ID   SHC1_XENLA              Reviewed;         465 AA.
AC   Q8AY68; Q5FWW5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=SHC-transforming protein 1;
DE   AltName: Full=Src homology 2 domain-containing-transforming protein C1;
DE            Short=SH2 domain protein C1;
DE   AltName: Full=p60Shc;
GN   Name=shc1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12941529; DOI=10.1016/s0248-4900(03)00058-3;
RA   Chesnel F., Heligon C., Richard-Parpaillon L., Boujard D.;
RT   "Molecular cloning and characterization of an adaptor protein Shc isoform
RT   from Xenopus laevis oocytes.";
RL   Biol. Cell 95:311-320(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Implicated in ras-dependent oocyte maturation induced by
CC       insulin/IGF-1. {ECO:0000269|PubMed:12941529}.
CC   -!- SUBUNIT: Interacts with grb2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in oocytes and embryo. Also
CC       expressed in liver. Detected in ovary, testis and heart and to a lesser
CC       extent in liver (at protein level). {ECO:0000269|PubMed:12941529}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK14789.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY027793; AAK14789.1; ALT_INIT; mRNA.
DR   EMBL; BC089178; AAH89178.1; -; mRNA.
DR   RefSeq; NP_001083932.1; NM_001090463.1.
DR   RefSeq; XP_018084264.1; XM_018228775.1.
DR   AlphaFoldDB; Q8AY68; -.
DR   SMR; Q8AY68; -.
DR   BioGRID; 100523; 1.
DR   IntAct; Q8AY68; 1.
DR   DNASU; 399198; -.
DR   GeneID; 399198; -.
DR   KEGG; xla:399198; -.
DR   CTD; 399198; -.
DR   Xenbase; XB-GENE-494866; shc1.L.
DR   OrthoDB; 1351843at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 399198; Expressed in spleen and 20 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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; IPR029586; Shc1/ShcA.
DR   InterPro; IPR035676; SHC_SH2.
DR   PANTHER; PTHR10337:SF2; PTHR10337:SF2; 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   1: Evidence at protein level;
KW   Cytoplasm; Growth regulation; Reference proteome; SH2 domain.
FT   CHAIN           1..465
FT                   /note="SHC-transforming protein 1"
FT                   /id="PRO_0000327223"
FT   DOMAIN          44..227
FT                   /note="PID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          370..461
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          228..369
FT                   /note="CH1"
FT   REGION          281..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  51730 MW;  E0E6726579965089 CRC64;
     MNKLSCGRKS RVEGGQLAGD EWTRHGSFVN KPTRGWLHPD DKVMGPGVPY LVRYMGCVEV
     LQSMRALDFN TRTQVTREAI SLVCDAVPGA KGAMRRRKTC GRSLNSILGK SNLKFAGMPI
     TLTVSTSSLN LMASDCKQII ANHHMQSISF ASGGDPDTAE YVAYVAKDPV NQRACHILEC
     PEGLAQDVIS TIGQAFELRF KQYLKNPPKL VTPHDRMAGF DGSAWDEEEE ELPDHAYYND
     FPGKEPPIGG VVDMRLRDGA APAVLRQSPN HMGATLPVGQ VSGAEQDSRK MQPTLQGRER
     FPVPCSRPPN RPDLFDDPSY VNVQNLEKSR QPLRAANGQR DIFDMKPFDD ALPSAQAIVS
     MEDQLKREPW YQGKMSRKEA ERLLKVNGDF LVRESTTTPG QYVLTGLQCG QPKHLLLVDP
     EGVVRTKDHR FESVSHLISY HMDNHLPIIS AGSELCLQQP VERRQ