ID   SHC2_RAT                Reviewed;         573 AA.
AC   O70142;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=SHC-transforming protein 2;
DE   AltName: Full=Protein Sck;
DE   AltName: Full=SH2 domain protein C2;
DE   AltName: Full=Src homology 2 domain-containing-transforming protein C2;
GN   Name=Shc2; Synonyms=Sck;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 97-573.
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 and MEGF12. Once activated, binds to GRB2 (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The PID domain mediates binding to the TrkA receptor.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosine by the Trk receptors. {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AABR03055985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03059160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB001452; BAA28173.1; -; mRNA.
DR   RefSeq; NP_001101535.1; NM_001108065.1.
DR   AlphaFoldDB; O70142; -.
DR   SMR; O70142; -.
DR   STRING; 10116.ENSRNOP00000010714; -.
DR   iPTMnet; O70142; -.
DR   PhosphoSitePlus; O70142; -.
DR   PaxDb; 10116-ENSRNOP00000010714; -.
DR   Ensembl; ENSRNOT00000010714.6; ENSRNOP00000010714.5; ENSRNOG00000008030.6.
DR   Ensembl; ENSRNOT00055055385; ENSRNOP00055045723; ENSRNOG00055032016.
DR   Ensembl; ENSRNOT00060052088; ENSRNOP00060043321; ENSRNOG00060029984.
DR   Ensembl; ENSRNOT00065034858; ENSRNOP00065027998; ENSRNOG00065020589.
DR   GeneID; 314612; -.
DR   KEGG; rno:314612; -.
DR   UCSC; RGD:1307137; rat.
DR   AGR; RGD:1307137; -.
DR   CTD; 25759; -.
DR   RGD; 1307137; Shc2.
DR   eggNOG; KOG3697; Eukaryota.
DR   GeneTree; ENSGT00950000182870; -.
DR   HOGENOM; CLU_029532_2_0_1; -.
DR   InParanoid; O70142; -.
DR   OMA; GDEWSRK; -.
DR   OrthoDB; 2903566at2759; -.
DR   PhylomeDB; O70142; -.
DR   TreeFam; TF315807; -.
DR   Reactome; R-RNO-167044; Signalling to RAS.
DR   Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR   PRO; PR:O70142; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000008030; Expressed in frontal cortex and 18 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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:SF5; SHC-TRANSFORMING PROTEIN 2; 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.
DR   Genevisible; O70142; RN.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome; SH2 domain.
FT   CHAIN           1..573
FT                   /note="SHC-transforming protein 2"
FT                   /id="PRO_0000342264"
FT   DOMAIN          125..307
FT                   /note="PID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          478..569
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
SQ   SEQUENCE   573 AA;  61770 MW;  F81449473CB4F7AB CRC64;
     MTQGPGGRAA PEPEAPTTFC ALLPRMPQWK FAAPGSFLGR GPAAARVAGA AEAQPEPGVP
     ALAAVLGACE PRCAAPCPLP ALGRCRGSGS RGARGTPDVA DEWVRKGGFI HKPAHGWLHP
     DARVLGPGVS YIVRYMGCIE VLRSMRSLDF NTRTQVTREA INRLHEAVPG VRGSWKKKAP
     NKALASILGK SNLRFAGMSI SVNISVDGLN LSVPATRQII ANHHMQSISF ASGGDTDMTD
     YVAYVAKDPI NQRACHILEC CEGLAQSVIS TVGQAFELRF KQYLHSPPKA VVPPERLTGL
     EESAWGDGEV TADHDYYNSI PGKEPPLGGL VDSRLAVTQP CALTTLGGLG QGLSPAWRDV
     RGLPWDMGPS GAVPPGDGYV QADARGPHDY EEHLYVNTQG LDALELEDTS ETPLQPEDSP
     KKDLFDMRPF EDALKLHECS VAAGITAASL PLEDQWPSPP TRRAPIAPTE EQLRQEPWYH
     GRMSRRAAEK LLRADGDFLV RDSITNPGQY VLTGMHAGQP KHLLLVDPEG VVRTKDVLFE
     SISHLIDYHL KNGLPIVAAE SELHLRGVVS REP
//