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Database: UniProt
Entry: A0A1S3GH54_DIPOR
LinkDB: A0A1S3GH54_DIPOR
Original site: A0A1S3GH54_DIPOR 
ID   A0A1S3GH54_DIPOR        Unreviewed;      1500 AA.
AC   A0A1S3GH54;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   16-OCT-2019, entry version 17.
DE   SubName: Full=rho GTPase-activating protein 35 {ECO:0000313|RefSeq:XP_012888203.1};
GN   Name=Arhgap35 {ECO:0000313|RefSeq:XP_012888203.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha;
OC   Heteromyidae; Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012888203.1};
RN   [1] {ECO:0000313|RefSeq:XP_012888203.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012888203.1};
RG   RefSeq;
RL   Submitted (FEB-2017) to UniProtKB.
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DR   RefSeq; XP_012888203.1; XM_013032749.1.
DR   Ensembl; ENSDORT00000001801; ENSDORP00000001686; ENSDORG00000001800.
DR   GeneID; 105998119; -.
DR   CTD; 2909; -.
DR   OrthoDB; 110157at2759; -.
DR   Proteomes; UP000081671; Genome assembly.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR   GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
DR   GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; IEA:Ensembl.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IEA:Ensembl.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
DR   GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; IEA:Ensembl.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IEA:Ensembl.
DR   GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0044319; P:wound healing, spreading of cells; IEA:Ensembl.
DR   Gene3D; 1.10.10.440; -; 2.
DR   Gene3D; 1.10.555.10; -; 1.
DR   InterPro; IPR002713; FF_domain.
DR   InterPro; IPR036517; FF_domain_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039007; pG1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR032835; RhoGAP-FF1.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR039006; RhoGAP_pG2.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF01846; FF; 1.
DR   Pfam; PF00071; Ras; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF16512; RhoGAP-FF1; 1.
DR   SMART; SM00441; FF; 4.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81698; SSF81698; 1.
DR   PROSITE; PS51676; FF; 4.
DR   PROSITE; PS51852; PG1; 1.
DR   PROSITE; PS51853; PG2; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000081671};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT   DOMAIN      270    327       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      368    422       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      429    483       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      485    550       FF. {ECO:0000259|PROSITE:PS51676}.
FT   DOMAIN      592    767       PG1 pseudoGTPase. {ECO:0000259|PROSITE:
FT                                PS51852}.
FT   DOMAIN      783    947       PG2 pseudoGTPase. {ECO:0000259|PROSITE:
FT                                PS51853}.
FT   DOMAIN     1250   1437       Rho-GAP. {ECO:0000259|PROSITE:PS50238}.
FT   REGION      969    992       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1063   1082       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1125   1147       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1178   1210       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1460   1500       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COILED      413    440       {ECO:0000256|SAM:Coils}.
FT   COILED      485    505       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    969    988       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS   1125   1140       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS   1183   1197       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1467   1487       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1500 AA;  170587 MW;  F8FFA9233F496895 CRC64;
     MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST
     SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA
     AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF
     VSNLYNQLAK TKKPIVVVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF
     STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ
     ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEIDH
     LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE RVPFDLMDTV PAEQLYEAHL
     ERLRNERKRA EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH
     QKQIIDKAKE EFQELLLEYS ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER
     DALILKHIHF VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL
     VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS FQTPTFQPHG
     CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL ILVNKRGDTS GETLHSLIQQ
     GQQIASKLQC VFLDPASAGI GYGRNINEKQ ISQVLKGLLD SKRNLNLVSS TASIKDLADV
     DLRIVMCLMC GDPFSADDIL FPVLQSQTCK SSHCGSNNSV LLELPIGLHK KRIELSVLSY
     HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAVDVLDNDL
     SREQLTEGEE IAQEIDGRFT SLPCSQPQHK LDIFHPFFKD VVEKKNIIEA THMYDNVAEA
     CSTTEEVFNS PRAGSPLCNS NLQDSEEDME PPSYSLFRED TSLPSLSKDH SKLSMELEGN
     DGLSFIMSNF ESKLNNKVPP PVKPKPPVHF EITKGDLSYL DQGHRDGQRK SMSSSPWLPQ
     DGFDPSDYAE PMDAVVKPRN EEENIYSVPH DSTQGKIITI RNINKAQSNG SGNGSDSEMD
     TSSLERGRKV SIVSKPVLYR TRCTRLGRFA SYRTSFSVGS DDELGPIRKK EEDQASQGYK
     GDNTVIPYET DEDPRRRNIL RSLRRNTKKP KPKPRPSITK ATWESNYFGV PLTTVVTPEK
     PIPIFIERCI EYIEATGLST EGIYRVSGNK SEMESLQRQF DQDHNLDLAE KDFTVNTVAG
     AMKSFFSELP DPLVPYSMQI DLVEAHKIND REQKLHALKE VLKKFPKENH EVFKYVISHL
     NKVSHNNKVN LMTSENLSIC FWPTLMRPDF STMDALTATR TYQTIIELFI QQCPFFFYNR
     PISEPPGAVP SSPSAMAATV PFLTSTPVPS QPSPPQSPPP TPQSPLQPLL PSQLQAEHTL
//
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