ID M7BJ27_CHEMY Unreviewed; 548 AA.
AC M7BJ27;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ORFNames=UY3_14703 {ECO:0000313|EMBL:EMP28227.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP28227.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KB565118; EMP28227.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BJ27; -.
DR STRING; 8469.M7BJ27; -.
DR eggNOG; KOG3697; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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); 3.
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; 3.
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; 3.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS01179; PID; 2.
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:UP000031443};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 1..230
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 238..297
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 453..544
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 132..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 59660 MW; A622B7DB2BC2AD3F CRC64;
MGPGVSYLVR YMGCVEVLQS MRALDFNTRT QVTREAISLV CEAVPSAKGA VRRRKPCGRS
LNSILGKSNL KFAGMPITLT ISTSSLNLMA SDCKQIIANH HMQSISFASG GDPETAEYVA
YVAKDPVNQR AGTAINPTTA GRLPRPSAAP LPAGATRAGP ATSPAASHPQ ETAEYVAYVA
KDPVNQRACH ILECPEGLAQ DVISTIGQAF ELRFKQYLKN PPKLVTPHDR YGGTLSPALV
PSPACHILEC PEGLAQDVIS TIGQAFELRF KQYLKNPPKL VTPHDRMAGF DGSAWDEEEE
EPSDHQYYND FPGKEPPLGG VVDMRLRDGA SATQTPSHLG ATLPVGQMSS AEHEPRKQHP
PAQGRDKYPP GTGPAIRTDL FDDPSYVNVQ NLDRSRQASA TSIPGTANGN AQRDLFDMKP
FEDALRVPPA VPVGLPPAQL LASMEEQLRR EPWYHGKMSR KEAEKLLKVN GDFLVRESTT
TPGQYVLTGL QGGQPKHLLL VDPEGVVRTK DHRFESVSHL ISYHMDNHLP IISAGSELCL
QQPVERRL
//
