ID   DOK2_BOVIN              Reviewed;         413 AA.
AC   A7MBB8;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Docking protein 2;
DE   AltName: Full=Downstream of tyrosine kinase 2;
GN   Name=DOK2;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding
CC       proteins. They provide a docking platform for the assembly of
CC       multimolecular signaling complexes. DOK2 may modulate the cellular
CC       proliferation induced by IL-4, as well as IL-2 and IL-3. May be
CC       involved in modulating Bcr-Abl signaling. Attenuates EGF-stimulated MAP
CC       kinase activation (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with phosphorylated RASGAP and EGFR. Interacts with
CC       RET and NCK. Interacts (via PH domain) with TEK/TIE2 (tyrosine
CC       phosphorylated) (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: PTB domain mediates receptor interaction. {ECO:0000250}.
CC   -!- PTM: On immunoreceptor stimulation, phosphorylated on C-terminal
CC       tyrosine residues. Phosphorylation on Tyr-346 is required for binding
CC       to the SH2 domain of NCK. Phosphorylation on both Tyr-271 and Tyr-300
CC       is required for interaction with RASGAP. Phosphorylated on tyrosine
CC       residues by TEK/TIE2 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DOK family. Type A subfamily. {ECO:0000305}.
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DR   EMBL; BC151468; AAI51469.1; -; mRNA.
DR   RefSeq; NP_001095472.1; NM_001102002.2.
DR   AlphaFoldDB; A7MBB8; -.
DR   SMR; A7MBB8; -.
DR   STRING; 9913.ENSBTAP00000004337; -.
DR   PaxDb; A7MBB8; -.
DR   PRIDE; A7MBB8; -.
DR   Ensembl; ENSBTAT00000004337; ENSBTAP00000004337; ENSBTAG00000003341.
DR   GeneID; 514616; -.
DR   KEGG; bta:514616; -.
DR   CTD; 9046; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003341; -.
DR   VGNC; VGNC:28166; DOK2.
DR   eggNOG; KOG4047; Eukaryota.
DR   GeneTree; ENSGT00940000159868; -.
DR   HOGENOM; CLU_030101_2_0_1; -.
DR   InParanoid; A7MBB8; -.
DR   OMA; RPDHIYD; -.
DR   OrthoDB; 378139at2759; -.
DR   TreeFam; TF324994; -.
DR   Reactome; R-BTA-8853659; RET signaling.
DR   Proteomes; UP000009136; Chromosome 8.
DR   Bgee; ENSBTAG00000003341; Expressed in monocyte and 90 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IEA:Ensembl.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd01203; PTB_DOK1_DOK2_DOK3; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR037751; Dok1/2/3_PTB.
DR   InterPro; IPR002404; IRS_PTB.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   PROSITE; PS51064; IRS_PTB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..413
FT                   /note="Docking protein 2"
FT                   /id="PRO_0000356280"
FT   DOMAIN          4..114
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          147..252
FT                   /note="IRS-type PTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT   REGION          247..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..288
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         271
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O70469"
FT   MOD_RES         300
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O60496"
FT   MOD_RES         346
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O70469"
SQ   SEQUENCE   413 AA;  45729 MW;  86A6B66F6EA11B11 CRC64;
     MEDVVVKQGF LYLQQQQTFG KKWRRFGAAL YGGSGCALAR LELQEGSEKS RRGEAPRRVI
     RLNDCLRVSE ASGEASSPRD TSTFFLETTE RLYLLAAPTA ERGDWIQAIC LLAFPGRRKE
     LSGLEGKGGR PRMEENELYS STTAGTPQKE FAVTVRPTEV SERCRLRGSY TLRVGESALE
     LWGGPESGTQ LYEWPYRFLR RFGRDKVTFS FEAGRRCVSG EGNFEFETRQ GNEIFLALEE
     AISAQKNAAP PGPQTQPVPV PAVLPRPESP YARPHDSLPP PSPTVPVPTP RQQRGLEGEY
     AVPFDAVARS LGKSLRGVLA VPPQLPADPL YDSIEDHPPP RPDHIYDEPE GMAALALYDS
     PQEPRGEAWR RQATADRDSS GLKHGYIVGQ DFAASGWPQG TEYDNVVLKK GPK