DAB1_RAT
ID DAB1_RAT Reviewed; 555 AA.
AC Q8CJH2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Disabled homolog 1;
GN Name=Dab1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RA Kikkawa S., Misaki K., Terashima T.;
RT "Dab1 gene in the rat brain.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH DAB2IP.
RC TISSUE=Brain;
RX PubMed=11812785; DOI=10.1074/jbc.m110568200;
RA Wang Z., Tseng C.-P., Pong R.-C., Chen H., McConnell J.D., Navone N.,
RA Hsieh J.-T.;
RT "The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate
RT cancer. Characterization of a novel GTPase-activating protein associated
RT with N-terminal domain of DOC-2/DAB2.";
RL J. Biol. Chem. 277:12622-12631(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: Adapter molecule functioning in neural development. May
CC regulate SIAH1 activity. {ECO:0000250|UniProtKB:P97318}.
CC -!- SUBUNIT: Associates with the SH2 domains of SRC, FYN and ABL (By
CC similarity). Interacts (phosphorylated on tyrosine residues) with CRK
CC and CRKL (via respective SH2 domain) (By similarity). Interacts with
CC SIAH1, LRP8 and VLDLR (By similarity). Interacts with LRP1 (By
CC similarity). Interacts with APLP1 (via NPXY motif) (By similarity).
CC Interacts with DAB2IP (PubMed:11812785). {ECO:0000250|UniProtKB:O75553,
CC ECO:0000250|UniProtKB:P97318, ECO:0000269|PubMed:11812785}.
CC -!- DOMAIN: The PID domain specifically binds to the Asn-Pro-Xaa-Tyr(P)
CC motif found in many tyrosine-phosphorylated proteins.
CC -!- PTM: Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction in
CC embryonic neurons. Also phosphorylated on Ser-491 independently of
CC reelin signaling. {ECO:0000250|UniProtKB:P97318}.
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DR EMBL; AB072426; BAC20288.1; -; mRNA.
DR RefSeq; NP_705885.1; NM_153621.1.
DR RefSeq; XP_017448669.1; XM_017593180.1.
DR AlphaFoldDB; Q8CJH2; -.
DR SMR; Q8CJH2; -.
DR BioGRID; 251792; 2.
DR STRING; 10116.ENSRNOP00000009977; -.
DR iPTMnet; Q8CJH2; -.
DR PhosphoSitePlus; Q8CJH2; -.
DR PaxDb; Q8CJH2; -.
DR Ensembl; ENSRNOT00000009977; ENSRNOP00000009977; ENSRNOG00000007410.
DR GeneID; 266729; -.
DR KEGG; rno:266729; -.
DR UCSC; RGD:628770; rat.
DR CTD; 1600; -.
DR RGD; 628770; Dab1.
DR eggNOG; KOG3535; Eukaryota.
DR GeneTree; ENSGT00940000158038; -.
DR HOGENOM; CLU_020747_2_0_1; -.
DR InParanoid; Q8CJH2; -.
DR OMA; FDEKTGX; -.
DR PhylomeDB; Q8CJH2; -.
DR Reactome; R-RNO-8866376; Reelin signalling pathway.
DR PRO; PR:Q8CJH2; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007410; Expressed in frontal cortex and 11 other tissues.
DR ExpressionAtlas; Q8CJH2; baseline and differential.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0005903; C:brush border; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0021813; P:cell-cell adhesion involved in neuronal-glial interactions involved in cerebral cortex radial glia guided migration; ISO:RGD.
DR GO; GO:0021589; P:cerebellum structural organization; ISO:RGD.
DR GO; GO:0021795; P:cerebral cortex cell migration; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0051645; P:Golgi localization; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0097477; P:lateral motor column neuron migration; ISO:RGD.
DR GO; GO:0007494; P:midgut development; IEP:RGD.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; ISO:RGD.
DR GO; GO:0050771; P:negative regulation of axonogenesis; ISO:RGD.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:RGD.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; IDA:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
DR GO; GO:0021517; P:ventral spinal cord development; ISO:RGD.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Neurogenesis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..555
FT /note="Disabled homolog 1"
FT /id="PRO_0000253324"
FT DOMAIN 36..189
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97318"
FT MOD_RES 220
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97318"
FT MOD_RES 232
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97318"
FT MOD_RES 491
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:P97318"
SQ SEQUENCE 555 AA; 59900 MW; 24270CD20873CDAE CRC64;
MSTETELQVA VKTSAKKDSR KKGQDRSEAT LIKRFKGEGV RYKAKLIGID EVSAARGDKL
CQDSMMKLKG VVAGARSKGE HKQKIFLTIS FGGIKIFDEK TGALQHHHAV HEISYIAKDI
TDHRAFGYVC GKEGNHRFVA IKTAQAAEPV ILDLRDLFQL IYELKQREEL EKKAQKDKQC
EQAVYQTILE EDVEDPVYQY IVFEAGHEPI RDPETEENIY QVPTSQKKEG VYDVPKSQPV
SAVTQLELFG DMSTPPDITS PPTPATPGDA FLPAPSQTLP GSADVFGSMS FGTAAVPSGY
VAMGAVLPSF WGQQPLVQQQ IAMGAQPPVA QVIPGAQPIA WGQPGLFPAT QQPWPTVAGQ
FPPAAFMPTQ TVMPLPAAMF QGPLTPLATV PGTNDSARSS PQSDKPRQKM GKEMFKDFQM
AQPPPVPSRK PDQPSLTCTS EAFSSYFNKV GVAQDTDDCD DFDISQLNLT PVTSTTPSTN
SPPTPAPRQS SPSKSSASHV SDPTADDIFE EGFESPSKSE EQEAPDGSQA SSTSDPFGEP
SGEPSGDNIS PQDGS
