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Database: UniProt
Entry: D4AD82_RAT
LinkDB: D4AD82_RAT
Original site: D4AD82_RAT 
ID   D4AD82_RAT              Unreviewed;      1513 AA.
AC   D4AD82;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 3.
DT   11-DEC-2019, entry version 87.
DE   SubName: Full=Rho GTPase-activating protein 35 {ECO:0000313|Ensembl:ENSRNOP00000021223};
GN   Name=Arhgap35 {ECO:0000313|Ensembl:ENSRNOP00000021223,
GN   ECO:0000313|RGD:1308738}; Synonyms=Grlf1 {ECO:0000313|RGD:1308738};
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:ENSRNOP00000021223, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000021223, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000021223,
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:ENSRNOP00000021223}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000021223};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {ECO:0000213|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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DR   EMBL; AABR07002647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07002648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; D4AD82; -.
DR   jPOST; D4AD82; -.
DR   PeptideAtlas; D4AD82; -.
DR   PRIDE; D4AD82; -.
DR   Ensembl; ENSRNOT00000021223; ENSRNOP00000021223; ENSRNOG00000015852.
DR   RGD; 1308738; Arhgap35.
DR   eggNOG; KOG4271; Eukaryota.
DR   eggNOG; ENOG410XR4E; LUCA.
DR   GeneTree; ENSGT00950000182819; -.
DR   OMA; WAPGSDG; -.
DR   TreeFam; TF324451; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015852; Expressed in 10 organ(s), highest expression level in brain.
DR   ExpressionAtlas; D4AD82; baseline and differential.
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   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:D4AD82};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN          270..327
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          368..422
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          429..483
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          485..550
FT                   /note="FF"
FT                   /evidence="ECO:0000259|PROSITE:PS51676"
FT   DOMAIN          592..767
FT                   /note="PG1 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51852"
FT   DOMAIN          783..947
FT                   /note="PG2 pseudoGTPase"
FT                   /evidence="ECO:0000259|PROSITE:PS51853"
FT   DOMAIN          1249..1436
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1124..1148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1177..1212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1492..1513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          413..440
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          485..505
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1124..1139
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1182..1196
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1513 AA;  172455 MW;  608B6E680F0F3139 CRC64;
     MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST
     SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA
     AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF
     VSNLYNQLAK TKKPIVIVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF
     STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKSHNE NWLSVSRKMQ
     ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEVDH
     LSCIKAKKLL ETKPEFLKWF VVLEETPWDE TSHIDNMENE RIPFDLMDTV PAEQLYETHL
     EKLRNERKRA EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH
     QKQIIDRAKE 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 SPVLQSQTCK SSHCGSSNSV LLELPIGVHK KRIELSVLSY
     HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAIDVLDNDL
     SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LELFHPFFKD VVEKKNIIEA THMYDNVAEA
     CSTTEEVFNS PRAGSPLCNS NLQDSEEDVE PPSYHLFRED ATLPSLSKDH SKFSMELEGN
     DGLSFIMSNF ESKLNNKVPP PVKPKPPVHF EITKDLSYLD QGHREGQRKS MSSSPWMPQD
     GFDPSDYAEP MDAVVKPRNE EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT
     SSLERGRKVS AVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG
     DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP LTTVVTPEKP
     IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD QDHNLDLAEK DFTVNTVAGA
     MKSFFSELPD PLVPYSMQID LVEAHKINDR EQKLHALKEV LKKFPKENHE VFKYVISHLN
     RVSHNNKVNL MTSENLSICF WPTLMRPDFS SMDALTATRS YQTIIELFIQ QCPFFFYNRP
     ISEPPGAALA PLQPWHPLSP SSPLHLLPVS HHLPSHLLQP LSPQCSHCSP LSSKPNTRCE
     PPQPRKQENQ LSS
//
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