ID E7F8G5_DANRE Unreviewed; 1536 AA.
AC E7F8G5; A0A8M1PZQ1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Rho GTPase-activating protein 35 {ECO:0000256|ARBA:ARBA00040788};
GN Name=arhgap35a {ECO:0000313|Ensembl:ENSDARP00000085108,
GN ECO:0000313|ZFIN:ZDB-GENE-120516-2};
GN Synonyms=LOC100004299 {ECO:0000313|RefSeq:XP_001343636.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000085108};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000085108}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000085108};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000085108, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000085108};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_001343636.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_001343636.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR293508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001343636.1; XM_001343600.5.
DR STRING; 7955.ENSDARP00000127935; -.
DR PaxDb; 7955-ENSDARP00000127935; -.
DR Ensembl; ENSDART00000090675.6; ENSDARP00000085108.3; ENSDARG00000062577.7.
DR Ensembl; ENSDART00000154171.3; ENSDARP00000127935.1; ENSDARG00000062577.7.
DR GeneID; 100004299; -.
DR KEGG; dre:100004299; -.
DR AGR; ZFIN:ZDB-GENE-120516-2; -.
DR CTD; 100004299; -.
DR ZFIN; ZDB-GENE-120516-2; arhgap35a.
DR eggNOG; KOG4271; Eukaryota.
DR HOGENOM; CLU_004268_0_0_1; -.
DR OMA; IVMCLLC; -.
DR OrthoDB; 5405671at2759; -.
DR TreeFam; TF324451; -.
DR Reactome; R-DRE-416550; Sema4D mediated inhibition of cell attachment and migration.
DR Reactome; R-DRE-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR Reactome; R-DRE-9013026; RHOB GTPase cycle.
DR Reactome; R-DRE-9013106; RHOC GTPase cycle.
DR Reactome; R-DRE-9013148; CDC42 GTPase cycle.
DR Reactome; R-DRE-9013149; RAC1 GTPase cycle.
DR Reactome; R-DRE-9013404; RAC2 GTPase cycle.
DR Reactome; R-DRE-9013405; RHOD GTPase cycle.
DR Reactome; R-DRE-9013406; RHOQ GTPase cycle.
DR Reactome; R-DRE-9013408; RHOG GTPase cycle.
DR Reactome; R-DRE-9013409; RHOJ GTPase cycle.
DR Reactome; R-DRE-9013423; RAC3 GTPase cycle.
DR Reactome; R-DRE-9696264; RND3 GTPase cycle.
DR Reactome; R-DRE-9696270; RND2 GTPase cycle.
DR Reactome; R-DRE-9696273; RND1 GTPase cycle.
DR PRO; PR:E7F8G5; -.
DR Proteomes; UP000000437; Chromosome 15.
DR Bgee; ENSDARG00000062577; Expressed in cardiac ventricle and 24 other cell types or tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0008361; P:regulation of cell size; IBA:GO_Central.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd00882; Ras_like_GTPase; 1.
DR CDD; cd04373; RhoGAP_p190; 1.
DR Gene3D; 1.10.10.440; FF domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 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; IPR045786; RhoGAP_pG1_pG2.
DR InterPro; IPR039006; RhoGAP_pG2.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR46005; RHO GTPASE-ACTIVATING PROTEIN 190; 1.
DR PANTHER; PTHR46005:SF1; RHO GTPASE-ACTIVATING PROTEIN 35; 1.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16512; RhoGAP-FF1; 1.
DR Pfam; PF19518; RhoGAP_pG1_pG2; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00441; FF; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51676; FF; 2.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|PeptideAtlas:E7F8G5};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 270..327
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 484..550
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 594..775
FT /note="PG1 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51852"
FT DOMAIN 801..971
FT /note="PG2 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51853"
FT DOMAIN 1268..1455
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 987..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1253
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1536 AA; 173556 MW; B2D853FB8B2EA11C CRC64;
MMMAKKQDAR APTYNLVVVG LSGTEKEKGQ CGVGKSCLCN RFVRPSADDF HLDHTSVLST
SDFGGRVVNN DHFLFWGEAV RMLEEGAECR MHVVEQTEFI DDQTFQPHRS TALQPYIKRA
ASTKLASAEK LMYFCTDQLG LEQDFEQKQM PEGKLLVDGF LLCVDVSRGM NRNFDDQMKF
VTNLYNQLAK TKKPVVLVLT KCDEGVERYI KDSHTFALAK KNLQVVESSA RSNVNVDLAF
ITLVQLIDKS RGKPKIIPYF EALKQQSQQI ATAKDRYEWL VSRIVKNHNE TWPNTNRRMQ
TSPEYKDYVF LEGTSKAKKL FQQHVHRLKQ EHIERRRKIY LSTLPQALNS LVPDLDEIDH
LSWSGVQKVL ETKREFSHWF VVLDDTPWET TPHIDNMEDE RIPQDLLETP VAEGIYESHL
EQLHNERKRA EMRWEFKEKL TCSPFVTPGK RWEEARSFIM NEEFYQWLEE QEYIDIYNKY
QKIITDQAKE DFQELLLEYS ELFYELEVDA KPSKEKMGAI QEVLGDEQRF KALQKLQAER
DALVLKHIHF VYHPTKETCP SSPHCVDGKI EQHLALRYPT RYSFDGSSKS QFGEGKVDRI
NLVILGKDGL ARELANEIRA LCTNDERYVL DGRTYELTLR PIEGNVRLPV NSFHTPTFAP
HGCLCLYNSK ESLSYVVDSI EKLRESTIGR RETNLVQLPL SLLLVTKRGV GSISDIGGET
AQTLIQQGQQ VAGRFQCSYL EPASPGVGYG RNINDKHLNQ ILRGLLEMRR PSVSLGSSSP
PLLPSLAGFR DSQQSTEGDL RIVMCLMCGD TYDVDQLLSP FLLPQHCRPL SNLSSGTSVL
LDLSIGGQRL SIDLAILSYH SSFSLRKSRL VHGYIAVYSA KRKASMETLC AFLCEVQDII
PVQLLAVAET QSELADSEAV RDQLAQGEEL AHEIDARFSS VICGPGGVVG GLHRIDHFQP
FFKEVVEKKT IVEATHMYDN VAENVTNENV SSPRCSSPSI TLLDSEDDIE PSPPYPTSRN
DDTLTRGGFK LPDLEGDSYS LISEITNLEN KINNKVPPQV RPKPNVTFDI PKTQNSSLYT
DLALHGSNRR SLPSVTWPEA GYDPSDYAEP MDAVAKPRPT EEENIYSVPH DSTQGKIITI
RNANKSHSNG AGNGSDSEAD SSSLERRRKL SALGVKPRLY RDRSKRLGKF SSFRTSFIGS
DDELGGTPKA KEDELGAQKG DTSLNEEGED PKKRNILRSL GRRTTKKTRP KARQTSLSKP
PESNYFGVPL ANVVTPERPI PLFIEKCIHY IETTGLSTEG IYRVSGNKAE MESMQRQFDQ
DPNIDLVEKD MSVNTVAGAL KSFFSELPDP LVPYSMQVEL VEAFKINDRE HRLHTMKDVL
RRFPRENYDV FKYVITHLNK VSLNSRLNLM TSENLSICFW PTLMRPDFTT MDALTATRTY
QTIIETFIHQ CAFFFYNQPF ADTPSGLPGQ PASPTATLSS GSAYSTSYAS IQPVAPPFSP
AQQSPPHSPP PTPQSPIQSL LPPLHPHHTP TEQHML
//
