ID W5NCI5_LEPOC Unreviewed; 1535 AA.
AC W5NCI5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Rho GTPase-activating protein 35 {ECO:0000256|ARBA:ARBA00040788};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000018344.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000018344.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AHAT01023916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01023917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01023918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006627687.1; XM_006627624.2.
DR RefSeq; XP_015196455.1; XM_015340969.1.
DR RefSeq; XP_015196456.1; XM_015340970.1.
DR Ensembl; ENSLOCT00000018376.1; ENSLOCP00000018344.1; ENSLOCG00000014893.1.
DR GeneID; 102689375; -.
DR KEGG; loc:102689375; -.
DR CTD; 100004299; -.
DR GeneTree; ENSGT00940000154553; -.
DR HOGENOM; CLU_004268_0_0_1; -.
DR OrthoDB; 5405671at2759; -.
DR Proteomes; UP000018468; Linkage group LG2.
DR Bgee; ENSLOCG00000014893; Expressed in camera-type eye and 11 other cell types or tissues.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd22221; pseudoGTPaseD_p190RhoGAP-A; 1.
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; SM00175; RAB; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF81698; FF domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51676; FF; 3.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 369..422
FT /note="FF"
FT /evidence="ECO:0000259|PROSITE:PS51676"
FT DOMAIN 424..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 597..777
FT /note="PG1 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51852"
FT DOMAIN 804..968
FT /note="PG2 pseudoGTPase"
FT /evidence="ECO:0000259|PROSITE:PS51853"
FT DOMAIN 1272..1459
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 775..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1535 AA; 173224 MW; 3240FD5D09511A66 CRC64;
MMMAKKQDVR TPTYNLVVVG LSGTEKEKGQ CGVGKSCLCN RFVRPSADDF YLDHTSVLST
SDFGGRVVNN DHFLFWGEVG RQMEEGPECR MHVVEQTEFI DDQTFQPHRS TALQPYIKRA
AATKLASAEK LMYFCTDQLG LEQDFEQKQM PEGKLQVDGF LLCVDVSRGM NRNFDDQMKF
VTNLYNQLAK TKKPVVLVLT KCDEGVERYI KDAHTFALAK KNLQVVETSA RSNVNVDLAF
LTLVQLIDKS RGKPKIIPYF EALKQQSQQI ASAKDRYEWL VSRIVKNHNE TWPNISRRMQ
NSTEYKDYVY LEGTMKAKKL FQQHIHRLKQ EHIERRRKMY LSTLPQALNT LVPELDDIDH
LSWPGVQQQL RTKRDFSTWF VVLEETPWEE TSHIDNMEDE RIPLDLLDTP AAEQIYENHL
EHLRNERKRA EMRRLFKGSL NTSPFITAGK PWEEARSFIM NEEFYQWLEE PEYLDIYSRH
QKEIIEKAKE DFQELLLEYS ELFYELEVDA KPSKEKMGAI QEVLGEEQRF KALQKLQAER
DALVLKHIHF VYHPTKETCP SGTQCVDSKI EQLLASRFPT RYPFFDSGNQ KSHFGGDSKV
DKINLVILGK DGLARELANE IRGLCTNDDR YVLDGKMYEL SLRPIEGNVR LPVNSFHTAT
FKPHGCLCLY NSKESLSYVM ESIEKVREST LGRKDNHLAH LPMTLILITK RGVGSVGDIG
GETTHSLIAQ GQQVASKLQC GFLEPAAPGM GYGRSVNEKQ INQVLKGLLD SKRNMNLGSS
SPPLHPPPSA RDSHHQQNPE ADMRIVMCVM CGDSYDVEQL LSPFLQPQHC RPSSLPGSGT
SVLLELSVGC QRQSIELLIL SYHSSFSLRK SRLVHGYITV YSAKRKASLE TLCAFLCEVQ
DIIPVQLLAV EDELSDHEIA RDQLAQGEEL AHEIEGRFTS VACGAGGGQH TIDLFQSFFK
EVVEKKTIVE ATHMYDNVAE ACSTNESMHS PRAGSPSPIT TLLDSEDDVE PSPPYTTLRE
DSTLSSSHSG SKLPDTEASD TFSVISEISA FESKLNNKVP PQVRPKPTVS FDFRKVSLTS
YMDPGANRRS LPSAVTWTPG GDGGYDPNDY AEPIDAVAKP RPTDEENIYS VPHDSTQGKI
ITIRNANKAH SNGGGNGSDS EADSSSLERR RKLSSVSIKP RLYRDRSKRL GKFSSFRTSF
SIGSDDELGG PPKLKSEDDG GVLKGDNSII EIEGEDPKRR NILRSLRRPG KKTRPKPRHS
ISKPLESNYF GVPLVTVVSP ERPIPIFIDK CIRYIEATGL STEGIYRVSG NKAEMESMQR
QFDQDHSLDL AEKDFTVNTV AGAMKSFFSE LPEPLVPYSM QLELVEAYKI NEREQRLQAM
KDILRRFPRE NYDVFKYVIC HLNKVSQNNR VNLMTSENLS ICFWPTLMRP DFTTMDALTA
TRTYQTIIET FIHQCAFFFY NQPLVDTPSG LPASPTTLIG ASSYSCYTPV PPPLPSSSSP
GAPQQSPPHS PPPTPQSPLL PLLPPQHVSA EQHTL
//
