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Database: UniProt
Entry: U3BFB2_CALJA
LinkDB: U3BFB2_CALJA
Original site: U3BFB2_CALJA 
ID   U3BFB2_CALJA            Unreviewed;       834 AA.
AC   U3BFB2; F7I8P7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Enhancer of filamentation 1 isoform 1 {ECO:0000313|EMBL:JAB04364.1};
GN   Name=NEDD9 {ECO:0000313|EMBL:JAB04364.1};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB04364.1};
RN   [1] {ECO:0000313|EMBL:JAB04364.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bladder {ECO:0000313|EMBL:JAB04364.1}, Hippocampus
RC   {ECO:0000313|EMBL:JAB14136.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB36274.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
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   EMBL; GAMT01007497; JAB04364.1; -; mRNA.
DR   EMBL; GAMS01009000; JAB14136.1; -; mRNA.
DR   EMBL; GAMQ01005577; JAB36274.1; -; mRNA.
DR   AlphaFoldDB; U3BFB2; -.
DR   Bgee; ENSCJAG00000005060; Expressed in ovary and 6 other cell types or tissues.
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; 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   2: Evidence at transcript level;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          3..65
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          237..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..397
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   834 AA;  92939 MW;  77A096BD1A370CA0 CRC64;
     MKYKNLMARA LYDNVPECAE ELAFRKGDIL TVIEQNTGGL EGWWLCSLHG RQGIVPGNRV
     KLLIGPVQEN ASSHEQPVSG LMQQTFGQQK LYQVPNPQAA PRDTIYQVPS SYQNQGIYQV
     PTGHGTQEQE VYQVPPSVQR SLGGTSGPHG GKKVITPVRT GHGYVYEYPS RYQKDVYDIP
     PSHTTQGVYD IPPSSVKGPM FSVPVGEIKP QGVYDIPPTK GVYAIPPSAC RDEAGFREKD
     YDFPPPMRQA GRPDLRPEGV YDIPPTSTKP AGKDLHVKYN CDIPGAAEPV ARRHQSLSPN
     HPPPQLGQSV GPQNDAYDVP RGIQFLEPPA ETSEKPNPQE RDGVYDVPLH NPPDAKGSRD
     LVDGINRLSF SSTGSTRSNM STSSTSSKES SLSASPAQDK RLLLDPDTAI ERLQRLQQAL
     EMGVSSLMAL VTTDWRCYGY MEKHINEIRT SVEKVELFLK EYLHFVKGAV ANASCLPELI
     LHNKMKRELQ RVEDSHQILS QTSHDLNECS WSLNILAINK PQNKCDDLDR FVMVAKTVPD
     DAKQLTTTIN TNAETLFKPG PGSLHLKNGP ESIMNSTEYP HGSPQVQLLH PGDHKAQAHS
     KALPPGLGKE QAPDCSSSDG SERSWMDDYD YVHLQGKEEF ERQQKELLEK ENIIKQNKMQ
     LEHHQLSQFQ LLEQEITKPV ENDISKWKPS QSLPTTNSGV SAQDRQLLCF YYDQCETHFI
     SLLNAIDALF SCVSSAQPPR IFVAHSKFVI LSAHKLVFIG DTLTRQVTAQ DIRNKVMNSS
     NQLCEQLKTI VMATKMAALH YPSTTALQEM VHQVTDLSRN AQLFKRSLLE MATF
//
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