ID A0A4W5JUW6_9TELE Unreviewed; 2311 AA.
AC A0A4W5JUW6;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Trio Rho guanine nucleotide exchange factor {ECO:0000313|Ensembl:ENSHHUP00000003581.1};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000003581.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Proteomes:UP000314982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Macqueen D.J., Gundappa M.K.;
RT "Genome assembly of Danube salmon.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000003581.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSHHUT00000003707.1; ENSHHUP00000003581.1; ENSHHUG00000001508.1.
DR GeneTree; ENSGT00940000154766; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11852; SH3_Kalirin_1; 1.
DR CDD; cd00176; SPEC; 6.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
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; IPR000219; DH-domain.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR028570; Kalirin_TRIO_SH3_1.
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 InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF206; TRIPLE FUNCTIONAL DOMAIN PROTEIN-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 7.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000314982};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 5..151
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1234..1409
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1421..1533
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1599..1664
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1916..2092
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1548..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1871..1904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2234..2311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 699..726
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1571..1593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1768..1782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1877..1902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2247..2261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2271..2311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2311 AA; 263381 MW; 852224F67C703B0A CRC64;
MRAMEVLPIL KEKVAFLSGG RDRRGGPVLT FPSRSNHDRI RADDLRSLIA YLAGIPNEEV
IQHGFTVIVD MRGSKWDSIK SLLKILQESF PCCIHIALII KPDNFWQKQR TNFGSSKFEF
ETTMVSLEGL SKVVDPSQLT ADFEGSLEYN HDEWIEVRVA FEEFTGHAGH MLSRLEEMQE
VVARKDFPTD LDGARCMIEE HATLKKKVIK APIEELDTEG QRLLQRIQSS ESYRNSNASG
VCNADTQGLV PRVATLLDKL HSTRQHLHQA WHIRKLQLDQ CFQLRLFEQD AEKMFDWIMA
NKGLFLAGYT EIGNNHPHAM ELQTQHNHFA MNCMNVYVNI NRIMSVGNRL LESGHYASVQ
IKQISGQLEA EWKAFAAALD ERSTLLEMSA AFHQKCDQYM SNVDSWCKAC GEVDLPSELQ
DLEDAIHHHQ GLYEHITAAY SEVSQDGKAL LDKLQRPLTP GGADSLTASA NYSKAVHHVL
DVIHEVLHHQ RQLENIWQHR KVRLHQRLQL CVFQQDVQQV LDWIENHGEA FLSKHTGVGK
SLHRARALQK RHEDFEEVAQ NTYTNADKLL EAAEQLAQTG ECDPEEIYQA AHQLEDRIQD
FVRRVEQRKV LLDMSVAFHT HVKELWTWLE ELQKELLDDV YAESVEAVQD LIKRFSQQQL
TILQVTVNVI KEGEDLIQQL RDSAISSNKT PHNSSINHIE SVLLQLDEAQ AQMEELFQER
KIKLELFLQL RIFERDAIDI ISDLESWNEE LSVQMSEFDT EDLTLAEQRL QHHADKALTM
NNLTFDVIHQ GQELLQYVNE VQASGVELLC DRDVDMATRV QDLLEFLHEK QQELDVAGEQ
HRRHLEQCVQ LRHLQAEVKQ VLGWIRNGES MLNAGLITAS SLQEAEQLQR EHEQFQHAIE
KTHQSALQVQ QKAEALLQAN HYDMDLIRDC AESVASHWQQ LMLKMEDRLK LVNASVAFYK
TSEQVCSVLE SLEQEYKREE DWCGGADKLG PNCESDHVTP MISKHLEQKE AFLKACTLAR
RNADVFLKYM HRNSVNMPGM LSHVKAPEQQ VKNILNELLQ RENRVLHFWT MRRRRLDQCQ
QYVVFERSAK QALEWIHDTG EFYLSTHTST GSSIHHTQEL LKEHEDFHIT ARQTKERVKL
LIQLADGFCD KGHSHAVEIK KWVTVVDKHY RDFSLRMDKY RTSLEKALGI SSDTNSKSKD
LQLDIIPATP QGSEVKLRDA AHELNEEKRK SARRKEFIMA ELIQTEKTYV RDLRECTDTY
LWEMTSGVEE IPPGIVNKEH IIFGNMVDLY EFHHNIFLKE LEKYEQLPED VGHCFVTWAD
KFQMYVNYCK NKPDSTQLIL EHAGPYFDEI QQRHRLANSI SSYLIKPVQR ITKYQLLLKE
LLTCCEEGKG EIKDGLEVML SVPKRANDAM HLSMLEGFDE NIESQGELIL QESCQVWDPK
TLIRKGRERH LFLFEMSLIF SKEVKDSNGR SKYMYKSKLY TSELGVTEHV EGDPCKFALW
VGRTPTSDNK IVLKASSIEN KQDWIKHVRE VIQERTIHLR GALKEPIHIP KSATAKHHKG
HRRDGEDLDS QGDGSSQPDT ISIASRTSQN TLDSDKLSGG CELTVVIHDF MAGNSNELTV
RRGQTVEVLE RCHDKPDWCL VRTTDRSPAH EGLVPCAMLC IAHSRSSMEM EGIFNHKDTL
SVCSNDSIMP GSSATLQPGH HGMGSHTSPG PKRPGNTLRK WLTSPVRRLS SGKADGHVKK
LAHKQKKNRE VRKSGEMTGS AQKDSDDSAA TPQDETVEER VRNEGLSSGT LSKSSSSGMQ
SCGEEEGEEG PDSVPLPPPM AIQQHSLLQP DTQDDKSSSR LSVRPSSSET PSAAELVSAI
EELVKSKMAL EDRPSSLSVE QGDSSSPSFN PSDNSLLSSS SPIDEMEERK TGFLKRRHYV
LLELVETERD YVRDLGVVVG GYMTRMKEEG VPDDMKGKDK IVFGNIHQIY DWHRDFFMGE
LEKCLEDPER LGPLFVKHER RLHMYVVYCQ NKPKSELIVS EYIDTYFEDL KQRLGHRLQI
TDLLIKPVQR IMKYQLLLKD FLKFSKKAGL DSVELEKGVE IMCIVPKRCN DMMNVGRLQG
FDGKIVAQGR LLLQDTFIVS DPEEGVGRMR ERRVFLFEQI VIFSEPLDKK RGFSMPGFLY
KKSIKVSCLG LEDSADGDPC KFVLTSRVTN SSIESFVLHS SHLGVRQVWT LQISQILESQ
RNFLNALTSP TEYQRNHVGA SGPQGGAGSS RRPSRIPQPS RLHSTHSKEA DRMSTCSSAS
EQSIQSTQSN GVRDVPAAQA SGRSSSASAP G
//