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Database: UniProt
Entry: E1BQ32_BOVIN
LinkDB: E1BQ32_BOVIN
Original site: E1BQ32_BOVIN 
ID   E1BQ32_BOVIN            Unreviewed;       304 AA.
AC   E1BQ32;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Adapter molecule crk {ECO:0000256|ARBA:ARBA00039213};
GN   Name=CRK {ECO:0000313|Ensembl:ENSBTAP00000007443.5,
GN   ECO:0000313|VGNC:VGNC:27716};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000007443.5, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000007443.5, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000007443.5,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000007443.5}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000007443.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; NP_001179263.1; NM_001192334.1.
DR   AlphaFoldDB; E1BQ32; -.
DR   SMR; E1BQ32; -.
DR   STRING; 9913.ENSBTAP00000007443; -.
DR   PaxDb; 9913-ENSBTAP00000007443; -.
DR   Ensembl; ENSBTAT00000007443.6; ENSBTAP00000007443.5; ENSBTAG00000005665.6.
DR   GeneID; 512841; -.
DR   KEGG; bta:512841; -.
DR   CTD; 1398; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005665; -.
DR   VGNC; VGNC:27716; CRK.
DR   eggNOG; KOG4792; Eukaryota.
DR   GeneTree; ENSGT00820000127055; -.
DR   HOGENOM; CLU_060542_0_1_1; -.
DR   InParanoid; E1BQ32; -.
DR   OMA; DNHMIIE; -.
DR   OrthoDB; 2900795at2759; -.
DR   TreeFam; TF321436; -.
DR   Reactome; R-BTA-170984; ARMS-mediated activation.
DR   Reactome; R-BTA-186763; Downstream signal transduction.
DR   Reactome; R-BTA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-BTA-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-BTA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-BTA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR   Reactome; R-BTA-8875555; MET activates RAP1 and RAC1.
DR   Reactome; R-BTA-8875656; MET receptor recycling.
DR   Reactome; R-BTA-912631; Regulation of signaling by CBL.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000005665; Expressed in abomasum and 106 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR   GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR   GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR   GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR   GO; GO:0030159; F:signaling receptor complex adaptor activity; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0098749; P:cerebellar neuron development; IEA:Ensembl.
DR   GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR   GO; GO:0016358; P:dendrite development; IEA:Ensembl.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR   GO; GO:0035685; P:helper T cell diapedesis; IEA:Ensembl.
DR   GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:Ensembl.
DR   GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl.
DR   GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl.
DR   GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0098698; P:postsynaptic specialization assembly; IEA:Ensembl.
DR   GO; GO:0038026; P:reelin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl.
DR   GO; GO:2000404; P:regulation of T cell migration; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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:UP000009136};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          13..118
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          132..192
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          235..296
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          61..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..82
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   304 AA;  33831 MW;  4CFBFB65BFC2E265 CRC64;
     MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY
     IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVSR
     SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG
     MIPVPYVEKY RPASASVSAL IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA
     RVIQKRVPNA YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD
     EDFS
//
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