAR EQETVRAVPT RVDEESGRLI ARVAGLSPFT TYAFRAAFVS
AYGEGPMTAE ASTQNRTLRG VPGAPSLRNL RETGDGLLVQ WSAPGQEAGP IDFYTVYFTN
IDNGTEVSMR VQEAGLLLQG LVPGSTYTVT VTASTPAGES ERSRVLTHTL LAAASSSGSS
VSNGALAGIA VAVVLIVAVA MVVLLLHSRR QQRAAGQRLE LQLQHMKLNA DQLADQVRVM
FSQEFAETIG GDLAQTEEDF ARLEVDRTRL QLGSELGKGA FGVVYRGTLT LNGQAQTVAV
KTLLDGVVQD ELTKFLVEAR LMSLLRHDNL LRLVAVCTRD TPFYLVTEFM PKGDLKRFLR
DCRPTRPEPR ERLTTAQLNR MVLQIASAMQ YLESRRVIHR DLAARNVLVN DNNVVKIADF
GMSRNTEESD YYKKRSDDRV PIKWMAPESV TDRIYTSRSD VWSFGVLTWE VYSFARAPYA
EYTAMEAVAA AAAGYRLPRP DMCPEGMYTV MQLCWAYGSQ DRPSFAVLAH EIDFFLRTGR
FKALVQAEST QTKRGADSRR HHHPAPSTAI GSGGGGYDNV GSHTGYFGER EVAPVAVDAT
GYVADASLDG NDADSGSGGT VTYPRLEPNT PAATTLYAET PARRRQHEPP YPRTVPNTQG
GMVQNAAYQR LPNLHGQSPA P
//