ID Q9YH44_XENLA Unreviewed; 821 AA.
AC Q9YH44;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN Name=ntrk2.L {ECO:0000313|RefSeq:NP_001079579.1,
GN ECO:0000313|Xenbase:XB-GENE-6256346};
GN Synonyms=ntrk2 {ECO:0000313|RefSeq:NP_001079579.1,
GN ECO:0000313|Xenbase:XB-GENE-6256346}, ntrk2-a
GN {ECO:0000313|RefSeq:NP_001079579.1}, ntrk2-b
GN {ECO:0000313|RefSeq:NP_001079579.1}, ntrk2.S
GN {ECO:0000313|RefSeq:NP_001079579.1}, trkb
GN {ECO:0000313|RefSeq:NP_001079579.1}, trkb-b
GN {ECO:0000313|RefSeq:NP_001079579.1}, xTrkB
GN {ECO:0000313|EMBL:AAD00001.1}, xtrkb
GN {ECO:0000313|RefSeq:NP_001079579.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAD00001.1};
RN [1] {ECO:0000313|EMBL:AAD00001.1, ECO:0000313|RefSeq:NP_001079579.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8946245;
RA Islam N., Gagnon F., Moss T.;
RT "Catalytic and non-catalytic forms of the neurotrophin receptor xTrkB mRNA
RT are expressed in a pseudo-segmental manner within the early Xenopus central
RT nervous system.";
RL Int. J. Dev. Biol. 40:973-983(1996).
RN [2] {ECO:0000313|RefSeq:NP_001079579.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [3] {ECO:0000313|RefSeq:NP_001079579.1}
RP IDENTIFICATION.
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 ECO:0000256|RuleBase:RU000312};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
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DR EMBL; U39670; AAD00001.1; -; mRNA.
DR RefSeq; NP_001079579.1; NM_001086110.1.
DR DNASU; 379266; -.
DR GeneID; 379266; -.
DR KEGG; xla:379266; -.
DR AGR; Xenbase:XB-GENE-6256346; -.
DR Xenbase; XB-GENE-6256346; ntrk2.L.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 379266; Expressed in brain and 8 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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; cd05855; IgI_TrkB_d5; 1.
DR CDD; cd05093; PTKc_TrkB; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR020777; NTRK.
DR InterPro; IPR031635; NTRK_LRRCT.
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 InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF136; BDNF_NT-3 GROWTH FACTORS RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF16920; LRRCT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR01939; NTKRECEPTOR.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR620777-
KW 51}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000313|RefSeq:NP_001079579.1};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR620777-51, 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:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000312};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..282
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 537..806
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 474..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 675
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR620777-50"
FT BINDING 543..551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR620777-51"
FT BINDING 571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR620777-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT SITE 515
FT /note="Interaction with SHC1"
FT /evidence="ECO:0000256|PIRSR:PIRSR620777-52"
FT SITE 816
FT /note="Interaction with PLCG1"
FT /evidence="ECO:0000256|PIRSR:PIRSR620777-52"
SQ SEQUENCE 821 AA; 92312 MW; 0AF81BE74FD8FED3 CRC64;
MRLWKGSHGP DLVEVYGALW ILLALFWRGL ACPQYCSCNS TRIWCTLMDK GIAAFPVLED
SSLAENITDI YIANQRSLAS INDDDVKIYT GLRNLTVVDS GLQIVSRQAF RKNLKLTYIN
FSRNKLTSLT KKIFRHLTLS QLLLGGNPFQ CSCDLMWVKV LLETNSLNME NQNIHCFNDN
KKKIPLFNMH IPNCGLPIAN VSTVNITVLE GNETTLYCDA NGLPDPNVSW DISQIISKKR
MEMAKRPVLL TLKNVTSLDN KRIIVCVAEN SVGEDHISVE LNVHFPPVIT FIDLPTLDHH
WCIPFSVRGN PKPTLQWFHE GNILSETDFI WSKIHETSNY TSEHHGCLQL DSPTHLNNGF
YTLRAENIYG RDERSISALF MKGPDDGNPI TDPGFYDYET TSNDIGGTST DIGTGVTSTD
VSNGGNEDSI TVYVVVGIAA LVCTGLVIML IILKFGRHSK FGLKGPSSVI SNDDDSASPL
HHISNGSNTP SSSEGGPDTV IIGMTKIPVI ENPQYFGITN SHLKSDTFVQ HIKRHNIVLK
RELGEGAFGK VFLAECYNLY PEQDKILVAV KTLKDASDNA RKDFHREAEL LTNLQHEHIV
KFYGVCVEGD PLIMVFEYMK HGDLNKFLRA HGPDAVLMAE GNRPAELTQS QMLHIAQQIA
AGMVYLASQH FVHRDLATRN CLVGENLLVK IGDFGMSRDV YSTDYYRVGG HTMLPIRWMP
PESIMYRKFT TESDVWSLGV VLWEIFTYGK QPWYQLSNNE VIECITQGRV LQRPRTCPKE
VYDLMLGCWQ REPHMRLNIK EIHSLLQNLS KASPVYLDIL G
//