ID A0A154P7U0_DUFNO Unreviewed; 1247 AA.
AC A0A154P7U0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN ORFNames=WN55_09052 {ECO:0000313|EMBL:KZC07989.1};
OS Dufourea novaeangliae (Sweat bee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Halictidae; Rophitinae; Dufourea.
OX NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC07989.1, ECO:0000313|Proteomes:UP000076502};
RN [1] {ECO:0000313|EMBL:KZC07989.1, ECO:0000313|Proteomes:UP000076502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0120121106 {ECO:0000313|EMBL:KZC07989.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KZC07989.1};
RA Pan H., Kapheim K.;
RT "The genome of Dufourea novaeangliae.";
RL Submitted (JUL-2015) 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,
CC ECO:0000256|RuleBase:RU000312};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; KQ434839; KZC07989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A154P7U0; -.
DR STRING; 178035.A0A154P7U0; -.
DR Proteomes; UP000076502; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; 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:0022008; P:neurogenesis; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd07459; CRD_TK_ROR_like; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd05048; PTKc_Ror; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR041775; Ror-like_CRD.
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 PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR24416:SF611; TYROSINE-PROTEIN KINASE TRANSMEMBRANE RECEPTOR ROR; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00018; KRINGLE.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000313|EMBL:KZC07989.1};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW Reference proteome {ECO:0000313|Proteomes:UP000076502};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transferase {ECO:0000313|EMBL:KZC07989.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000312};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 700..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..319
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 425..607
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 620..696
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 802..1076
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 318..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 836
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1247 AA; 139905 MW; C58C1E9018B85A02 CRC64;
MKAHRCISST FVCGLRWVHR VGQIAKQKVD KRESWGEKME EVMLRRKLSE RTRYYGKQER
YIRWNNKQGR LFRCNDCVEA RGVRDGFLAQ PSGLAGKNKQ GRVALAPFLA HGTYVGSASM
TRIKFVDIVP RTPRGQMRSV ETPMNDSSNG GRFYAVLNKY FRAGYLKAWQ TGDGNGDVED
LDTDVQDYST DEDYNDLFDA TTNGTDVEAT SGTKSGTLKF VRTPTNISKD AGGVAHMRCE
VVGDPPPTRI KWFKNEAPLE ERRPKITIKK IHAQAHEHAA KNIAGSRLKI INLDVSDVGF
YACRVTNGID QIQSEGTLRV DSSKSRHVPV NPEPPIGQTS NDDRFSPDMT GGDDFMDSIR
PGDGLDLSGS GMSTPHISHL ASTNPFSILS PSPQPTSSQS STTDMHTIGG LRNVNMQLSP
GRNDNHEGKC EIYVGKTCAQ FLEKQSVYIP YPMTQELLDD KLMKAFGVIE YSNEVSSNCE
GYAKPSLCYS AFPICRDPAS ILKLKNAKRI PTLGPGSEFN PYVDGKPSNK KLLSESYGDT
LSSSRSDINR KLRRICRQEC EVLENDLCRK EYAIAKRHPL IGHQVPLVNC SDLPVENTPE
ARDCLSLGIS TENNVQEKDY CYWGNGKTYR GIVNTSIRGR PCLQWLTHFN LPISDYPELA
GKHSYCRNPG DTELQPWCYV DVNHTMQKEF CDIPKCVENL WIYAVVGFVL TGGFVVILVC
YCCCYRSRKS TRQMNHLPSN KMLTGIQCDK NIYDGRRSTT QPMEMSSLLA GPGNTTPGTG
TLSSGSSRTS NNRVPQFTTN NVVLLQELGE GAFGKVYKGE LQTGNKCEPP IYVAVKTLKE
NASPKTQSDF KREVDLMTDL RHPNIICLLG VILKGEPMCM LFEYMTQGDL HEFLICHSPR
SDVPLNNGTG KILEQAEFLH IALQIASGME YLASHHYVHR DLAARNCLVG DNLTVKISDF
GLSRDIYSSD YYRVQSKSLL PVRWMPPESI VYGKFTTESD VWSFGVVLWE IYSYGLQPYY
GYNNQEVIDM IRSRQLLPCP EDCPTMIYSL MIECWHEVAN RRPQFPEIHH RLHNWYVNQT
YLSDFCNESI TSYSGSSHKS TNKTNSTQLS APIYKCDPKD MGNFKGGNME QTFCIVNEQT
NGLKLLPPSF QNSNSIEQRP NCGFSEHNTP MKTPIYPNQT NINFNEYDDK QCCSPKLSGA
KKVLPPTAQQ VGKTNTLNGT RPMQNGAQLV VRLPDPSKVT TETRVSK
//
