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Database: UniProt
Entry: G3RME5_GORGO
LinkDB: G3RME5_GORGO
Original site: G3RME5_GORGO 
ID   G3RME5_GORGO            Unreviewed;       670 AA.
AC   G3RME5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Rho GTPase activating protein 28 {ECO:0000313|Ensembl:ENSGGOP00000016959.2};
GN   Name=ARHGAP28 {ECO:0000313|Ensembl:ENSGGOP00000016959.2};
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:ENSGGOP00000016959.2, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000016959.2, 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:ENSGGOP00000016959.2, 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:ENSGGOP00000016959.2}
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   RefSeq; XP_018869794.1; XM_019014249.1.
DR   AlphaFoldDB; G3RME5; -.
DR   Ensembl; ENSGGOT00000027760.2; ENSGGOP00000016959.2; ENSGGOG00000000529.3.
DR   GeneTree; ENSGT00940000158929; -.
DR   HOGENOM; CLU_023268_2_0_1; -.
DR   OrthoDB; 11483at2759; -.
DR   Proteomes; UP000001519; Chromosome 18.
DR   Bgee; ENSGGOG00000000529; Expressed in testis and 5 other cell types or tissues.
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          328..525
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          560..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   670 AA;  75748 MW;  85C78759F88E0112 CRC64;
     MLSNESLHPP AFSRSNSEAS VDSASMEDFW REIESIKDSS MGGQEEPPPA EVTPVDEGEL
     EAEWLQDVGL STLISGDEEE DGKALLSTLT RTQAAAVEKR YNTYTQTMRK KNKQSIRDVR
     DIFGVSESPP RDTCGNHTNQ LDGTKEEREL PRVIKTSGSM PDDASLNSTT LSDASQDKEG
     SFAVPRSDSV AVLETIPVLP VHSNGSPEPG QPVQNAISDD DYLEKNIPPE AEELSFEVSY
     SEMVTEALKR NKLKKSEIKK EDYVLTKFIV QKTRFGLTEA GDLSAEDMKK IRHLSLIELT
     AFFDAFGIQL KRNKTEKVKG RDNGIFGVPL TVLLDSDRKK DPGVKVPLVL QKFFEKVEES
     GLESEGIFRL SGCTAKVKQY REELDAKFNA DKFKWDKMCH REAAVMLKAF FRELPTSLFP
     VEYIPAFISL MERGPHVKVQ FQALHLMVMA LPDANRDAAQ ALMTFFNKVI ANESKNRMSL
     WNISTVMAPN LFFSRSKHSD YEELLLANTA AHIIRLMLKY QKILWKVPSF LITQVRRMNE
     ATMLLKKQLP SVRKLLRRKT LERETASPKT SKVLQKSPSA RRMSDVPEGV IRVHAPLLSK
     VSMAIQLNNQ TKAKDILAKF QYENRILHWQ RAALSFLNGK WVKKEREEST EANRSPKHVF
     LFTIGLDIST
//
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