ID A0A3Q1CPF3_AMPOC Unreviewed; 475 AA.
AC A0A3Q1CPF3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=SHC-transforming protein 1 {ECO:0000256|ARBA:ARBA00020297};
DE AltName: Full=Src homology 2 domain-containing-transforming protein C1 {ECO:0000256|ARBA:ARBA00031530};
GN Name=SHC1 {ECO:0000313|Ensembl:ENSAOCP00000021146.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000021146.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000021146.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR AlphaFoldDB; A0A3Q1CPF3; -.
DR STRING; 80972.ENSAOCP00000021146; -.
DR Ensembl; ENSAOCT00000011314.1; ENSAOCP00000021146.1; ENSAOCG00000005681.1.
DR GeneTree; ENSGT00950000182870; -.
DR OMA; DKPRMEH; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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:SF2; SHC-TRANSFORMING PROTEIN 1; 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 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 53..231
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 360..451
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
SQ SEQUENCE 475 AA; 51994 MW; A345524443D87ECD CRC64;
MEYMDMNRLG GASRRARVEG GQLGGDEWTR HGSFVNKPTR GWLHSDNVVS TTGVPYTVRY
MGCVEVLQSM RALDFNTRTQ VTREAISVVC EAVPGAKGAQ RRRKPSSRCL TSILGKSNLQ
FAGMTISLTI STSSLNLLAS DCKQIIANHH MQSISFASGG DPDTAEYVAY VAKDPVNQRA
CHILECSEGL AQEVISTIGQ AFELRFKQYL KNPPKLVTPH DRMAPFDGSA WEEEDDEAAP
PPDVPYYNNF PGKQPPPGGL VDMRTRPGAT LPYGQPGQND IHKQPLPPLP VGAKEGAREM
FDDPSYVNVD KPRPPAAANG NAHRDAFDMK PLDDALGVSG HGGPASVTPS LVQQLQCETW
FHGSLSRREA ERLLTRDGDF LVRESGTTPG QYVLTGQQGG QPKHLLLVDP EGVVRTKDHR
FGSVSHLISY HMDNRLPIVS AGSEVCLQQP VERRDAHLKM QQMSIVGFLN STLMS
//