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Database: UniProt
Entry: A0A663FK80_AQUCH
LinkDB: A0A663FK80_AQUCH
Original site: A0A663FK80_AQUCH 
ID   A0A663FK80_AQUCH        Unreviewed;      1203 AA.
AC   A0A663FK80;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=MCF.2 cell line derived transforming sequence like {ECO:0000313|Ensembl:ENSACCP00020024112.1};
GN   Name=MCF2L {ECO:0000313|Ensembl:ENSACCP00020024112.1};
OS   Aquila chrysaetos chrysaetos.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Aquila.
OX   NCBI_TaxID=223781 {ECO:0000313|Ensembl:ENSACCP00020024112.1, ECO:0000313|Proteomes:UP000472275};
RN   [1] {ECO:0000313|Ensembl:ENSACCP00020024112.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A663FK80; -.
DR   Ensembl; ENSACCT00020025184.1; ENSACCP00020024112.1; ENSACCG00020016512.1.
DR   GeneTree; ENSGT00940000157874; -.
DR   Proteomes; UP000472275; Unplaced.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd01227; PH_Dbs; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd00170; SEC14; 1.
DR   CDD; cd11857; SH3_DBS; 1.
DR   CDD; cd00176; SPEC; 1.
DR   Gene3D; 1.20.58.60; -; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR035534; DBS_PH.
DR   InterPro; IPR035532; DBS_SH3.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   PANTHER; PTHR22826:SF115; GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS; 1.
DR   PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR   Pfam; PF13716; CRAL_TRIO_2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472275};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          22..194
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   DOMAIN          601..781
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          793..915
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1100..1161
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          1006..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1167..1203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1030
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1203 AA;  135862 MW;  B7CCDE671BEF2197 CRC64;
     MRCWLKIEEM ALEELMQRLN AVSQCADEIM HQDIIPLYAA DIQDQLKKQF AYLSGGRGGD
     GCPVITFPDY PAFSEIPEKE FQNVLTYLTS IPSLRDAGIG FILVIDRRQD KWTSVKASIL
     RIAASFPGNL QLVLVLRPTG FFHRALSDIA FKFNKDEFKM KVPIIMLGSV SELQGYIDKT
     QLTEDLGGTL DYCHNRWLSR RTAIEGFAQK VKQTAQILQS FGTELAETEL PNDVQSTSSL
     LATHTEKKDK MKEDIRLAVE QGDDILGSIT KPVTENPEYK LNQDQLDNQT TVERLLAQLH
     ETETAFDEFW IKHQQKLEQC LRLRNFEQNF REVKAALDIV SERLSTFTDV GNSCSHVEHI
     LKDLANFEEK SCETVAKARM LASEGDAFIQ SNHYAVDSII PKCSELHHLC DAFTTETERR
     RNLLNKSLEL HGLLEKSLKW CDEGIYLLAS QPVDKCQSQD GAESALQEIE KFLDTGAGNK
     IKELNKIYRE YAHILNEDLK EHVQKVFQKQ ESMEEMFQKR QVSLKKLAAK QTRPVQPVAP
     RPEAFVKSPC TSPGLQREYV SNSESSALRR VNCRRGKSEM TELHQSRGGS TMDDEENLAV
     LRQHVMNELI ETERAYVEEL LCVLEGYAAE MDNPLMAHLI SPELQNKKDI LFGNMEEIYH
     FHNRIFLREL ENYVEFPELV GRCFLDQMED FQIYEKYCQN KPRSESLWRQ FSDSVFFQEC
     QRKLDHKLSL DSYLLKPVQR ITKYQLLLKE MLKYSKNCEG AEDLQEALTS ILGILKAVND
     SMHQIAITGY DGNLNELGKL LMQGSFNVWT DHKKGHSKVK DLARFKPMQR HLFLHEKAVL
     FCKKREENGE GYEKAPSYSY KHSLNMAAVG ITENVKGDAK KFEIWYNARE EVYIIQAPTP
     EVKATWVNEI RKVLTSQLQA CREASQHRTL EQTQSLPLPA SSCASPSRNH IRNTKKMEER
     KADLASLEGY GTAVAPKYPE KGKDDTSSTS ECSVLSKKRF TLQGFTNLKS QKETPSPSAK
     SQTLPMILLT GPASPTSPDK KAKRHEVVSD PTPFGLRGWA KTSHSLDASE ENDGWSSAED
     PLNSSDAEEE GGGGGGEMKL TPGKYTVVTD YEKGVSEEFT VKSGELVQLI REGEDGLWYV
     KNLSTGKEGW IPANNLLMLI GNSKSAQSLS SSESGTASST LSTSSSCSDS CNASSTSFSD
     IKG
//
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