ID G3QE36_GORGO Unreviewed; 729 AA.
AC G3QE36;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Rho GTPase activating protein 28 {ECO:0000313|Ensembl:ENSGGOP00000000521.3};
GN Name=ARHGAP28 {ECO:0000313|Ensembl:ENSGGOP00000000521.3};
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:ENSGGOP00000000521.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000000521.3, 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:ENSGGOP00000000521.3, 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:ENSGGOP00000000521.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; CABD030107212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030107213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030107214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030107215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030107216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3QE36; -.
DR STRING; 9593.ENSGGOP00000000521; -.
DR Ensembl; ENSGGOT00000000534.3; ENSGGOP00000000521.3; ENSGGOG00000000529.3.
DR eggNOG; KOG2200; Eukaryota.
DR GeneTree; ENSGT00940000158929; -.
DR InParanoid; G3QE36; -.
DR OMA; WVIKPQA; -.
DR TreeFam; TF314044; -.
DR Proteomes; UP000001519; Chromosome 18.
DR Bgee; ENSGGOG00000000529; Expressed in testis and 5 other cell types or tissues.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IBA:GO_Central.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04391; RhoGAP_ARHGAP18; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR PANTHER; PTHR14963:SF5; RHO GTPASE-ACTIVATING PROTEIN 28; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 380..577
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 20..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 82037 MW; 8B3958B8583177FA CRC64;
MEVEDSGGVV LTAYHSYARA QPPNAESRCA PRAAASHPLS RKSIPRCRRI NRMLSNESLH
PPAFSRSNSE ASVDSASMED FWREIESIKD SSMGGQEEPP PAEVTPVDEG ELEAEWLQDV
GLSTLISGDE EEDGKALLST LTRTQAAAVE KRYNTYTQTM RKKNKQSIRD VRDIFGVSES
PPRDTCGNHT NQLDGTKEER ELPRVIKTSG SMPDDASLNS TTLSDASQDK EGSFAVPRSD
SVAVLETIPV LPVHSNGSPE PGQPVQNAIS DDDYLEKNIP PEAEELSFEV SYSEMVTEAL
KRNKLKKSEI KKEDYVLTKF IVQKTRFGLT EAGDLSAEDM KKIRHLSLIE LTAFFDAFGI
QLKRNKTEKV KGRDNGIFGV PLTVLLDSDR KKDPGVKVPL VLQKFFEKVE ESGLESEGIF
RLSGCTAKVK QYREELDAKF NADKFKWDKM CHREAAVMLK AFFRELPTSL FPVEYIPAFI
SLMERGPHVK VQFQALHLMV MALPDANRDA AQALMTFFNK VIANESKNRM SLWNISTVMA
PNLFFSRSKH SDYEELLLAN TAAHIIRLML KYQKILWKVP SFLITQVRRM NEATMLLKKQ
LPSVRKLLRR KTLERETASP KTSKVLQKSP SARRMSDVPE GVIRVHAPLL SKVSMAIQLN
NQTKAKDILA KFQYENSHGS SECIKIQNQR LYEIGGNIGE HCLDPDAYIL DVYRINPQAE
WVIKPQPSS
//
