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NTRK3_MACFA
ID   NTRK3_MACFA             Reviewed;         825 AA.
AC   Q5IFJ9;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=NT-3 growth factor receptor;
DE            EC=2.7.10.1;
DE   AltName: Full=Neurotrophic tyrosine kinase receptor type 3;
DE   Flags: Precursor;
GN   Name=NTRK3;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
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 {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Ligand-mediated auto-phosphorylation. {ECO:0000250}.
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; AY742818; AAW55576.1; -; mRNA.
DR   AlphaFoldDB; Q5IFJ9; -.
DR   SMR; Q5IFJ9; -.
DR   STRING; 9541.XP_005560479.1; -.
DR   eggNOG; KOG1026; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005030; F:neurotrophin receptor activity; IEA:InterPro.
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:0007507; P:heart development; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
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; IPR013098; Ig_I-set.
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; PF07679; I-set; 1.
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_0000016732"
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..825
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         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6VNS1"
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   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;  92870 MW;  648794AB439672EA CRC64;
     MDVSLCPAKC SFWRIFLLGS VWLDYVGSVL ACPANCVCSK TEINCRRPDD GNLFPLLEGQ
     DSGNSNGNAS INITDISRNI TSIHIENWRS LHTLNAVDME LYTGLQKLTI RNSGLRSIQP
     RAFAKNPHLR YINLSSNRLT TLSWQLFQTL SLRELQLEQN FFNCSCDIRW MQLWQEQGEA
     KLNNQNLYCI NADGSQLPLF RMNISQCDLP EISVSHVNLT VREGDNAVIT CNGSGSPLPD
     VDWIVTGLQS INTHQTNLNW TNVHAINLTL VNVTSEDNGF TLTCIAENVV GMSNASVALT
     VYYPPRVVSL EEPELRLEHC IEFVVRGNPP PTLHWLHNGQ PLRESKIIHV EYYQEGEISE
     GCLLFNKPTH YNNGNYTLIA KNPLGTANQT INGHFLKEPF PESTDNFILF DEVSPTPPIT
     VTHKPEEDTF GVSIAVGLAA FACVLLVVLF IMINKYGRRS KFGMKGPVAV ISGEEDSASP
     LHHINHGITT PSSLDAGPDT VVIGMTRIPV IENPQYFRQG HNCHKPDTYV QHIKRRDIVL
     KRELGEGAFG KVFLAECYNL SPTKDKMLVA VKALKDPTLA ARKDFQREAE LLTNLQHEHI
     VKFYGVCGDG DPLIMVFEYM KHGDLNKFLR AHGPDAMILV DGQPRQAKGE LGLSQMLHIA
     SQIASGMVYL ASQHFVHRDL ATRNCLVGAN LLVKIGDFGM SRDVYSTDYY RVGGHTMLPI
     RWMPPESIMY RKFTTESDVW SFGVILWEIF TYGKQPWFQL SNTEVIECIT QGRVLERPRV
     CPKEVYDVML GCWQREPQQR LNIKEIYKIL HALGKATPIY LDILG
 
 
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