ID   A0A091F521_CORBR        Unreviewed;       817 AA.
AC   A0A091F521;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Enhancer of filamentation 1 {ECO:0000313|EMBL:KFO56980.1};
DE   Flags: Fragment;
GN   ORFNames=N302_10629 {ECO:0000313|EMBL:KFO56980.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO56980.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO56980.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO56980.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK718485; KFO56980.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091F521; -.
DR   STRING; 85066.A0A091F521; -.
DR   Proteomes; UP000052976; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:UP000052976};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..62
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          347..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO56980.1"
FT   NON_TER         817
FT                   /evidence="ECO:0000313|EMBL:KFO56980.1"
SQ   SEQUENCE   817 AA;  91058 MW;  7EDC927A36C62701 CRC64;
     QNLMARALYD NVPECAEELA FRKGDILTVI EQNTEGLEGW WLCSLHGRQG IVPGNRVKLL
     IGPVVQDCPS GQDMPSSGLM NQPFSHQKIY QVPSSQASAR DPVYQVPPSH QNQGIYQIPT
     GHGLVGQDIY QVPPSVQRCI DGPAVINKVI TPVRSGQGYV YEFPSKHQKD AYDIPPIRPL
     QGIYDIPPTS VKGPALPVPT GEAKALGVYD IPLPKGVYAA PPSACQDDTA LRENLQDFSS
     PVGHSVRQEG VYDIPPPITK ATGKELNRFS PESLLLPGGM PQTQSVYDIP VNHQNQFLGQ
     QIAPEKDVYD TPRGTAFPGQ QTGLSESLIA EGREGVYDVP PQVLQDNKGL QDVTDGMNRL
     SFSSTGSTRS NMSTSSTTSK DSSHSSSTAQ DKRLILDPDT AIERLYHLQQ MVETAVNHLT
     AFITPDWRSY GYMEKHINEI HAAVDKVEQS LLEYLQFAKG SAANASCLSE FSLLNKMRRE
     VQRLEDSHQI LTQTSHDLNS YSWSLNVLAV NRVQNKCDDL DRFVMVARTV PDDAKQLTTT
     ISVNAELLFK QALASSRFKT VPENIMNTPD CVYDSPQMQR HGEKAQTHCS SLPLLLSKGQ
     HPYNATSEVS EKSWMDDYDY VHLQGKEEFE RQQKELLEKE NIIKQSKMEL EHHQINQFQR
     LEQEITKPVE NDISKWKPPQ DLQTSHDSRL LLFYSDQCET HFNSLLNAID AFFSCVNSSQ
     PPRIFVAHSK FIILSAHKLV FIGDTLARQM MTQGMCNKVM NSSNQLCELL KSVVLATKAA
     ALSYPSTAAL QKMVDQVTEL SHHAQLFKLS LVQMASM
//