ID L5KVT5_PTEAL Unreviewed; 303 AA.
AC L5KVT5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Crk-like protein {ECO:0000313|EMBL:ELK15569.1};
GN ORFNames=PAL_GLEAN10010830 {ECO:0000313|EMBL:ELK15569.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK15569.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SIMILARITY: Belongs to the CRK family. {ECO:0000256|ARBA:ARBA00009756}.
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DR EMBL; KB030536; ELK15569.1; -; Genomic_DNA.
DR RefSeq; XP_006908711.1; XM_006908649.2.
DR AlphaFoldDB; L5KVT5; -.
DR STRING; 9402.L5KVT5; -.
DR GeneID; 102898080; -.
DR KEGG; pale:102898080; -.
DR CTD; 1399; -.
DR eggNOG; KOG4792; Eukaryota.
DR InParanoid; L5KVT5; -.
DR OrthoDB; 2900795at2759; -.
DR Proteomes; UP000010552; 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:UP000010552};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 14..102
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 123..183
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 235..296
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 184..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 303 AA; 33816 MW; 9278203F01C611F0 CRC64;
MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRD SSTCPGDYVL SVSENSRVSH
YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPSV GSVSAPNLPT
AEENLEYVRT LYDFPGNDAE DLPFKKGEIL VIIEKPEEQW WSARNKDGWI GMIPVPYVEK
LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPAVS STPGAAINPL PSTQNGPVFA
KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIIDPQNPD
ENE
//
