SHC2_RAT
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 03-AUG-2022, entry version 119.
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}.
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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; O70142; -.
DR PRIDE; O70142; -.
DR Ensembl; ENSRNOT00000010714; ENSRNOP00000010714; ENSRNOG00000008030.
DR GeneID; 314612; -.
DR KEGG; rno:314612; -.
DR UCSC; RGD:1307137; rat.
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; HGGQPKH; -.
DR OrthoDB; 1351843at2759; -.
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 tissues.
DR Genevisible; O70142; RN.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; 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:0043410; P:positive regulation of MAPK cascade; 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; -; 1.
DR Gene3D; 3.30.505.10; -; 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; IPR029591; SHC2.
DR InterPro; IPR035676; SHC_SH2.
DR PANTHER; PTHR10337:SF5; PTHR10337:SF5; 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; SSF55550; SSF55550; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50001; SH2; 1.
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