NTRK3_PIG
ID NTRK3_PIG Reviewed; 825 AA.
AC P24786;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=NT-3 growth factor receptor;
DE EC=2.7.10.1;
DE AltName: Full=GP145-TrkC;
DE Short=Trk-C;
DE AltName: Full=Neurotrophic tyrosine kinase receptor type 3;
DE AltName: Full=TrkC tyrosine kinase;
DE Flags: Precursor;
GN Name=NTRK3; Synonyms=TRKC;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1653651; DOI=10.1016/0092-8674(91)90442-2;
RA Lamballe F., Klein R., Barbacid M.;
RT "trkC, a new member of the trk family of tyrosine protein kinases, is a
RT receptor for neurotrophin-3.";
RL Cell 66:967-979(1991).
CC -!- FUNCTION: Receptor tyrosine kinase involved in nervous system and
CC probably heart development. Upon binding of its ligand
CC NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different
CC signaling pathways, including the phosphatidylinositol 3-kinase/AKT and
CC the MAPK pathways, that control cell survival and differentiation.
CC {ECO:0000250|UniProtKB:Q16288}.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Exists in a dynamic equilibrium between monomeric (low
CC affinity) and dimeric (high affinity) structures (By similarity). Binds
CC SH2B2. Interacts with SQSTM1 and KIDINS220. Interacts with PTPRS (By
CC similarity). Interacts with MAPK8IP3/JIP3 (By similarity).
CC {ECO:0000250|UniProtKB:P04629, ECO:0000250|UniProtKB:Q03351}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Preferentially in the brain, low levels in the
CC ovaries.
CC -!- PTM: Ligand-mediated auto-phosphorylation.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; M80800; AAA31130.1; -; mRNA.
DR PIR; A40026; A40026.
DR RefSeq; NP_999436.1; NM_214271.1.
DR AlphaFoldDB; P24786; -.
DR SMR; P24786; -.
DR IntAct; P24786; 1.
DR MINT; P24786; -.
DR STRING; 9823.ENSSSCP00000005487; -.
DR PaxDb; P24786; -.
DR GeneID; 397511; -.
DR KEGG; ssc:397511; -.
DR CTD; 4916; -.
DR eggNOG; KOG1026; Eukaryota.
DR InParanoid; P24786; -.
DR BRENDA; 2.7.10.1; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043121; F:neurotrophin binding; IBA:GO_Central.
DR GO; GO:0005030; F:neurotrophin receptor activity; IBA:GO_Central.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IBA:GO_Central.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 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; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR020777; NTRK.
DR InterPro; IPR020446; NTRK3.
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 Pfam; PF00047; ig; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF16920; LRRCT_2; 1.
DR Pfam; PF01462; LRRNT; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR01939; NTKRECEPTOR.
DR PRINTS; PR01942; NTKRECEPTOR3.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 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; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Kinase; Leucine-rich repeat; Membrane;
KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..825
FT /note="NT-3 growth factor receptor"
FT /id="PRO_0000016734"
FT TOPO_DOM 32..429
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..825
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 104..125
FT /note="LRR 1"
FT REPEAT 128..149
FT /note="LRR 2"
FT DOMAIN 160..209
FT /note="LRRCT"
FT DOMAIN 210..300
FT /note="Ig-like C2-type 1"
FT DOMAIN 309..382
FT /note="Ig-like C2-type 2"
FT DOMAIN 538..814
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 679
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 544..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 572
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 516
FT /note="Interaction with SHC1"
FT /evidence="ECO:0000250"
FT SITE 820
FT /note="Interaction with PLC-gamma-1"
FT /evidence="ECO:0000250"
FT MOD_RES 516
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q16288"
FT MOD_RES 705
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 709
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 710
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 820
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..38
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 36..45
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 164..189
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 166..207
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 231..284
FT /evidence="ECO:0000250|UniProtKB:Q91044"
FT DISULFID 320..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 825 AA; 93130 MW; A3C6716B10D28540 CRC64;
MDVSLCPAKC SFWRIFLLGS VWLDYVGSVL ACPANCVCSK TEINCRRPDD GNLFPLLEGQ
DSGNSNGNAS INITDISRNI TSIHIENWRG LHTLNAVDME LYTGLQKLTI KNSGLRSIQP
RAFAKNPHLR YINLSSNRLT TLSWQLFQTL SLRELRLEQN FFNCSCDIRW MQLWQEQGEA
KLNSQSLYCI SADGSQLPLF RMNISQCDLP EISVSHVNLT VREGDNAVVT CNGSGSPLPD
VDWIVTGLQS INTHQTNLNW TNVHAINLTL VNVTSEDNGF TLTCIAENVV GMSNASVALT
VHYPPRVVSL EEPELRLEHC IEFVVRGNPP PTLHWLHNGQ PLRESKITHV EYYQEGEVSE
GCLLFNKPTH YNNGNYTLNR QEPLGTANQT INGHFLKEPF PESTDNFVSF YEVSPTPPIT
VTHKPEEDTF GVSIAVGLAA FACVLLVVLF IMINKYGRRS KFGMKGPVAV ISGEEDSASP
LHHDQPWHHH TLITGRRAGH SVIGMTRIPV IENPQYFRQG HNCHKPDTYV QHIKRRDIVL
KRELGEGAFG KVFLAECYNL SPTKVKMLVA VKALKDPTLA ARKDFQREAE LLTNLQHEHI
VKFYGVCGDG DPLIMVFEYM KHGDLNKFLR AHGPDAMILV DGQPRQAKGE LGLSQMLHIA
SQICSGMVYL ASQHFVHRDL ATRNCLVGAN LLVKIGDFGM SRDVYSTDYY RVGGHTMLPI
RWMPPESIMY RKFTTESDVW SFGVILWEIF TYGKQPWFQL SNTEVIECIT QGRVLERPRV
CPKEVYDVML GCWQREPQQR LNIKEIYKIL HALGKATPIY LDILG
