GenomeNet

Database: UniProt
Entry: A0A0G2JWW2_RAT
LinkDB: A0A0G2JWW2_RAT
Original site: A0A0G2JWW2_RAT 
ID   A0A0G2JWW2_RAT          Unreviewed;       708 AA.
AC   A0A0G2JWW2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Rho GTPase activating protein 28 {ECO:0000313|Ensembl:ENSRNOP00000070038.2};
GN   Name=Arhgap28 {ECO:0000313|Ensembl:ENSRNOP00000070038.2,
GN   ECO:0000313|RGD:1559882};
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 {ECO:0000313|Ensembl:ENSRNOP00000070038.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000070038.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070038.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000070038.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070038.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_006245688.1; XM_006245626.3.
DR   AlphaFoldDB; A0A0G2JWW2; -.
DR   Ensembl; ENSRNOT00000090111.2; ENSRNOP00000070038.2; ENSRNOG00000017065.8.
DR   GeneID; 301709; -.
DR   AGR; RGD:1559882; -.
DR   CTD; 79822; -.
DR   RGD; 1559882; Arhgap28.
DR   VEuPathDB; HostDB:ENSRNOG00000017065; -.
DR   GeneTree; ENSGT00940000158929; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000017065; Expressed in skeletal muscle tissue and 17 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2JWW2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:RGD.
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:UP000002494}.
FT   DOMAIN          363..560
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          71..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   708 AA;  80113 MW;  168772FC4A77822A CRC64;
     MVELDPASLR VLSKRFCPAD RKSIPRCRRI NRMLSNESLH PPTFSRSNSQ ASVDSSTSVE
     EFWKEISSIK ESSIGGQEEQ SPTAPTEVKP VDEGELEAEW LQDVGLSTLI SGDEEEDGKA
     LLSTLTRTQA AAVKKRYNTY TQTLRKKNKQ AIRDVRDVFG VSESPPSDSC EHATQLDSTK
     EEKDLPGVTK TSRPLPDDAS LNSTTLSNGA QDEEGGFVAL QSGSVSILEA IPDIPVHTNG
     SADTEQSVQR GLSDDDYLEK NIPPEAEELS FEVSYSEVVT ETPDRNKWKK SDIKKEDYVL
     PKFIVQKTRF GLTETGDLSA EDMKKIRHLS LIELTAFFDA FRIQLKRNKT ERVRGRDNGI
     FGVPLTVLLD NDRKKDPAVK VPLVLQKFFQ KVEESGLESE GIFRLSGCTA KVKQYREELD
     ARFNTDKFKW DKMCHREAAV MLKAFFRELP TSLFPIEYIP AFISLMERGP DIKVQFQALH
     LMVMALPDAN RDTAQALMTF FNKVIANESK NRMSLWNIST VMAPNLFFSR SKHSDCEELL
     VANTAAHIIR LMLTYQKILW KVPSFLITQV RRMNEATMLL KKQLPSMRKL LRRKTLEREV
     SNPKTSKVPQ KSPSSRRMSD VPEGVIRVHA PLLSKVSMAI QLNSQTKAKD ILAKFQYENS
     HASSDRIKMQ NQRLYEVGGN IGQHCLDPDA YILDVYHVNP HAEWVIKP
//
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