ID   DAB1_MACFA              Reviewed;         555 AA.
AC   Q9BGX5;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Disabled homolog 1;
GN   Name=DAB1; ORFNames=QflA-11558;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Frontal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
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. Interacts
CC       (phosphorylated on tyrosine residues) with CRK and CRKL (via respective
CC       SH2 domain). Interacts with DAB2IP, SIAH1, LRP8 and VLDLR. Interacts
CC       with LRP1. Interacts with APLP1 (via NPXY motif). Interacts with DAB2IP
CC       (By similarity). {ECO:0000250|UniProtKB:O75553,
CC       ECO:0000250|UniProtKB:P97318, ECO:0000250|UniProtKB:Q8CJH2}.
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; AB055282; BAB21906.1; -; mRNA.
DR   RefSeq; NP_001270758.1; NM_001283829.1.
DR   AlphaFoldDB; Q9BGX5; -.
DR   SMR; Q9BGX5; -.
DR   STRING; 9541.XP_005543297.1; -.
DR   GeneID; 102130276; -.
DR   CTD; 1600; -.
DR   eggNOG; KOG3535; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Neurogenesis; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..555
FT                   /note="Disabled homolog 1"
FT                   /id="PRO_0000079768"
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          384..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..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;  59920 MW;  A38002A1D0C4EE51 CRC64;
     MSTETELQVA VKTSAKKDSR KKGQDRSEAT LIKRFKGEGV RYKAKLIGID EVSAARGDKL
     CQDSMMKLKG VVAGARSKGE HKQKIFLTIS FGGIKIFDEK TGALQHHHAV HEISYIAKDT
     TDHRAFGYAC GKEGNHRFVA IKTAQAAEPV ILDLRDLFQL IYELKQREEL EKKAQKDKQC
     EQAVYQTILE EDVEDPVYQY IVFEAGHEPI RDPETEENIY QVPTSQKKEG VYDVPKSQPV
     SAVTQLELFG DMSTPPDITS PPTPATPGDA FIPSSSQTLP ASADVFGSVP FSTAAVPSGY
     VAMGAVLPSF WGQQPLVQQQ MVMGAQPPVA QVMPGAQPIA WGQPGLFPAT QQPWPTVAGQ
     FPPAAFMPTQ TVMPLPAAMF QGPLTPLATV PGTSDSTRPS PQTDKPRQKM GKETFKDFQM
     AQPPPVPSRK PDQPSLTCTS EAFSSYFNKV GVAQDTDDCD DFDISQLNLT PVTSTTPSTN
     SPPTPAPRQS SPSKSSASHA SDPTTDDIFE EGFESPSKSE EQEAPDGSQA SSNSDPFGEP
     SGEPSGDNIS PQAGS