ID G3NKC5_GASAC Unreviewed; 1535 AA.
AC G3NKC5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Rho guanine nucleotide exchange factor (GEF) 28a {ECO:0008006|Google:ProtNLM};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000005787.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000005787.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000005787.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR STRING; 69293.ENSGACP00000005787; -.
DR Ensembl; ENSGACT00000005803.1; ENSGACP00000005787.1; ENSGACG00000004374.1.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000155831; -.
DR InParanoid; G3NKC5; -.
DR OMA; SFCHENS; -.
DR TreeFam; TF325887; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000004374; Expressed in mesonephros and 2 other cell types or tissues.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR CDD; cd14680; PH_p190RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing 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; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037819; ARHGEF28_PH.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR PANTHER; PTHR13944:SF22; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 28; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 664..711
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 861..1058
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1100..1202
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 294..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1471..1529
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 306..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1535 AA; 172131 MW; F1D6FD0F62EAD53D CRC64;
MELSRRRVPL YGQAKVFALL EGYDSVPEDA EVYIVLEGST LVHVTRAQSD VMLCFIVPGH
NLAEVVSVQA YLSSGTALVT WVGGASLEYV QDDAQDLAEH LVMHAHCLSS KDHTELSSLF
NLGQESSRGA MDRRVALAVA NLDIPRSWNV LGSHGGDERT PRESPLHLAV RWGLFRLAEL
LLCQPGGLMA VSLPNQEGVT PLQLAQTAAN TEILELLAHP PNPLATPPAG LSQVWADRSR
LLRFCHDSGN LTLTVRQNLR WSSEESRHAD ILLLRERLRD QDFLREAALR PMRAQELTGP
RGAADVLSKR RGRGKEKGQT ERENSPGSVV QSVRGLSREE EEDSGQTQST RESQAQSPTL
AAAVRLSAMI HGKGRVFANA MLVDQVDGAD IKYRLGRPCS FSTTPPASRN HAQDRHPPSP
RGGEKGIRGP EIRKEPSCRT SPPSTFTSPP SFPSSPLVSA FRLYEGGQRR PCLPVSPALN
RRGYSLTEAS QGLSPSLEGD SGEEDILGHS YPSSSVKKQS IPRSSSREER DSFEASPDFN
RLHSPPKSAS STQSPEEAEV RLRSYSFSSP KAKPSRPLLN RDTTVADQAE EQRAFSLTET
TKEKRIEDEE WDKYIIPSKV ESEKYKVSRT FSFLKSRMSS TRNKTKVKGK EAKEGKEKAG
ATNGHQFVSA SPPSAALCVG CDRSVSGKEL LQCSNCFLNV HKNCRESVAA CGKATSPLDM
MTIIMGVVGS GSIDVKPAPG NNARDKGGLI VCAPVGDSVK DNSPSTFCSS ASLPTTTREK
RETAGPLSKS FSVSIDSRLE RDRFREEKGE RRGAPFLSHT DGVDAPLMSG LSAEELGLEV
ESWSLAVSPE FCRQHDRHTI KRQEVIYELM QTELHHIQTL TVMSGVFRRG MLEELQLDWD
CVARIFPCLD PLLLFHKNLF GALLERRQAA AHTDTPGDYL IHQIGDILLQ QFSDEYAEEM
KQVYGEFCSH HTEAVNVFKE LQQQNKKLQN FVKQQSNNTL VRRREVPEFI LLVTQRITKY
PVLLERILHY TREESQEHAD LSRALAQIRN IIAAVDLTVN RHERCQELQE VLVRLENKSF
AKLKNDKVFR KQDLHSQHRV LQYKGLVYWK TATGRLKDTL ALLLTDVLVF LQEKDQRFVF
AAVDQKPPVI PLQKLIVREV ANEERGMFLI SASSVGPEMY EVHTNTRDER NAWMRHIRQA
VESCPEEEEE EERTAEIEES RRVAELRVQK ISKFQEMLSG QDQLICNSLE EKLQLYAELT
EFTLRSPEPV PHRHLVLADP DAETPRQASA LLIAALREGE SVAGRRGVAV AKRDKIRQNS
CFAPSAAENL IVPATRPKDQ SAAATTAGGA ACTSLHLSVS HFGTPTRHRS VFTDAGERRR
DVAESVQNLT QLLYSLQAAV TVQDSCYEVQ KLLLLEGERP QLHLVSIKND DRVSVVILHV
KLKQVQQRWD KECLARDKRQ CEQESVLEQR EHRCLLEAER LRCEREELEA QLLEYQQNLE
RLKAGQRSVE REKEKIEAQQ RLLQRWRHHR QSSLP
//
