ID M7BVI3_CHEMY Unreviewed; 304 AA.
AC M7BVI3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Crk-like protein {ECO:0000313|EMBL:EMP32147.1};
GN ORFNames=UY3_10717 {ECO:0000313|EMBL:EMP32147.1};
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:EMP32147.1, 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 -!- SIMILARITY: Belongs to the CRK family. {ECO:0000256|ARBA:ARBA00009756}.
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DR EMBL; KB542019; EMP32147.1; -; Genomic_DNA.
DR RefSeq; XP_007063807.1; XM_007063745.1.
DR AlphaFoldDB; M7BVI3; -.
DR STRING; 8469.M7BVI3; -.
DR GeneID; 102942619; -.
DR KEGG; cmy:102942619; -.
DR CTD; 1399; -.
DR eggNOG; KOG4792; Eukaryota.
DR OrthoDB; 2900795at2759; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:2000145; P:regulation of cell motility; IEA:UniProt.
DR CDD; cd09926; SH2_CRK_like; 1.
DR CDD; cd11759; SH3_CRK_C; 1.
DR CDD; cd11758; SH3_CRK_N; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR InterPro; IPR035458; CRK_SH3_C.
DR InterPro; IPR035457; CRK_SH3_N.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR19969:SF20; CRK-LIKE PROTEIN; 1.
DR PANTHER; PTHR19969; SH2-SH3 ADAPTOR PROTEIN-RELATED; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 2.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 15..103
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 124..184
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 236..297
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 184..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 33792 MW; 20CF9EC90DBF6C99 CRC64;
MSSAARFDSS DRSSWYVGPL SRAEAQTRLQ GQRHGMFLVR DSSTCPGDYV LSVSENSRVS
HYIINSLPSR RFKIGDQEFE HLPALLEFYK IHYLDTTTLI EPAPRYPSPP MGSGSAPTIP
TAEENLEYVR TLYDFLGNDA EDLPFKKGEI LVIVEKPEDQ WWSARNKDGR VGMIPVPYVE
KLVRSSPHGK HGNRNSNSYG IPEPAHAYAQ PQTTSPLPSV SSTPGAVINP LPSTQNGPVY
AKAIQKRVPC AYDKTALALE VGDIVKVTRM NINGQWEGEV NGRKGLFPFT HVKIIDPQNP
DENE
//
