ID A0A369RPZ3_9METZ Unreviewed; 849 AA.
AC A0A369RPZ3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Rho guanine nucleotide exchange factor 11 {ECO:0000313|EMBL:RDD36757.1};
GN ORFNames=TrispH2_011016 {ECO:0000313|EMBL:RDD36757.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD36757.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD36757.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD36757.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD36757.1};
RX PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT "Trichoplax genomes reveal profound admixture and suggest stable wild
RT populations without bisexual reproduction.";
RL Sci. Rep. 8:11168-11168(2018).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDD36757.1}.
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DR EMBL; NOWV01000318; RDD36757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369RPZ3; -.
DR STRING; 287889.A0A369RPZ3; -.
DR Proteomes; UP000253843; 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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.60.20; -; 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 Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR PANTHER; PTHR45872:SF2; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 19..97
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 312..363
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 500..688
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 448..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 96325 MW; 8A24E46636D2A646 CRC64;
MDTLKPINKN DDSDVRQKII VVCRDKNNKY GVSITGHNPV SIKAVRKGCP ADIAGLKAGD
MIIKVDGKLV IAASHETVTD MMKAANQVTL TLAERDDTTI DCSSLLKPKS EKTAAFLRYL
IANEKPNALL FLLMCEAYRQ KSGKVKDKKR WLYEISTAFL VPTAPLEISV EPQIIYNIVN
VIQNESIRDD QVFSNIFLAA REPAKSVVME KFTEYKKTRP NLIDKSKSDD IKAAEGILTP
QLNRLMEDIE AFRQVSQSTL DVQSVIASSI ATFLRFLDYE PASANSALGR CPAFLQKDRS
GTGPNEECFI KGHRFQPQAF TTIKYCGQCN RVIWGIGKNA YHCQACGFNV HISACAKSLL
YSCQGSSARK PIKTASNKRT SWWNFSGNTA DKQSSDARNF ESRRQEELAI SQVARKKLQF
RNQNTDATGT ITEDEARIRK ITANLRTRPM PTENSENDLA LSDDEDDDPD LAIPAEVPDW
ETVVSKEMAE LIINNDLETK RQKVILELIH TEKLHLKSLK VLRKLFYKPF IRSRLFDMNF
IYELFPNLLD LIKIHKSIIA AMEKRQAESE IVESIGDVII NKFSGKPGYE LKEAYVVCYS
NQSLTLAIFK EKLKDPKIEK FIRECESHPL CKHTSFQDLI SSGCRRLMRY PLLLDQIAKY
TQVDDPDFEG VVKALGCSKE VSMFVNSGIR EAENYQTLIS IVNNMDRSAI DQSNDPQLME
YKAIDFMKQR LLHSNDVKFK SPEGEEIHLK LLLLEEYIVL LEIKDNKYYL KCGNMAEIEP
HSTKQKRKQS SLQIPIIPLV DINAHASKTE KRTLVIVNTR ASPQLAYNLE TESKSAKEDW
LKEIQQAKK
//
