ID SHC3_RAT Reviewed; 594 AA.
AC O70143;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=SHC-transforming protein 3;
DE AltName: Full=Neuronal Shc;
DE Short=N-Shc;
DE AltName: Full=SHC-transforming protein C;
DE AltName: Full=Src homology 2 domain-containing-transforming protein C3;
DE Short=SH2 domain protein C3;
GN Name=Shc3; Synonyms=Nshc, Shcc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P52 AND P66), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9507002; DOI=10.1074/jbc.273.12.6960;
RA Nakamura T., Muraoka S., Sanokawa R., Mori N.;
RT "N-Shc and Sck, two neuronally expressed Shc adapter homologs. Their
RT differential regional expression in the brain and roles in neurotrophin and
RT Src signaling.";
RL J. Biol. Chem. 273:6960-6967(1998).
CC -!- FUNCTION: Signaling adapter that couples activated growth factor
CC receptors to signaling pathway in neurons. Involved in the signal
CC transduction pathways of neurotrophin-activated Trk receptors in
CC cortical neurons (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the Trk receptors in a phosphotyrosine-
CC dependent manner. Once activated, binds to GRB2. Interacts with
CC activated EGF receptors (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=p66;
CC IsoId=O70143-1; Sequence=Displayed;
CC Name=p52;
CC IsoId=O70143-2; Sequence=VSP_018793;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the adult brain, in the
CC hippocampus. {ECO:0000269|PubMed:9507002}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250}.
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DR EMBL; AB001453; BAA28174.1; -; mRNA.
DR EMBL; AB001453; BAA28175.1; -; mRNA.
DR AlphaFoldDB; O70143; -.
DR SMR; O70143; -.
DR IntAct; O70143; 2.
DR MINT; O70143; -.
DR STRING; 10116.ENSRNOP00000019442; -.
DR iPTMnet; O70143; -.
DR PhosphoSitePlus; O70143; -.
DR PaxDb; 10116-ENSRNOP00000019442; -.
DR AGR; RGD:69348; -.
DR RGD; 69348; Shc3.
DR eggNOG; KOG3697; Eukaryota.
DR InParanoid; O70143; -.
DR PhylomeDB; O70143; -.
DR Reactome; R-RNO-167044; Signalling to RAS.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-8853659; RET signaling.
DR PRO; PR:O70143; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; TAS:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd01209; PTB_Shc; 1.
DR CDD; cd09925; SH2_SHC; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006019; PID_Shc-like.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035676; SHC_SH2.
DR PANTHER; PTHR10337; SHC TRANSFORMING PROTEIN; 1.
DR PANTHER; PTHR10337:SF4; SHC-TRANSFORMING PROTEIN 3; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00629; SHCPIDOMAIN.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..594
FT /note="SHC-transforming protein 3"
FT /id="PRO_0000022342"
FT DOMAIN 149..334
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 499..590
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 95..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..498
FT /note="CH1"
FT REGION 428..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61120"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform p52)"
FT /evidence="ECO:0000303|PubMed:9507002"
FT /id="VSP_018793"
SQ SEQUENCE 594 AA; 64100 MW; 6AC6531CA30DA514 CRC64;
MLPRTKYNRF RNDSVTSVDD LLHSLSVSGS GGKVSAEPAA SPYLVSGEAL RKAPDDGPGS
LGHLLHKVSH LKLSSSGLRG LSSAARERAG ARLSGSCSAP SLAAPDGGSA TPGSRAPAAS
MSATRKSRAS DEPLPRPPRG APHASDQVLG SGVTYVVKYL GCIEVLRSMR SLDFSTRTQV
TREAISRVCE AVPGAKGAFK KRKPPSKMLS SILGKSNLQF AGMSISLTIS TASLNLRTPD
SKQIISNHHM RSISFASGGD PDTTDYVAYV AKDPVNRRAC HILECCDGLA QDVIGSIGQA
FELRFKQYLQ CPSKIPALQD RMQSLDEPWT EEEGDGPDHP YYNSVPNKMP PPGGFLDARL
KARPHAPDAA QFSGKEQTYY QGRHLGDAFG EDWQRAPTRQ GSLDIYSTPE GKAHMVPVGE
TPTYVNTQPV PPQVWPAATS STESSPRKDL FDMKPFEDAL RNQPLGPVLS KAASVECISP
VTPRAPDAKM LEELNAEPWY QGEMSRKEAE ALLQEDGDFL VRKSTTNPGS FVLTGMHNGQ
AKHLLLVDPE GTVRTKDRVF DSISHLITYH LESSLPIVSA GSELCLRQPV ERKP
//
