ID A0A091HTI7_CALAN Unreviewed; 305 AA.
AC A0A091HTI7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Adapter molecule crk {ECO:0000256|ARBA:ARBA00039213};
GN ORFNames=N300_14565 {ECO:0000313|EMBL:KFO98464.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO98464.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO98464.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO98464.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the CRK family. {ECO:0000256|ARBA:ARBA00009756}.
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DR EMBL; KL217786; KFO98464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HTI7; -.
DR STRING; 9244.A0A091HTI7; -.
DR OrthoDB; 2900795at2759; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:SF8; ADAPTER MOLECULE CRK; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 13..119
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 133..193
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 236..297
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 200..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 33894 MW; B823F1F8CACAC30A CRC64;
MAGQFDSEDR ASWYWGRLSR NDAVLLLQGQ RHGTFLVRDS GTIPGDFVLS VSESSRVSHY
IVNSLGPAGG RRSGGEGPGA PGLSPTRFRI GDQEFDSLPS LLEFYKIHYL DTTTLIEPVS
RSRQNSGVIL RQEEAEYVRA LFDFNGNDEE DLPFKKGDIL RIRDKPEEQW WNAEDSEGKR
GMIPVPYVEK YRPSSASVSA IIGGNQDSSH PQPLGGPEPG PYAQPSINTP LPNLQNGPIY
ARVIQKRVPN AYDKTALALE VGELVKVTKI NVSGQWEGEC NGRRGHFPFT HVRLLDQQNP
DEDFS
//
