ID A0A2K6ACF5_MANLE Unreviewed; 770 AA.
AC A0A2K6ACF5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=DAB adaptor protein 2 {ECO:0000313|Ensembl:ENSMLEP00000037754.1};
GN Name=DAB2 {ECO:0000313|Ensembl:ENSMLEP00000037754.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000037754.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000037754.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_011821623.1; XM_011966233.1.
DR AlphaFoldDB; A0A2K6ACF5; -.
DR STRING; 9568.ENSMLEP00000037754; -.
DR Ensembl; ENSMLET00000061363.1; ENSMLEP00000037754.1; ENSMLEG00000042924.1.
DR GeneID; 105529140; -.
DR CTD; 1601; -.
DR GeneTree; ENSGT00940000155567; -.
DR OrthoDB; 2913989at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0038024; F:cargo receptor activity; IEA:Ensembl.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:Ensembl.
DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR GO; GO:0035026; P:leading edge cell differentiation; IEA:Ensembl.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR CDD; cd01215; PTB_Dab; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR048559; DAB1/2_SBM.
DR InterPro; IPR048561; Dab_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR PANTHER; PTHR47695:SF5; DISABLED HOMOLOG 2; 1.
DR PANTHER; PTHR47695; PID DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF21792; DAB2_SBM; 1.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS01179; PID; 1.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT DOMAIN 45..196
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 82466 MW; 16EEB4712B97D3A5 CRC64;
MSNEVETGAT NGQPDQQAAP KAPSKKEKKK GPEKTDEYLL ARFKGDGVKY KAKLIGIDDV
PDARGDKMSQ DSMMKLKGMA AAGRSQGQHK QRIWVNISLS GIKIIDEKTG VIEHEHPVNK
ISFIARDVTD NRAFGYVCGG EGQHQFFAIK TGQQAEPLVV DLKDLFQVIY NVKKKEEEKK
KIEEANKAVE NGSEALMILD DQTNKLKLGV DQMDLFGDMS TPPDLNSPTE SKDILLVDLN
SEIDTNQNSL RENPFLTNGI TSCSLPRPKP QASFLPENAF SANLNFFPTP NPDPFRDDPF
TQPDQSTPSS FDSLKSPDQK KENLSSSSTP LSNGPLNGDV DYFGQQFDQI SNRTGKQEAQ
AGPWPFSSSQ TQPAVRTQNG VSEREQNGFS VKSSPNPFVG SPPKGLSIQN GVKQDLESSV
QSSPHDSIAI IPPPQSTKPG RGRRTAKSSA NDLLASDIFA PPVSEPSGQA SPTGQPTALQ
PNPLDLFKTS APAPVGPLAG LGGVTVTLPQ AGPWNTASLV FNQSPSIVPG AMMGGQPSGF
GQPVIFGTSP AVPGWNQPSP FAASTSPPMP VVWGPSASAA PNAWSTTSPL GNPFQSNIFP
APAVSTQPQS MHSSLLATPP QPPPRAGPPK DISSDAFTAL DPLGDKEIKD VKEMFKDFQL
RQPPAVPARK GEQTPSGTSS SFSSYFNSKV GIPQENADHD DFDANQLLSK INEPPKPAPR
QVSLPVTKSA DNAFENPFFK DSFGSSQASM ASPQPVSSEI YRDPFGNPFA
//
