ID A0A2K5Z598_MANLE Unreviewed; 561 AA.
AC A0A2K5Z598;
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=Embryonal Fyn-associated substrate {ECO:0000313|Ensembl:ENSMLEP00000023001.1};
GN Name=EFS {ECO:0000313|Ensembl:ENSMLEP00000023001.1};
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:ENSMLEP00000023001.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000023001.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000256|ARBA:ARBA00007848}.
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DR RefSeq; XP_011846068.1; XM_011990678.1.
DR AlphaFoldDB; A0A2K5Z598; -.
DR STRING; 9568.ENSMLEP00000023001; -.
DR Ensembl; ENSMLET00000046514.1; ENSMLEP00000023001.1; ENSMLEG00000035707.1.
DR GeneID; 105547192; -.
DR KEGG; mleu:105547192; -.
DR CTD; 10278; -.
DR GeneTree; ENSGT00950000183008; -.
DR OMA; LHNEYEG; -.
DR OrthoDB; 3030146at2759; -.
DR Proteomes; UP000233140; Unplaced.
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:UP000233140};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 5..68
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 69..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 59121 MW; BFF7D9A73234284B CRC64;
MAIATSAQLA RALYDNTAES PQELSFRRGD VLRVLQREGA GGLDGWCLCS LHGQQGIVPA
NRVKLLPAGP APKPGLSPAP PAQLGSPYPA PDHSNEDQEV YVVPPPARPC PTSGPPAGPC
PPSPDPIYKI PRASGTQLAA PRDVLEVYDV PPTALRVLSS SPYDCPASFS HPLTRVALQP
PEEDDAPYDV PLTPKPPAEL EPDLEWEGGR EPGPPIYAAP SNLKRASALL NLYEAPEELL
ADGEGGGTDE GIYDVPLLGP EAPPSPEPPG ALASHDQDTL AQLLARSPPP PHRPRLPSAE
SLSRRPLPAL PVPEAPSPSP VPSPAPGRKG SIQDRPLPPP PPRLPGYGGP KVEGDPEGRE
MEDDPAGHHN EYEGIPMAEE YDYVHLKGMD KAQGSRPPDQ ACTRDPELPE RGMPALQEAL
SPGEPLVLST GDLQLLHFYA GQCQSHYSAL QVAVAALMSS TQANQPPRLF VPHSKRVVVA
AHRLVFVGDT LGRLAASAPL RAQVRTGGTA LGQALRATVL AVKGAALGYP SSPAVQEMMQ
CVTELAGQAL RFTTLLTSLA P
//
