ID A0A2K6D0A8_MACNE Unreviewed; 839 AA.
AC A0A2K6D0A8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Neural precursor cell expressed, developmentally down-regulated 9 {ECO:0000313|Ensembl:ENSMNEP00000029335.1};
GN Name=NEDD9 {ECO:0000313|Ensembl:ENSMNEP00000029335.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000029335.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000029335.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000256|ARBA:ARBA00007848}.
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DR AlphaFoldDB; A0A2K6D0A8; -.
DR STRING; 9545.ENSMNEP00000029335; -.
DR Ensembl; ENSMNET00000053733.1; ENSMNEP00000029335.1; ENSMNEG00000038134.1.
DR GeneTree; ENSGT00950000183008; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000038134; Expressed in lung and 12 other cell types or tissues.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0061523; P:cilium disassembly; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0097021; P:lymphocyte migration into lymphoid organs; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IEA:Ensembl.
DR GO; GO:2000522; P:positive regulation of immunological synapse formation; IEA:Ensembl.
DR GO; GO:0140131; P:positive regulation of lymphocyte chemotaxis; IEA:Ensembl.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:1903829; P:positive regulation of protein localization; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:Ensembl.
DR CDD; cd11570; FAT-like_NEDD9_C; 1.
DR CDD; cd11550; Serine_rich_NEDD9; 1.
DR CDD; cd12002; SH3_NEDD9; 1.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 1.
DR Gene3D; 1.20.120.830; Serine-rich domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR035746; NEDD9_SH3.
DR InterPro; IPR014928; Serine_rich_dom.
DR InterPro; IPR038319; Serine_rich_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654; CAS SCAFFOLDING PROTEIN; 1.
DR PANTHER; PTHR10654:SF20; ENHANCER OF FILAMENTATION 1; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 8..70
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 296..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 93391 MW; DBAD6D97776BC550 CRC64;
SKYKCYLYCN LMARALYDNV PECAEELAFR KGDILTVIEQ NTGGLEGWWL CSLHGRQGIV
PGNRVKLLIG PVQETTSSHD QPASGLMQQT FGQQKLYQVP NPQAAPRDTI YQVPPSYQNQ
GIYQVPTGHG TQEQEVYQVP PSVQRSIGGT SGPHVGKKVI TPVRTGHGYV YEYPSRYQKD
VYDIPPSHTT QGVYDIPPSS VKGPVFSVPV GEIKPQGVYD IPPTKGVYAI PPSACRDEAG
LREKDYDFPP PMRQVGRADL RPEGVYDIPP TSAKPAGKDL HVKYNCDIPG AAEPVARRHQ
SLSPNHPPPQ LGQSVGSHND AYDVPRGVQF LEPPAETSEK ANPQERDGVY DVPLHNPPDA
KGSRDLVDGI NRLSFSSTGS TRSNMSTSST SSKESSLSAS PAQDKRLLLD PDTAIERLQR
LQQALEMGVS SLMALVTTDW RCYGYMERHI NEIRTAVDKV ELFLKEYLHF VKGAVANAAC
LPELVLHNKM KRELQRVEDS HQILSQTSHD LNECSWSLNI LAINKPQNKC DDLDRFVMVA
KTVPDDAKQL TTTINTNAEA LFRPGPGSLH LKNGPESIMN STEYPHSGSQ GQLLHPGDHK
AQAHNKALPP GLSKEQAPDC SSSDGSERSW MDDYDYVHLQ GKEEFERQQK ELLEKENIMK
QNKMQLEHHQ LSQFQLLEQE ITKPVENDIS KWKPSQSLPT TNGGVSAQDR QLLCFYYDQC
ETHFISLLNA IDALFSCVSS AQPPRIFVAH SKFVILSAHK LVFIGDTLTR QVTAQDIRNK
VMNSSNQLCE QLKTIVMATK MAALHYPSTT ALQEMVHQVT DLSRNAQLFK RSLLEMATF
//
