ID A0A2Y9PDQ3_DELLE Unreviewed; 1390 AA.
AC A0A2Y9PDQ3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Pleckstrin homology domain-containing family G member 2 isoform X1 {ECO:0000313|RefSeq:XP_022441381.1, ECO:0000313|RefSeq:XP_022441382.1};
GN Name=PLEKHG2 {ECO:0000313|RefSeq:XP_022441381.1,
GN ECO:0000313|RefSeq:XP_022441382.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022441382.1};
RN [1] {ECO:0000313|RefSeq:XP_022441381.1, ECO:0000313|RefSeq:XP_022441382.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022441381.1,
RC ECO:0000313|RefSeq:XP_022441382.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_022441381.1; XM_022585673.2.
DR RefSeq; XP_022441382.1; XM_022585674.2.
DR STRING; 9749.A0A2Y9PDQ3; -.
DR Ensembl; ENSDLET00000021115; ENSDLEP00000019158; ENSDLEG00000013940.
DR KEGG; dle:111180868; -.
DR OrthoDB; 5400510at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:Ensembl.
DR CDD; cd13243; PH_PLEKHG1_G2_G3; 1.
DR CDD; cd00160; RhoGEF; 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; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR043324; PH_PLEKHG1_G2_G3.
DR PANTHER; PTHR45924; FI17866P1; 1.
DR PANTHER; PTHR45924:SF3; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY G MEMBER 2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 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.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT DOMAIN 101..282
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 312..410
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 36..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1088..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1390 AA; 148847 MW; 66143E64BAE4F281 CRC64;
MPEGARGLGL SKPSPSLGRR GEVCDCAAVC ETRTAAPATP AMASPRGSGS STSLSTVGSE
GDPAPGPTPA CLASRPEPLP GPPIRLHLSP VGTPASAKPS RLERVAREIV ETERAYVRDL
RSIVEDYLGP LLDGGVLGLS AEQVGTLFAN IEDIYEFSSE LLEDLEGSSS AGGIAECFVQ
RSEDFDIYTL YCMNYPSSLA LLRELSVSPP AALWLQERQA QLHHSLPLQS FLLKPVQRIL
KYHLLLQELG KHWVEGPDAG GRELVEEAIV SMTAVAWYIN DMKRKQEHAA RLQEVQRRLG
GWTGPELSAF GELVLEGAFR GGGGGGPRLR GGERLLFLFS RMLLVAKRRG PEYTYKGHIF
CCNLSVTESP RDPLGFKVSD LTIPKHRHLL QAKNQEEKRL WIHCLQRLFF ENHPASIPAK
AKQVLLENSL HCAPKSKSIP EPLTPPLGSP RPRDARSFTP GRRNTAPSPG PATTRRGRRQ
SEPLKDPYVM FPQNAKPRLK HTGSEGELYP PLEPLPPVPA SEPPEDLEDT GPPTLDPSGT
SITEEILELL NQRGLRDPGC PLQPPPHDIP KFPGDSQVPG DSDTLAFQAL PSRDSSEEEE
EEELDMDERG PSPLHVLEGL ESSSAAEIPD IPSLSKSPDV PNLPEIPSLS EIPQMPRLPS
LSDISSVFEM PCLPAIPSVP NIPSLSNAPT LPCDSWLQGP LQEPDEALAT RRELFPGSSS
GKLGEPSSES RAGQEEGEGV SYPAFQPRDV TQGQEFPDEL EFRPCSEIRS AWRALEQGQP
ARPGFPEPLL ILEDSDLSGG SGSGKAGAPT SERSASRVRE LARLYSERIQ QMQRAETRAS
ANAPRRRPRA LAQPQLLPCL PREQAEPGPL PAFGHVLVCE LAFPLTCAQE SVPLSPAAQV
QAATAVTKQR GCLDGQGLNV SSLPEQHHLG IQVPAATPLP EQGGLWNIRI PATTPLPKQE
GPPNGQMPAI TTLPDQEGHP EIQVPAAAPL PEHRGHVDIP VPCTTSFPEQ GCHVDIQVPI
TPALPKRGSC SDVMALAATP TPKREGHLDS QSSTNTPLTK QGDSRAVQSP ATACGQAVDP
LLIHRSSLDP QIPADTPLPL QHDLPDTQVP GTSPLPAHGG HLDHQTPANT LPSLPQDLPH
FQVPAATPFP QPQGLTDTQV QALPPLPQQG GLLDIQGPAA APLLEEQSLT DLQVQKLTPL
LEQKSLTNDH VPAAPPLPEQ GGPRDIQGLL PTRVQTTVVL SKQGGHAVSH VARSESSDLS
PPHSPPLATR QLLGSNAAAL SRYLAASYIS QSLARRQGPG GEAPPASRGP WSSSAPTSRA
PSPPPQPQPP APPARRLSYA TTVNIHVGGG GRLQPAKAQV RLNHPALLAT PQESVGLRRA
QGAPDAPFHM
//