ID C3YQL9_BRAFL Unreviewed; 1534 AA.
AC C3YQL9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_82713 {ECO:0000313|EMBL:EEN57375.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN57375.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN57375.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN57375.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; GG666543; EEN57375.1; -; Genomic_DNA.
DR RefSeq; XP_002601363.1; XM_002601317.1.
DR eggNOG; KOG0200; Eukaryota.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; C3YQL9; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00033; CCP; 3.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 2.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003410; HYR_dom.
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; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF617; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR Pfam; PF02494; HYR; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00084; Sushi; 3.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00032; CCP; 4.
DR SMART; SM01411; Ephrin_rec_like; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50825; HYR; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50923; SUSHI; 4.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1534
FT /note="Receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002933940"
FT DOMAIN 42..98
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 121..177
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 198..498
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 606..690
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 691..778
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 779..848
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 849..913
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 202..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 69..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 148..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1534 AA; 168878 MW; 5A711713005495CE CRC64;
MTADVFFLIL VSLSGVFTEY CSSNPCQSYE TCKDEANGYI CVFCPILSAP DNGEISGGAQ
YEDVVTFTCN HGYRLVGQST RICNALAMWS GVNPTCTGFC SSNPCPSYEI CKDDANGYIC
VYCPELSAPE NGEISGGAGY SDLVTFTCNQ GYRLVGDATR KCEGDKTWSG ANPACTAIAS
TDTTPTSVPL ARDLTSRYNR EYTNSPQETG PTFSMSARTS VSTGGTRPLQ HIPMKVMPVN
NTVNRELTWK DICLTSELLG AGHFGEVRKG TVIVNGKRIP SAIKILKSQQ YMALEMAGNG
DLLKFLRNSR VQDAVTYVNH QPKFGGTVST ISPVQLLRIA CDVAAGMDHL SSKQVIHRDL
AARNVLLTDS LIAKVADFGL SRGEGIYEQT SKRAIPFRST ALEALARRIY TTKSDVWSFG
ILLWEIVTIG GTPYRGMKSR TILGRLREGY RLPKPRNCEA DLYQLMVMCW NTRPEDRPSF
ADLAEQIEIM IEDKHSYVNI DKGDDFEYEV VDSSDIGIYS LTTPVHLTEN PHGGASHDVT
QQNHAMKEDH GARESSPVRH QPQEGVIQND RAPSRRTRGI NKRLLLGALA WHILQNSNRP
PPPPPPDTTR PTLTHCPFVG DVTLPSGQTQ ACINIGQPTY TDDRSKSVRV IQNGNTPPGG
CFPEGAYVIY YIALDDAGNR NDQCQVRFSV KDVKPPKFTN CPDDVIAYAE RNEDHVTVAW
PPLQAHDNSG DEPIIVQVDG PLNGSVLRTD GRKNRVVYTA TDNQGNRNNC SFNVIPQVIT
CEPLYVSQAK LSVTCTDGFN FGSTCQFRCE AGYPLVGMAN TSCELTNDNH PRGQWVPDPK
EQNPTCKVMK CPPLRLPKNG AISCSGWALG ETCQLQCEDR YDIPYNMPSN GLWVCSTTNG
VWAPDDRVLD CTRRRNPRRL RLPGEVYYYS GSCGDLHTLQ EIRHNFIRAL NSSSYSQLCI
KFTECAATNV NVTCGPATRR ARDVHSSAKY RIRVGFSIEI TPTNESLTQQ DMYKLDETLN
LMAAAVEDDI TEGRFNLDPV RVKDMALELD VNSVYFDYPE MECPYGTVPR YNTQSCASCS
TGTFYDEAVH DCTECPRGQY QDQDGQLECK TCPSGTSTVQ TAATSVLDCK GLCPPGKYSA
TGLEPCSTCQ INTFQPDARK TFCNNCPNTT VTKYAGASSS EECVGMNKIT FCATFYLTQL
LRVFYHLLPT KTQIMMTWTA YMHMAATIAC VKTTGLVSSD KSVNVQLDSM VISVKQSKGY
KLADVAVNVR PLMTLARNAV VPEWKFGLAR RRNVQEPLLN YQCGEKTGYI WPHQNALNPD
GRLPACGRVT LPRSISLHYK FKYPELPCEP DMVDALPVDP LPCVTEGRCR RDVTMTCDDS
SVGTTPTSVM LSITAEVPDH SIMWQSDDID DGELDTKLSA ALDAFKPVLR DIEEVLSIVT
SDGYDINVNG TMYTADTVPG QPTTDVNCPI GTVRQVVLCV TCPPGTLYNR GTCQECPLGS
YQELQGQTQC QYCPDGKTTL GIGASSQIDC VDTI
//
