GenomeNet

Database: UniProt
Entry: Q5XG33_XENLA
LinkDB: Q5XG33_XENLA
Original site: Q5XG33_XENLA 
ID   Q5XG33_XENLA            Unreviewed;       646 AA.
AC   Q5XG33;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Embryonal Fyn-associated substrate L homeolog {ECO:0000313|RefSeq:NP_001088375.1};
DE   SubName: Full=LOC495224 protein {ECO:0000313|EMBL:AAH84637.1};
GN   Name=efs.L {ECO:0000313|RefSeq:NP_001088375.1,
GN   ECO:0000313|Xenbase:XB-GENE-865961};
GN   Synonyms=efs {ECO:0000313|RefSeq:NP_001088375.1,
GN   ECO:0000313|Xenbase:XB-GENE-865961}, LOC495224
GN   {ECO:0000313|EMBL:AAH84637.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH84637.1};
RN   [1] {ECO:0000313|RefSeq:NP_001088375.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH84637.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH84637.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001088375.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the CAS family. {ECO:0000256|ARBA:ARBA00007848}.
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DR   EMBL; BC084637; AAH84637.1; -; mRNA.
DR   RefSeq; NP_001088375.1; NM_001094906.1.
DR   GeneID; 495224; -.
DR   KEGG; xla:495224; -.
DR   AGR; Xenbase:XB-GENE-865961; -.
DR   CTD; 495224; -.
DR   Xenbase; XB-GENE-865961; efs.L.
DR   OrthoDB; 3030146at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 495224; Expressed in neurula embryo and 16 other cell types or tissues.
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; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
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   Reference proteome {ECO:0000313|Proteomes:UP000186698};
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          88..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  70458 MW;  AA6F5C1BE12E2ACB CRC64;
     MAQLAQALYD NAAESPEELS FRRGDVMLVL ERDDPSLGGW WRCSLRGQQG IAPGNRLQLI
     PETPQQESEY QAPRFLGVNV DAGKLQKYEK GAQEKREEPK NEEEPENQTG AEVYQVPSIA
     RLRLSGQPAN AQDDIYNSPR LVGSCIEQPL EVYDTPSALR KDPLSTLDTY DSPALRVKAA
     DSAAQVPEEI PEDIYDVPPT FNKSPSDDEE DEGVYSMPSN LKRVSGLQNL YEAPEDILSS
     GHLPEILPPP PAQRLSVCST GSTRSADSAG SRESNIPPLS IWEPRNDGTC TMEGLRMLHQ
     ELQVSIAPVL AGAEKSAEPG GQEDSGTTKK VLGALRDFLV MAHVAGLRSC QASDPALHRE
     LSVHLDQLEN AARELLDKGS ERPLIQLIQE HSNCFVRLVS ANAGLLFPRP RLSSSESLSR
     RPLPALPTAS PAIQRKGSIQ DRPLPPPPTL QHVASDPSDD IHSEYERIQC RDNHYVHLQG
     SITAQNISKR KDRQKDTGQG STLEEREVDP FPEASEEDRH LLHFYATQSH SHLQTLLSCV
     GTFLGSASSQ PPRVFVGHGK QLVIAAHKLV FIGDTLGRLL SCPQLQTRLA GEGAALCQAL
     KDVVLATKEA ATLYPAPAAL KAMAGTVSVL CTCAHSFTHL LQHLAT
//
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