ID A0A1S3HD56_LINUN Unreviewed; 1438 AA.
AC A0A1S3HD56;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR000619};
GN Name=LOC106153603 {ECO:0000313|RefSeq:XP_013383049.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013383049.1};
RN [1] {ECO:0000313|RefSeq:XP_013383049.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013383049.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. EGF receptor subfamily. {ECO:0000256|PIRNR:PIRNR000619}.
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DR RefSeq; XP_013383049.1; XM_013527595.1.
DR EnsemblMetazoa; XM_013527595.1; XP_013383049.1; LOC106153603.
DR GeneID; 106153603; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
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:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:UniProt.
DR CDD; cd00064; FU; 5.
DR CDD; cd05057; PTKc_EGFR_like; 1.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR032778; GF_recep_IV.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR PANTHER; PTHR24416:SF566; EPIDERMAL GROWTH FACTOR RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PIRSF; PIRSF000619; TyrPK_EGF-R; 3.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 7.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000619};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000619};
KW Membrane {ECO:0000256|PIRNR:PIRNR000619, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000619};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|PIRNR:PIRNR000619,
KW ECO:0000313|RefSeq:XP_013383049.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000619};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000619}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1438
FT /note="Receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010222745"
FT TRANSMEM 819..842
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 887..1143
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1199..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1012
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-1"
FT BINDING 920
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000619-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1438 AA; 160566 MW; EBE227A083C74947 CRC64;
MKNIMLKDVL RWSVVVLTWT MCPWLVKGDQ QKTCIGTKYE LSMQGDAIYR YNLYRERYMN
CTYVQGNLEI TFLDNPQLDH PYDLSFLKHI REVTGYVLIV SVFANYVPLE NLRVIRGKTL
YYQNNRGYSL YVALNSKPSN SDMFGLKELR FVNLHEIMAG DVYFSKNPLL CYENTVVWNG
KIVTGEGSQV FVDDDAKGRS CGSCHRSCEG HCWGAGPNMC QRIIKCAPQC DGSCYGSGPV
ECCHYQCAGG CTGPTNKNCT ACRHFLDDGA CVPYCPQRQI YDEKTFTFVD NPKFKYTYGS
LCVKECPDHL LMDQSGCVKK CPEGKVANNR KCEPCKGPCP KSCNGTGDTY ITSQNINSFN
GCTIIEGNLK ILSPTIDGDM FNNIPPMSPS QLEALSQVRE VTHYVLIQSN SPNLTSLAFL
RNLEIIHGRE LHTGGKATLG VPQRGSALDV YSQTVTYLGF SSLKRVNGGE IRITHNSALC
YWYTIKWETL TGPKSLHFVE QNKIEAECER EGRVCSAECR DGCWGPGDDK CVKCANKRLG
NKCLATCDPS LGIYTKDDNV TCDYCHPECA RTCTGPEAKD CDSCKNYKNG PYCVKECPES
MYGDNTTKEC KKCHENCLLL QEESGCSGPG NFVGPGGCSK CKMFIYDKRT KNVTECLPTS
DKGQPQCPAG YYGHRVTSHE HLNTAYGLQG MQSCELCNPL CKTCFGALPT ECNECTFFKD
ISMSVHFCVV SCTERNYEDH NDKTCKPCNS ECRKGCTGPN STQCNFCSNV KVPLGITVNG
VDMFNCSSEC PSHLPHKRRE AGDEVCSTPP VIGLATGQIA GIAGGSVVFG LICIILLAFL
CYKRQKAKET TIKLTSKMIG YGDDEPLTPT DAVPDLSKLR LIKECEIRKG GIIGSGAFGT
VYKGVWIPDG ENVKIPVAIK VLQEGTSPNH NRELLEEARV MCSVEHQCCV RILAVCMTAQ
MMLITQLMPL GCLLDYVRKN KQNIGSKVLL NWCAQIAKGM SYLEERGIVH RDLAARNVLV
QSPSYVKITD FGLAKLLDYN EAEYHAAGGK MPIKWLALEC IQHRIFTHKT DVWSYGVTVW
ELLTYGLRPY ENVRARDIPD LLEKGERLPQ PSIATIDVYM IMIKCWMLDA ESRPSFKELH
EEFSKMARDP GRYLVIHGDR LMRLPSHTYD KRDLIRSISG GTEGPEEIME AEDYLMPRSS
TENEQGPMSP TSPVSPSGGI TKPLLPVSEP YDNDRGARAY PRGDYLNTEN KRDKKYGNLE
AASAASRGRG NSVNSRYSSD PCKLLVDMKG RGFFERIKEE DEVDSPVNPQ QKSRPDRPPM
LPVDEDDYLQ PKSTNPAAYM DLIGGKEQVE EPKDNHDNDV FTETGNIDNP EYFAAFSPTS
PETPLNGPFS DKRPLYNHNN NNNRQLNKSS ASAEDLPDRN YYNDIRPMEM SKVEESNC
//
