TRK1_LYMST
ID TRK1_LYMST Reviewed; 794 AA.
AC O76997;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Putative neurotrophin receptor LTRK 1;
DE EC=2.7.10.1;
DE Flags: Precursor;
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9564036; DOI=10.1093/emboj/17.9.2534;
RA van Kesteren R.E., Fainzilber M., Hauser G., van Minnen J., Vreugdenhil E.,
RA Smit A.B., Ibanez C.F., Geraerts W.P.M., Bulloch A.G.M.;
RT "Early evolutionary origin of the neurotrophin receptor family.";
RL EMBO J. 17:2534-2542(1998).
CC -!- FUNCTION: May bind an endogenous invertebrate neurotrophin. Binds human
CC NT-3, but not NGF or BDNF.
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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expression is confined to the central nervous
CC system and its associated endocrine tissues.
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; U61728; AAC26840.1; -; mRNA.
DR AlphaFoldDB; O76997; -.
DR SMR; O76997; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
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; PF13855; LRR_8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 3.
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; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Neurogenesis; Nucleotide-binding;
KW Phosphoprotein; Receptor; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..794
FT /note="Putative neurotrophin receptor LTRK 1"
FT /id="PRO_0000016737"
FT TOPO_DOM 34..419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..794
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 181..202
FT /note="LRR 1"
FT REPEAT 205..226
FT /note="LRR 2"
FT DOMAIN 237..280
FT /note="LRRCT"
FT DOMAIN 504..775
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 36..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 647
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 510..518
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 673
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 677
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 678
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 789
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 794 AA; 89054 MW; FFF3EF5766E1A440 CRC64;
MRGPRRFRLW TRANVLTVIS ILTSILSGAG CSPLSQLPSD NPAHVGVQDG VTTERVDRSK
NHRNTTASSG AHRVTSGEPL GDRVTTRSTT APDQVPGDAS RNTTMAGTKC SLQVDLSTFA
CPADCQCNAT SEGMVVSCVT PDTLREFPVI AREVARAVIK LELRGQSKLT SLKTELKFFT
CLKHLTIENC GLNNIQGIAF KTLTSLETIN LRHNHLTEFP QELLRTLNLR ELWLEGNALT
CSCTNLWLRS VDVAADRSEM TCSTRDGVSK MKMTQFKCEP CGIPDIRNMT LVFEPKNGMF
LLRFVISGCP KPKIDLLRNH HHVLRSGSSQ FKLTDFKSEF NGQVVTGTIT ILPHMETSQT
TYVLTAVNSK GQANQTFHLY DQTTPASSIH IPLSNIPPRI SSATTPRASP TEDFGPQTQV
ILPVVGVVIL LISAVFIIYL CQRAKHRSHA RQRCKKALLD KKFNEFQEGV PLTGLQLVDN
PNYNLTKKKH VATTCPKTVR LQTILLMRVI GEGAFGRVFL GTCAHLIQKN EFAIVAVKTL
KGSCSDSLKR DFEREAEMLA TIEHANIVTF YGVCTESDQW MMIFEFMENG DLNKYLRMHG
PDAAFLKDRD SMDSDEGQLT REQLMKIVLQ IASAMEYLAL QHFVHRDLAT RNCLVGCDLV
VKLGDFGMSR DVYTTDYYRV EGTAMLPVRW MPPESIIYRT FTTESDVWSF GVTLWEVFTY
GKQPWFEYSN SEVIEHIKNS RTLKRPPRTC TDGVYRVMQG CWKPNPQDRL TMKDIAELLR
EEVSGDPVYI DIIA
