GenomeNet

Database: UniProt
Entry: A0A2R9C0J5_PANPA
LinkDB: A0A2R9C0J5_PANPA
Original site: A0A2R9C0J5_PANPA 
ID   A0A2R9C0J5_PANPA        Unreviewed;       549 AA.
AC   A0A2R9C0J5;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Embryonal Fyn-associated substrate {ECO:0000313|Ensembl:ENSPPAP00000032274.1};
GN   Name=EFS {ECO:0000313|Ensembl:ENSPPAP00000032274.1};
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:ENSPPAP00000032274.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000032274.1, 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:ENSPPAP00000032274.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the CAS family. {ECO:0000256|ARBA:ARBA00007848}.
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DR   EMBL; AJFE02024194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2R9C0J5; -.
DR   STRING; 9597.ENSPPAP00000032274; -.
DR   Ensembl; ENSPPAT00000055140.1; ENSPPAP00000032274.1; ENSPPAG00000039022.1.
DR   GeneTree; ENSGT00950000183008; -.
DR   OMA; LHNEYEG; -.
DR   Proteomes; UP000240080; Chromosome 14.
DR   Bgee; ENSPPAG00000039022; Expressed in cerebellum and 6 other cell types or tissues.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd11571; FAT-like_EFS_C; 1.
DR   CDD; cd12003; SH3_EFS; 1.
DR   Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR021901; CAS_C.
DR   InterPro; IPR037362; CAS_fam.
DR   InterPro; IPR035747; EFS_SH3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10654; CAS SCAFFOLDING PROTEIN; 1.
DR   PANTHER; PTHR10654:SF14; EMBRYONAL FYN-ASSOCIATED SUBSTRATE; 1.
DR   Pfam; PF12026; CAS_C; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
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   Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          5..67
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          67..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..87
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..122
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..197
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..313
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..335
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..360
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  57519 MW;  FE271C54941F3698 CRC64;
     MAIATSAQLA RALYDNTAES PQELSFRRGD VLRVLQREGA GLDGWCLCSL HGQQGIVPAN
     RVKLLPAGPA PKPSLSPASP AQPGSPYPAP DHSNEDQEVY VVPPPARPCP TSGPPAGPCP
     PSPDLIYKIP RASGTQLAAP RDALEVYDVP PTALRVPSSG PYDCPASFSH PLTRVAPQPP
     GEDDAPYDVP LTPKPPAELE PDLQWEGGRE PGPPIYAAPS NLKRASALLN LYEAPEELLA
     DGEGGGTDEG IYDVPLLGPE APPSPEPPGA LASHDQDTLA QPRLPSAESL SRRPLPALPV
     PEAPSPSPVP SPAPGRKGSI QDRPLPPPPP RLPGYGGPKV EGDPEGREME DDPAGHHNEY
     EGIPMAEEYD YVHLKGMDKA QGSRPPDQAC TGDPELPERG MPAPQEALSP GEPLVLSTGD
     LQLLYFYAGQ CQSHYSALQA AVAALMSSTQ ANQPPRLFVP HSKRVVVAAH RLVFVGDTLG
     RLAASAPLRA QVRAAGTALG QALRATVLAV KGAALGYPSS PAIQEMVQCV TELAGQALQF
     TTLLTSLAP
//
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