ID A0A669BHM1_ORENI Unreviewed; 1166 AA.
AC A0A669BHM1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=MCF.2 cell line derived transforming sequence-like 2 {ECO:0000313|Ensembl:ENSONIP00000035223.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000035223.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000035223.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A669BHM1; -.
DR Ensembl; ENSONIT00000091696.1; ENSONIP00000035223.1; ENSONIG00000019195.2.
DR GeneTree; ENSGT00940000161734; -.
DR Proteomes; UP000005207; Linkage group LG23.
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; cd00176; SPEC; 1.
DR Gene3D; 1.20.58.60; -; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 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 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; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR PANTHER; PTHR22826:SF211; GUANINE NUCLEOTIDE EXCHANGE FACTOR MCF2L2-RELATED; 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 SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00516; SEC14; 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; 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.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT DOMAIN 1..171
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 600..779
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 791..913
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 502..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..358
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 524..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 131975 MW; EDA7FA57DD7DF713 CRC64;
MGSVIYEIMQ QDIRPLLAVD IIEQLHRQFA LLSGGRGKDG APIITFPEYS GFSEVPEEDF
LNVVTYLTSI PSLDAASIGF IIIIDRRKDK WSSVKASLSR IAGAFPGNLQ LVLVLRPSRF
FQKHIADIGI KLHKDDFKMK IVMLNSLSDL HGYVDKTQLT RELGGNLEYC HSQWIHHRTA
IENFAMTVKT TAQMLQKFGT DLAETELPND VQCTKDLLTA HTDKHNNLKD ELRLAVKQGT
TLYSCIKDQS AKSEDHELNP DEMENQTTVE RLLAQLDETE NAFEQFWSKH HLKLEQCLQL
RHFEQDFREV KVSLDSLIDS LNSLSDTGDC VARVEKLLKE LKTLEEKAQA TLEKAQLHAL
HGDQLIQSNH YAVDSIRPKC VELRRVCDDF SNEVKKKTDI LSKSLQIHQG IDKVNQWCES
GIYLLASQAV DKCQSQEGAE SALTDIEHFL ESAEKNQLTE LRNLHNQYEV VLSEDIKGSV
LKALKRLEDV QEMFEKRHLS LKRLSAKQTR PIQPVAPRPE SSPKRPSVKN TARTAGGQQP
LARRASDNSN KQQAEADLNK KKNIRKAKGG IKIEVMHEES QGGSTHVVVT NETEESLSNR
RRHIMTELIE TERLYVEELQ SIMEGYFAEL NNSELSHLIP PSLENKRDVL FGNLPEIYEF
HNKTFLMELE NCAEKPELVG TCFLKRKEEL QVYEKYCQNK PRSEILWRQC GDSLFFQECQ
KKLDHKLSLD AYLLKPVQRI TKYQLMLKEM LKCSNGEGMA ELEEALATML DIIKSVNDSM
HQIAITGFEG NLSELGKLLM QGSFSVWTDH KKGHSKVKDL ARFKPMQRHL FLYDKMLLFC
KKREETTDGH EKTPSYSFKH SLKMSSVGIT ENVKGDSKKF EVWYNGREEV YIIQAPSMDV
KNMWVSEIRK VLTGQLEACR EASQLNIYGP PMRNVRKMAL KHSDSSSPES GFRRSNPSPN
MRQKRADASA SQSGHSAVNA RKHFTLQGLS NRRSLPAEPA AKEAEVPRRF SLTSSLASSS
SSSFATRRTK GPLSASIKSK RHEIKSDPTP FGYEDTLRGA MAAVRKRQSM TSSTSAGPGG
TSAVPRSTSQ PGWAQRRLLS MDTEDFETIP SSAEESSNSS DEEGNNKNGD SSRFRVQLTY
ESRDPQDLSL ETGDLVQFVE EAKNGN
//
