ID A0A2R9A1Z7_PANPA Unreviewed; 839 AA.
AC A0A2R9A1Z7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Neural precursor cell expressed, developmentally down-regulated 9 {ECO:0000313|Ensembl:ENSPPAP00000011263.1};
GN Name=NEDD9 {ECO:0000313|Ensembl:ENSPPAP00000011263.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000011263.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000011263.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000011263.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJFE02097046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02097047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9A1Z7; -.
DR STRING; 9597.ENSPPAP00000011263; -.
DR Ensembl; ENSPPAT00000033918.1; ENSPPAP00000011263.1; ENSPPAG00000028824.1.
DR GeneTree; ENSGT00950000183008; -.
DR Proteomes; UP000240080; Chromosome 6.
DR Bgee; ENSPPAG00000028824; Expressed in placenta and 6 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:UP000240080};
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 243..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..320
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..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 93428 MW; 93565DAE680375EB CRC64;
SKYKCYLYCN LMARALYDNV PECAEELAFR KGDILTVIEQ NTGGLEGWWL CSLHGRQGIV
PGNRVKLLIG PMQETASSHE QPASGLMQQT FGQQKLYQVP NPQAAPRDTI YQVPPSYQNQ
GIYQVPTGHG TQEQEVYQVP PSVQRSIGGT SGPHVGKKVI TPVRTGHGYV YEYPSRYQKD
VYDIPPSHTT QGVYDIPPSS AKGPVFSVPV GEIKPQGVYD IPPTKGVYAI PPSACRDEAG
LREKDYDFPP PMRQAGRPDL RPEGVYDIPP TCTKPAGKDL HVKYNCDIPG AAEPVARRHQ
SLSPNHPPPQ LGQSVGSQND AYDVPRGVQF LEPPAETSEK ANPQERDGVY DVPLHNPPDA
KGSRDLVDGI NRLSFSSTGS TRSNMSTSST SSKESSLSAS PAQDKRLLLD PDTAIERLQR
LQQALEMGVS SLMALVTTDW RCYGYMERHI NEIRTAVDKV ELFLKEYLHF VKGAVANAAC
LPELILHNKM KRELQRVEDS HQILSQTSHD LNECSWSLNI LAINKPQNKC DDLDRFVMVA
KTVPDDAKQL TTTINTNAEA LFRPGPGSLH LKNGPESIMN STEYPHGGSQ GQLLHPGDHK
AQAHNKALPP GLSKEQAPDC SSSDGSERSW MDDYDYVHLQ GKEEFERQQK ELLEKENIMK
QNKMQLEHHQ LSQFQLLEQE ITKPVENDIS KWKPSQSLPT TNSGVSAQDR QLLCFYYDQC
ETHFISLLNA IDALFSCVSS AQPPRIFVAH SKFVILSAHK LVFIGDTLTR QVTAQDIRNK
VMNSSNQLCE QLKTIVMATK MAALHYPSTT ALQEMVHQVT DLSRNAQLFK RSLLEMATF
//
