ID PKHG5_RAT Reviewed; 1039 AA.
AC Q6RFZ7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 120.
DE RecName: Full=Pleckstrin homology domain-containing family G member 5;
DE Short=PH domain-containing family G member 5;
DE AltName: Full=Neuronal RhoA GEF protein;
DE AltName: Full=Transcript highly enriched in cortex and hippocampus;
GN Name=Plekhg5; Synonyms=Tech;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-530.
RX PubMed=15686487; DOI=10.1111/j.1471-4159.2004.02930.x;
RA Marx R., Henderson J., Wang J., Baraban J.M.;
RT "Tech: a RhoA GEF selectively expressed in hippocampal and cortical
RT neurons.";
RL J. Neurochem. 92:850-858(2005).
RN [2]
RP INTERACTION WITH GIPC1 AND RHOA, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16467373; DOI=10.1091/mbc.e06-01-0002;
RA Liu M., Horowitz A.;
RT "A PDZ-binding motif as a critical determinant of Rho guanine exchange
RT factor function and cell phenotype.";
RL Mol. Biol. Cell 17:1880-1887(2006).
CC -!- FUNCTION: Functions as a guanine exchange factor (GEF) for RAB26 and
CC thus regulates autophagy of synaptic vesicles in axon terminal of
CC motoneurons (By similarity). Involved in the control of neuronal cell
CC differentiation. Plays a role in angiogenesis through regulation of
CC endothelial cells chemotaxis. Affects also the migration, adhesion, and
CC matrix/bone degradation in macrophages and osteoclasts (By similarity).
CC {ECO:0000250|UniProtKB:O94827, ECO:0000250|UniProtKB:Q66T02}.
CC -!- SUBUNIT: Interacts with GIPC1/synectin and RHOA.
CC {ECO:0000269|PubMed:16467373}.
CC -!- INTERACTION:
CC Q6RFZ7; Q9Z254: Gipc1; NbExp=3; IntAct=EBI-9079908, EBI-991162;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16467373}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:16467373}. Cell
CC membrane {ECO:0000269|PubMed:16467373}. Cell junction
CC {ECO:0000250|UniProtKB:Q66T02}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q66T02}. Note=Predominantly cytoplasmic, however
CC when endothelial cells are stimulated with lysophosphatidic acid,
CC PLEKHG5 is found in perinuclear regions and at the cell membrane
CC (PubMed:16467373). Localizes at cell-cell junctions in quiescent
CC endothelial cells, and relocalizes to cytoplasmic vesicle and the
CC leading edge of lamellipodia in migrating endothelial cells (By
CC similarity). {ECO:0000250|UniProtKB:Q66T02,
CC ECO:0000269|PubMed:16467373}.
CC -!- TISSUE SPECIFICITY: Selectively expressed in cortical and hippocampal
CC neurons with prominent expression in the cell bodies and dendrites.
CC Weakly expressed in rat fad pad ECs (RFPECs).
CC {ECO:0000269|PubMed:15686487, ECO:0000269|PubMed:16467373}.
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DR EMBL; AY499658; AAR89949.1; -; mRNA.
DR RefSeq; NP_958429.1; NM_201272.1.
DR AlphaFoldDB; Q6RFZ7; -.
DR SMR; Q6RFZ7; -.
DR BioGRID; 259803; 1.
DR IntAct; Q6RFZ7; 1.
DR STRING; 10116.ENSRNOP00000071902; -.
DR CarbonylDB; Q6RFZ7; -.
DR PhosphoSitePlus; Q6RFZ7; -.
DR PaxDb; 10116-ENSRNOP00000059729; -.
DR Ensembl; ENSRNOT00000064841.3; ENSRNOP00000059729.1; ENSRNOG00000022694.7.
DR GeneID; 310999; -.
DR KEGG; rno:310999; -.
DR UCSC; RGD:1303132; rat.
DR AGR; RGD:1303132; -.
DR CTD; 57449; -.
DR RGD; 1303132; Plekhg5.
DR eggNOG; KOG3521; Eukaryota.
DR GeneTree; ENSGT00510000046843; -.
DR InParanoid; Q6RFZ7; -.
DR OrthoDB; 2881273at2759; -.
DR Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR PRO; PR:Q6RFZ7; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000022694; Expressed in frontal cortex and 19 other cell types or tissues.
DR ExpressionAtlas; Q6RFZ7; baseline and differential.
DR Genevisible; Q6RFZ7; RN.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:0035767; P:endothelial cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
DR GO; GO:0140251; P:regulation protein catabolic process at presynapse; ISO:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd13244; PH_PLEKHG5_G6; 1.
DR CDD; cd17068; RBD_PLEKHG5; 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; IPR040181; PKHG5/7.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13217:SF11; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY G MEMBER 5; 1.
DR PANTHER; PTHR13217; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY G MEMBER 7; 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 SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1039
FT /note="Pleckstrin homology domain-containing family G
FT member 5"
FT /id="PRO_0000307136"
FT DOMAIN 372..564
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 620..720
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 58..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 760
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q66T02"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66T02"
FT MOD_RES 876
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q66T02"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66T02"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66T02"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66T02"
FT MUTAGEN 530
FT /note="L->E: No binding to RhoA."
FT /evidence="ECO:0000269|PubMed:15686487"
SQ SEQUENCE 1039 AA; 115784 MW; 874F74D61FEF441F CRC64;
MDKGRAAKVC HHADCQQLHH RGPLNLCEIC DSKFHNTTHY DGHVRFDLPP QGSVLARNVS
TRSCPPRTSP AGDLEEEDEG YTNGKGDRKS AGLKISKKKA RRRHTDDPSK ECFTLKFDLN
VDIETEIVPA MKKKSLGEVL LPVFERKGIA LGKVDIYLDQ SNTPLSLTFE AYRFGGHYLR
VKAKPGDEGK VEQGVKDSKS LSLPALRPSG AGTPVLERVD PQSRRESSLD ILAPGRRRKN
MSEFLGDTSI PGQESPAPSS CSLPVGSSVG SSGSSESWKN RAASRFSGFF SSSPSTGAFG
REVDKMEQLE SKLHAYSLFG LPRMPRRLRF DHDSWEEEED DEEEEDNSGL RLEDSWRELI
DGHEKLTRRQ CHQQEAVWEL LHTEVSYIRK LRVITNLFLC CLLNLQESGL LCEVEAERLF
SNIPELARLH RGLWSSVMVP VLEKARRTRA LLQPSDFLKG FKMFGSLFKP YIRYCMEEEG
CMEYMRSLLR DNDLFRAYVT WAEKHQQCQR LKLSDMLAKP HQRLTKYPLL LKSVLRKTDE
PRAKEAIITM ISSVERFIHH VNTCMRQRQE RQRLAGVVSR IDAYEVVEGS NDEVDKFLKE
FLHLDLTAPM PGTSPEETRQ LLLEGSLRMK EGKDSKMDVY CFLFTDLLLV TKAVKKAERT
KVIRPPLLVD KIVCRELRDP GSFLLIHLNE FHSAVGAYTF QASSQALCRS WVDTLYNAQN
QLQQLRAQLL CAQEHPGTQH LQSLEEEEDE QEEEGEESGT SAASSPTILR KSSNSLDSEH
CASDGSTETL AMVVVEPGET LSSPEFDRGP FSSQSDEASL SNTTSSITPT SELLPLGPVD
GRSCSMDSAY GTLSPTSLQD FAAPHPVVEP VPVPQTLSPQ PSPRLRRRTP VQLLPRLPHL
LKSKSEASLL QLLSGTTTSV SPPAPSRSLS ELCLITMAPG VRTQSSLQEG GPGWNCPGAC
GPCQGPPLSE SENRPSHKAG GPADSARRKC REMPCGTVPR VQPEPSPGIS AQHRKLTLAQ
LYRIRTTLLL NSTLTASEV
//
