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Database: UniProt
Entry: G3QSY4_GORGO
LinkDB: G3QSY4_GORGO
Original site: G3QSY4_GORGO 
ID   G3QSY4_GORGO            Unreviewed;      1031 AA.
AC   G3QSY4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Rho guanine nucleotide exchange factor 2 {ECO:0000256|ARBA:ARBA00017262};
DE   AltName: Full=Guanine nucleotide exchange factor H1 {ECO:0000256|ARBA:ARBA00031760};
GN   Name=ARHGEF2 {ECO:0000313|Ensembl:ENSGGOP00000005785.3};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000005785.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000005785.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000005785.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000005785.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC       {ECO:0000256|ARBA:ARBA00004435}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000256|ARBA:ARBA00004186}. Cytoplasmic vesicle
CC       {ECO:0000256|ARBA:ARBA00004541}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
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DR   EMBL; CABD030006688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030006689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030006690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030006691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030006692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030006693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030006694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030006695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_018879621.1; XM_019024076.1.
DR   AlphaFoldDB; G3QSY4; -.
DR   STRING; 9593.ENSGGOP00000005785; -.
DR   Ensembl; ENSGGOT00000005938.3; ENSGGOP00000005785.3; ENSGGOG00000005907.3.
DR   GeneTree; ENSGT00940000158341; -.
DR   HOGENOM; CLU_002466_1_1_1; -.
DR   InParanoid; G3QSY4; -.
DR   OMA; RVFQQGM; -.
DR   Proteomes; UP000001519; Chromosome 1.
DR   Bgee; ENSGGOG00000005907; Expressed in cerebellum and 6 other cell types or tissues.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0032587; C:ruffle membrane; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0055059; P:asymmetric neuroblast division; IEA:Ensembl.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0071225; P:cellular response to muramyl dipeptide; IEA:Ensembl.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IBA:GO_Central.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR   CDD; cd20877; C1_ARHGEF2; 1.
DR   CDD; cd13393; PH_ARHGEF2; 1.
DR   CDD; cd00160; RhoGEF; 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   InterPro; IPR037806; ARHGEF2_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:SF20; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2; 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; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022427};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          84..131
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          280..477
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          517..616
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          728..750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          907..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..994
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1031
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1031 AA;  116209 MW;  D39582FD2602D5FD CRC64;
     MLSKSVPVSG INCLLDHSDP DGNVSQSSAI DLRKRCSQLE GHSGTWVGSS LRQTFSFLSG
     MTRKAKTREK EKMKEAKDAR YTNGHLFTTI SVSGMTMCYA CNKSITAKEA LICPTCNVTI
     HNRCKDTLAN CTKVKQKQQK AALLKNNTAL QSVSLRSKTT IRERPSSAIY PSDSFRQSLL
     GSRRGRSSLS LAKSVSTTNI AGHFNDESPL GLRRILSQST DSLNVRNRTL SVESLIDEAE
     VIYNELMSDF EMDEKDFAAD SWSLAVDSSF LQQHKKEVMK QQDVIYELIQ TELHHVRTLK
     IMTRLFRTGM LEELHLEPGV VQGLFPCVDE LSDIHTRFLS QLLERRRQAL CPGSTRNFVI
     HRLGDLLISQ FSGPSAEQMC KTYSEFCSRH TKALKLYKEL YARDKRFQQF IRKVTRPAVL
     KRHGVQECIL LVTQRITKYP LLISRILQHS HGIEEERQDL TTALGLVKEL LSNVDEGIYQ
     LEKGARLQEI YNRMDPRAQT PVPGKGPFGR EELLRRKLIH DGCLLWKTAT GRFKDVLVLL
     MTDVLVFLQE KDQKYIFPTL DKPSVVSLQN LIVRDIANQE KGMFLISAAP PEMYEVHTAS
     RDDRSTWIRV IQQSVRTCPS REDFPLIETE DEAYLRRIKM ELQQKDRALV ELLREKVGLF
     AEMTHFQAEE DGGSGMALPT LPRGLFRSES LESPRGERLL QDAIREVEGL KDLLVGPGVE
     LLLTPREPAL PLEPDSGGNT SPGVTANGEA RTFNGSIELC RADSDSSQRD RNGNQLRSPQ
     EEALQRLVNL YGLLHGLQAA VAQQDTLMEA RFPEGPERRE KLCRANSRDG EAGRAGAAPV
     APEKQATELA LLQRQHALLQ EELRRCRRLG EERATEAGSL EARLRESEQA RALLEREAEE
     ARRQLAALGQ TEPLPAEAPW ARRPVDPRRR SLPAGDALYL SFNPPQPSRG TDRLDLPVTT
     RSVHRHFEDR ERQELGSPEE RLQDSSDPDT GSEEEGSSRL SPPHSPRDFT RMQDIPEETE
     SRDGEAVASE S
//
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